2.0 2012-05-31 10:21:46 -0600 2015-09-13 12:56:06 -0600 ECMDB00142 M2MDB000053 Formic acid Formic acid is the simplest carboxylic acid. Formate is an intermediate in normal metabolism. It takes part in the metabolism of one-carbon compounds and its carbon may appear in methyl groups undergoing transmethylation. It is eventually oxidized to carbon dioxide. In nature, formic acid is found in the stings and bites of many insects of the order Hymenoptera, including bees and ants. The principal use of formic acid is as a preservative and antibacterial agent in livestock feed. When sprayed on fresh hay or other silage, it arrests certain decay processes and causes the feed to retain its nutritive value longer. Add-F Ameisensaure Aminate Aminic acid Bilorin Collo-Bueglatt Collo-Didax Formate Formic acid Formira Formisoton Formylate Formylic acid Hydrogen carboxylate Hydrogen carboxylic acid Methanoate Methanoate monomer Methanoic acid Methanoic acid monomer Myrmicyl Sodium Formate Sodium Formic acid Sybest Wonderbond Hardener M 600L CH2O2 46.0254 46.005479308 formic acid formic acid 64-18-6 OC=O InChI=1S/CH2O2/c2-1-3/h1H,(H,2,3) BDAGIHXWWSANSR-UHFFFAOYSA-N Liquid Cytosol Extra-organism Periplasm logp -0.47 ALOGPS logs 1.02 ALOGPS solubility 4.77e+02 g/l ALOGPS melting_point 8.4 oC logp -0.27 ChemAxon pka_strongest_acidic 4.27 ChemAxon iupac formic acid ChemAxon average_mass 46.0254 ChemAxon mono_mass 46.005479308 ChemAxon smiles OC=O ChemAxon formula CH2O2 ChemAxon inchi InChI=1S/CH2O2/c2-1-3/h1H,(H,2,3) ChemAxon inchikey BDAGIHXWWSANSR-UHFFFAOYSA-N ChemAxon polar_surface_area 37.3 ChemAxon refractivity 8.15 ChemAxon polarizability 3.37 ChemAxon rotatable_bond_count 0 ChemAxon acceptor_count 2 ChemAxon donor_count 1 ChemAxon physiological_charge -1 ChemAxon formal_charge 0 ChemAxon Butanoate metabolism ec00650 Nitrogen metabolism The biological process of the nitrogen cycle is a complex interplay among many microorganisms catalyzing different reactions, where nitrogen is found in various oxidation states ranging from +5 in nitrate to -3 in ammonia. The ability of fixing atmospheric nitrogen by the nitrogenase enzyme complex is present in restricted prokaryotes (diazotrophs). The other reduction pathways are assimilatory nitrate reduction and dissimilatory nitrate reduction both for conversion to ammonia, and denitrification. Denitrification is a respiration in which nitrate or nitrite is reduced as a terminal electron acceptor under low oxygen or anoxic conditions, producing gaseous nitrogen compounds (N2, NO and N2O) to the atmosphere. Nitrate can be introduced into the cytoplasm through a nitrate:nitrite antiporter NarK or a nitrate / nitrite transporter NarU. Nitrate is then reduced by a Nitrate Reductase resulting in the release of water, an acceptor and a Nitrite. Nitrite can also be introduced into the cytoplasm through a nitrate:nitrite antiporter NarK Nitrite can be reduced a NADPH dependent nitrite reductase resulting in water and NAD and Ammonia. Nitrite can interact with hydrogen ion, ferrocytochrome c through a cytochrome c-552 ferricytochrome resulting in the release of ferricytochrome c, water and ammonia Another process by which ammonia is produced is by a reversible reaction of hydroxylamine with a reduced acceptor through a hydroxylamine reductase resulting in an acceptor, water and ammonia. Water and carbon dioxide react through a carbonate dehydratase resulting in carbamic acid. This compound reacts spontaneously with hydrogen ion resulting in the release of carbon dioxide and ammonia. Carbon dioxide can interact with water through a carbonic anhydrase resulting in hydrogen carbonate. This compound interacts with cyanate and hydrogen ion through a cyanate hydratase resulting in a carbamic acid. Ammonia can be metabolized by reacting with L-glutamine and ATP driven glutamine synthetase resulting in ADP, phosphate and L-glutamine. The latter compound reacts with oxoglutaric acid and hydrogen ion through a NADPH dependent glutamate synthase resulting in the release of NADP and L-glutamic acid. L-glutamic acid reacts with water through a NADP-specific glutamate dehydrogenase resulting in the release of oxoglutaric acid, NADPH, hydrogen ion and ammonia. PW000755 ec00910 Metabolic Folate biosynthesis The biosynthesis of folic acid begins with a product of purine nucleotides de novo biosynthesis pathway, GTP. This compound is involved in a reaction with water through a GTP cyclohydrolase 1 protein complex, resulting in a hydrogen ion, formic acid and 7,8-dihydroneopterin 3-triphosphate. The latter compound is dephosphatased through a dihydroneopterin triphosphate pyrophosphohydrolase resulting in the release of a pyrophosphate, hydrogen ion and 7,8-dihydroneopterin 3-phosphate. The latter compound reacts with water spontaneously resulting in the release of a phosphate and a 7,8 -dihydroneopterin. This compound reacts with a dihydroneopterin aldolase, releasing a glycoaldehyde and 6-hydroxymethyl-7,9-dihydropterin. The latter compound is phosphorylated with a ATP-driven 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase resulting in a (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate. Chorismate is metabolized by reacting with L-glutamine through a 4-amino-4-deoxychorismate synthase resulting in L-glutamic acid and 4-amino-4-deoxychorismate. The latter compound then reacts through an aminodeoxychorismate lyase resulting in pyruvic acid,hydrogen ion and p-aminobenzoic acid. (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl diphosphate and p-aminobenzoic acid react through a dihydropteroate synthase resulting in pyrophosphate and 7,8-dihydropteroic acid. This compound reacts with L-glutamic acid through an ATP driven bifunctional folylpolyglutamate synthetase / dihydrofolate synthetase resulting in a 7,8-dihydrofolate monoglutamate. This compound is reduced through an NADPH mediated dihydrofolate reductase resulting in a tetrahydrofate. This product goes on to a one carbon pool by folate pathway. PW000908 ec00790 Metabolic Pyruvate metabolism ec00620 Methane metabolism ec00680 Glyoxylate and dicarboxylate metabolism ec00630 One carbon pool by folate Dihydrofolic acid, a product of the folate biosynthesis pathway, can be metabolized by multiple enzymes. Dihydrofolic acid can be reduced by a NADP-driven dihydrofolate reductase resulting in a NADPH, hydrogen ion and folic acid. Dihydrofolic acid can also be reduced by an NADPH-driven dihydrofolate reductase resulting in a NADP and a tetrahydrofolic acid. Folic acid can also produce a tetrahydrofolic acid through a NADPH-driven dihydrofolate reductase. Dihydrofolic acid also interacts with 5-thymidylic acid through a thymidylate synthase resulting in the release of dUMP and 5,10-methylene-THF Tetrahydrofolic acid can be converted into 5,10-methylene-THF through two different reversible reactions. Tetrahydrofolic acid interacts with a S-Aminomethyldihydrolipoylprotein through a aminomethyltransferase resulting in the release of ammonia, a dihydrolipoylprotein and 5,10-Methylene-THF Tetrahydrofolic acid interacts with L-serine through a glycine hydroxymethyltransferase resulting in a glycine, water and 5,10-Methylene-THF. The compound 5,10-methylene-THF reacts with an NADPH dependent methylenetetrahydrofolate reductase [NAD(P)H] resulting in NADP and 5-Methyltetrahydrofolic acid. This compound interacts with homocysteine through a methionine synthase resulting in L-methionine and tetrahydrofolic acid. Tetrahydrofolic acid can be metabolized into 10-formyltetrahydrofolate through 4 different enzymes: 1.- Tetrahydrofolic acid interacts with FAICAR through a phosphoribosylaminoimidazolecarboxamide formyltransferase resulting in a 1-(5'-Phosphoribosyl)-5-amino-4-imidazolecarboxamide and a 10-formyltetrahydrofolate 2.-Tetrahydrofolic acid interacts with 5'-Phosphoribosyl-N-formylglycinamide through a phosphoribosylglycinamide formyltransferase 2 resulting in a Glycineamideribotide and a 10-formyltetrahydrofolate 3.-Tetrahydrofolic acid interacts with Formic acid through a formyltetrahydrofolate hydrolase resulting in water and a 10-formyltetrahydrofolate 4.-Tetrahydrofolic acid interacts with N-formylmethionyl-tRNA(fMet) through a 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-formyltransferase resulting in a L-methionyl-tRNA(Met) and a 10-formyltetrahydrofolate 10-formyltetrahydrofolate can interact with a hydrogen ion through a bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase resulting in water and 5,10-methenyltetrahydrofolic acid. Tetrahydrofolic acid can be metabolized into 5,10-methenyltetrahydrofolic acid by reacting with a 5'-phosphoribosyl-a-N-formylglycineamidine through a phosphoribosylglycinamide formyltransferase 2 resulting in water, glycineamideribotide and 5,10-methenyltetrahydrofolic acid. The latter compound can either interact with water through an aminomethyltransferase resulting in a N5-Formyl-THF, or it can interact with a NADPH driven bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase resulting in a NADP and 5,10-Methylene THF. PW000773 ec00670 Metabolic Propanoate metabolism Starting from L-threonine, this compound is deaminated through a threonine deaminase resulting in a hydrogen ion, a water molecule and a (2z)-2-aminobut-2-enoate. The latter compound then isomerizes to a 2-iminobutanoate, This compound then reacts spontaneously with hydrogen ion and a water molecule resulting in a ammonium and a 2-Ketobutyric acid. The latter compound interacts with CoA through a pyruvate formate-lyase / 2-ketobutyrate formate-lyase resulting in a formic acid and a propionyl-CoA. Propionyl-CoA can then be processed either into a 2-methylcitric acid or into a propanoyl phosphate. Propionyl-CoA interacts with oxalacetic acid and a water molecule through a 2-methylcitrate synthase resulting in a hydrogen ion, a CoA and a 2-Methylcitric acid.The latter compound is dehydrated through a 2-methylcitrate dehydratase resulting in a water molecule and cis-2-methylaconitate. The latter compound is then dehydrated by a bifunctional aconitate hydratase 2 and 2-methylisocitrate dehydratase resulting in a water molecule and methylisocitric acid. The latter compound is then processed by 2-methylisocitrate lyase resulting in a release of succinic acid and pyruvic acid. Succinic acid can then interact with a propionyl-CoA through a propionyl-CoA:succinate CoA transferase resulting in a propionic acid and a succinyl CoA. Succinyl-CoA is then isomerized through a methylmalonyl-CoA mutase resulting in a methylmalonyl-CoA. This compound is then decarboxylated through a methylmalonyl-CoA decarboxylase resulting in a release of Carbon dioxide and Propionyl-CoA. ropionyl-CoA interacts with a phosphate through a phosphate acetyltransferase / phosphate propionyltransferase resulting in a CoA and a propanoyl phosphate. Propionyl-CoA can react with a phosphate through a phosphate acetyltransferase / phosphate propionyltransferase resulting in a CoA and a propanoyl phosphate. The latter compound is then dephosphorylated through a ADP driven acetate kinase/propionate kinase protein complex resulting in an ATP and Propionic acid. Propionic acid can be processed by a reaction with CoA through a ATP-driven propionyl-CoA synthetase resulting in a pyrophosphate, an AMP and a propionyl-CoA. PW000940 ec00640 Metabolic Thiamine metabolism ec00730 Riboflavin metabolism ec00740 Microbial metabolism in diverse environments ec01120 Two-component system ec02020 Chloroalkane and chloroalkene degradation ec00625 Metabolic pathways eco01100 GTP degradation GTP, produced in the nucleotide de novo biosyntheis pathway, interacts with a water molecule through a GTP cyclohydrolase resulting in a formate, hydrogen ion and a 7,8-dihydroneopterin 3'-triphosphate. The latter compound interacts with a water molecule through a dihydroneopterin triphosphate pyrophosphohydrolase resulting in the release of a pyrophosphate, a hydrogen ion and a 7,8-dihydroneopterin 3'-phosphate. The latter compound interacts with water spontaneously resulting in the release of a phosphate and a 7,8 dihydroneopterin. The latter compound interacts with a dihydroneopterin aldolase resulting in the release of a glycolaldehyde and a 6-hydroxymethyl-7,8-dihydropterin. This compound then is then diphosphorylated by reacting with a ATP driven 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase resulting in the release of a hydrogen ion, an AMP and 6-hydroxymethyl-7,8-dihydropterin diphosphate. GTP interacts with a cyclic pyranopterin monophosphate synthase resulting in the release of a diphosphate and a cyclic pyranopterin phosphate. The latter compound interacts with a thiocarboxylated small subunit of molybdopterin synthase (a protein) and a water molecule through a molybdopterin synthase resulting in the release of 4 hydrogen ions, 2 small subunits of molybdopterin synthase and a molybdopterin. The molybdopterin interacts with an ATP and a hydrogen ion through a molybdopterin adenylyltransferase resulting in the release of a diphosphate and a molybdopterin adenine dinucleotide. PW001888 Metabolic N-oxide electron transfer The pathway can start in various spots. First step in this case starts with NADH interacting with a menaquinone oxidoreductase resulting in the release of a NADH and a hydrogen Ion, at the same time in the inner membrane a menaquinone interacts with 2 electrons and 2 hydrogen ions thus releasing a menaquinol. This allows for 4 hydrogen ions to be transferred from the cytosol to the periplasmic space. The menaquinol then interacts with a trimethylamine N-oxide reductase resulting in the release of 2 hydrogen ion and 2 electrons. At the same time trimethylamine N-oxide and 3 hydrogen ions interact with the enzyme trimethylamine N-oxide reductase resulting in the release of a trimethylamine and a water molecule, this reaction happening in the periplasmic space. The second set of reactions starts with a hydrogen interacting with a menaquinone oxidoreductase resulting in the release of two electrons being released into the inner membrane which then react with with 2 hydrogen ion and a menaquinone to produce a menaquinol. This menaquinol then reacts with a trimethylamine N-oxide reductase following the same steps as mentioned before. The third set of reactions starts with with formate interacting with a formate dehydrogenase-O resulting in a release of carbon dioxide and a hydrogen ion, this releases 2 electrons that interact with a menaquinone and two hydrogen ions. This releases a menaquinol which then reacts with a trimethylamine N-oxide reductase following the same steps as mentioned before PW001889 Metabolic One Carbon Pool by Folate I Dihydrofolic acid, a product of the folate biosynthesis pathway, can be metabolized by multiple enzymes. Dihydrofolic acid can be reduced by a NADP-driven dihydrofolate reductase resulting in a NADPH, hydrogen ion and folic acid. Dihydrofolic acid can also be reduced by an NADPH-driven dihydrofolate reductase resulting in a NADP and a tetrahydrofolic acid. Folic acid can also produce a tetrahydrofolic acid through a NADPH-driven dihydrofolate reductase. Dihydrofolic acid also interacts with 5-thymidylic acid through a thymidylate synthase resulting in the release of dUMP and 5,10-methylene-THF Tetrahydrofolic acid can be converted into 5,10-methylene-THF through two different reversible reactions. Tetrahydrofolic acid interacts with a S-Aminomethyldihydrolipoylprotein through a aminomethyltransferase resulting in the release of ammonia, a dihydrolipoylprotein and 5,10-Methylene-THF Tetrahydrofolic acid interacts with L-serine through a glycine hydroxymethyltransferase resulting in a glycine, water and 5,10-Methylene-THF. The compound 5,10-methylene-THF reacts with an NADPH dependent methylenetetrahydrofolate reductase [NAD(P)H] resulting in NADP and 5-Methyltetrahydrofolic acid. This compound interacts with homocysteine through a methionine synthase resulting in L-methionine and tetrahydrofolic acid. Tetrahydrofolic acid can be metabolized into 10-formyltetrahydrofolate through 4 different enzymes: 1.- Tetrahydrofolic acid interacts with FAICAR through a phosphoribosylaminoimidazolecarboxamide formyltransferase resulting in a 1-(5'-Phosphoribosyl)-5-amino-4-imidazolecarboxamide and a 10-formyltetrahydrofolate 2.-Tetrahydrofolic acid interacts with 5'-Phosphoribosyl-N-formylglycinamide through a phosphoribosylglycinamide formyltransferase 2 resulting in a Glycineamideribotide and a 10-formyltetrahydrofolate 3.-Tetrahydrofolic acid interacts with Formic acid through a formyltetrahydrofolate hydrolase resulting in water and a 10-formyltetrahydrofolate 4.-Tetrahydrofolic acid interacts with N-formylmethionyl-tRNA(fMet) through a 10-formyltetrahydrofolate:L-methionyl-tRNA(fMet) N-formyltransferase resulting in a L-methionyl-tRNA(Met) and a 10-formyltetrahydrofolate 10-formyltetrahydrofolate can interact with a hydrogen ion through a bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase resulting in water and 5,10-methenyltetrahydrofolic acid. Tetrahydrofolic acid can be metabolized into 5,10-methenyltetrahydrofolic acid by reacting with a 5'-phosphoribosyl-a-N-formylglycineamidine through a phosphoribosylglycinamide formyltransferase 2 resulting in water, glycineamideribotide and 5,10-methenyltetrahydrofolic acid. The latter compound can either interact with water through an aminomethyltransferase resulting in a N5-Formyl-THF, or it can interact with a NADPH driven bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase resulting in a NADP and 5,10-Methylene THF. PW001735 Metabolic dimethyl sulfoxide electron transfer The pathway can start in various spots. First step in this case starts with NADH interacting with a menaquinone oxidoreductase resulting in the release of a NADH and a hydrogen Ion, at the same time in the inner membrane a menaquinone interacts with 2 electrons and 2 hydrogen ions thus releasing a menaquinol. This allows for 4 hydrogen ions to be transferred from the cytosol to the periplasmic space. The menaquinol then interacts with a dimethyl sulfoxide reductase resulting in the release of 2 hydrogen ion and 2 electrons. At the same time dimethyl sulfoxide and 2 hydrogen ions interact with the enzyme resulting in the release of a dimethyl sulfide and a water molecule, this reaction happening in the periplasmic space. The second set of reactions starts with a hydrogen interacting with a menaquinone oxidoreductase resulting in the release of two electrons being released into the inner membrane which then react with with 2 hydrogen ion and a menaquinone to produce a menaquinol. This menaquinol then reacts with a trimethylamine N-oxide reductase following the same steps as mentioned before. The third set of reactions starts with with formate interacting with a formate dehydrogenase-O resulting in a release of carbon dioxide and a hydrogen ion, this releases 2 electrons that interact with a menaquinone and two hydrogen ions. This releases a menaquinol which then reacts with a trimethylamine N-oxide reductase following the same steps as mentioned before PW001892 Metabolic preQ0 metabolism PreQ0 or 7-cyano-7-carbaguanine is biosynthesized by degrading GTP. GTP first interacts with water through a GTP cyclohydrolase resulting in the release of a formate, a hydrogen ion and a 7,8-dihydroneopterin 3'-triphosphate. The latter compound then interacts with water through a 6-carboxy-5,6,7,8-tetrahydropterin synthase resulting in a acetaldehyde, triphosphate, 2 hydrogen ion and 6-carboxy-5,6,7,8-tetrahydropterin. The latter compound then reacts spontaneously with a hydrogen ion resulting in the release of a ammonium molecule and a 7-carboxy-7-deazaguanine. This compound then interacts with ATP and ammonium through 7-cyano-7-deazaguanine synthase resulting in the release of water, phosphate, ADP, hydrogen ion and a 7-cyano-7-carbaguanine. The degradation of 7-cyano-7-deazaguanine can lead to produce a preQ1 or a queuine by reacting with 3 hydrogen ions and 2 NADPH through a 7-cyano-7-deazaguanine reductase. PreQ1 then interacts with a guanine 34 in tRNA through a tRNA-guanine transglycosylase resulting in a release of a guanine and a 7-aminomethyl-7-deazaguanosine 34 in tRNA. This nucleic acid then interacts with SAM through a S-adenosylmethionine tRNA ribosyltransferase-isomerase resulting in a release of a hydrogen ion, L-methionine, adenine and an epoxyqueuosine PW001893 Metabolic purine nucleotides de novo biosynthesis The biosynthesis of purine nucleotides is a complex process that begins with a phosphoribosyl pyrophosphate. This compound interacts with water and L-glutamine through a amidophosphoribosyl transferase resulting in a pyrophosphate, L-glutamic acid and a 5-phosphoribosylamine. The latter compound proceeds to interact with a glycine through an ATP driven phosphoribosylamine-glycine ligase resulting in the addition of glycine to the compound. This reaction releases an ADP, a phosphate, a hydrogen ion and a N1-(5-phospho-β-D-ribosyl)glycinamide. The latter compound interacts with formic acid, through an ATP driven phosphoribosylglycinamide formyltransferase 2 resulting in a phosphate, an ADP, a hydrogen ion and a 5-phosphoribosyl-N-formylglycinamide. The latter compound interacts with L-glutamine, and water through an ATP-driven phosphoribosylformylglycinamide synthetase resulting in a release of a phosphate, an ADP, a hydrogen ion, a L-glutamic acid and a 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine. The latter compound interacts with an ATP driven phosphoribosylformylglycinamide cyclo-ligase resulting in a release of ADP, a phosphate, a hydrogen ion and a 5-aminoimidazole ribonucleotide. The latter compound interacts with a hydrogen carbonate through an ATP driven N5-carboxyaminoimidazole ribonucleotide synthetase resulting in a release of a phosphate, an ADP, a hydrogen ion and a N5-carboxyaminoimidazole ribonucleotide.The latter compound then interacts with a N5-carboxyaminoimidazole ribonucleotide mutase resulting in a 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate. This compound interacts with an L-aspartic acid through an ATP driven phosphoribosylaminoimidazole-succinocarboxamide synthase resulting in a phosphate, an ADP, a hydrogen ion and a SAICAR. SAICAR interacts with an adenylosuccinate lyase resulting in a fumaric acid and an AICAR. AICAR interacts with a formyltetrahydrofolate through a AICAR transformylase / IMP cyclohydrolase resulting in a release of a tetrahydropterol mono-l-glutamate and a FAICAR. The latter compound, FAICAR, interacts in a reversible reaction through a AICAR transformylase / IMP cyclohydrolase resulting in a release of water and Inosinic acid. Inosinic acid can be metabolized to produce dGTP and dATP three different methods each. dGTP: Inosinic acid, water and NAD are processed by IMP dehydrogenase resulting in a release of NADH, a hydrogen ion and Xanthylic acid. Xanthylic acid interacts with L-glutamine, and water through an ATP driven GMP synthetase resulting in pyrophosphate, AMP, L-glutamic acid, a hydrogen ion and Guanosine monophosphate. The latter compound is the phosphorylated by reacting with an ATP driven guanylate kinase resulting in a release of ADP and a Gaunosine diphosphate. Guanosine diphosphate can be metabolized in three different ways: 1.-Guanosine diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and a Guanosine triphosphate. This compound interacts with a reduced flavodoxin protein through a ribonucleoside-triphosphate reductase resulting in a oxidized flavodoxin a water moleculer and a dGTP 2.-Guanosine diphosphate interacts with a reduced NrdH glutaredoxin-like proteins through a ribonucleoside-diphosphate reductase 2 resulting in the release of an oxidized NrdH glutaredoxin-like protein, a water molecule and a dGDP. The dGDP is then phosphorylated by interacting with an ATP-driven nucleoside diphosphate kinase resulting in an ADP and dGTP. 3.-Guanosine diphosphate interacts with a reduced thioredoxin ribonucleoside diphosphate reductase 1 resulting in a release of a water molecule, an oxidized thioredoxin and a dGDP. The dGDP is then phosphorylated by interacting with an ATP-driven nucleoside diphosphate kinase resulting in an ADP and dGTP. dATP: Inosinic acid interacts with L-aspartic acid through an GTP driven adenylosuccinate synthase results in the release of GDP, a hydrogen ion, a phosphate and N(6)-(1,2-dicarboxyethyl)AMP. The latter compound is then cleaved by a adenylosuccinate lyase resulting in a fumaric acid and an Adenosine monophosphate. This compound is then phosphorylated by an adenylate kinase resulting in the release of ATP and an adenosine diphosphate. Adenosine diphosphate can be metabolized in three different ways: 1.-Adenosine diphosphate is involved in a reversible reaction by interacting with a hydrogen ion and a phosphate through a ATP synthase / thiamin triphosphate synthase resulting in a hydrogen ion, a water molecule and an Adenosine triphosphate. The adenosine triphosphate interacts with a reduced flavodoxin through a ribonucleoside-triphosphate reductase resulting in an oxidized flavodoxin, a water molecule and a dATP 2.- Adenosine diphosphate interacts with an reduced thioredoxin through a ribonucleoside diphosphate reductase 1 resulting in a release of a water molecule, a oxidized thioredoxin and a dADP. The dADP is then phosphorylated by a nucleoside diphosphate kinase resulting in the release of ADP and a dATP 3.- Adenosine diphosphate interacts with an reduced NrdH glutaredoxin-like protein through a ribonucleoside diphosphate reductase 2 resulting in a release of a water molecule, a oxidized glutaredoxin-like protein and a dADP. The dADP is then phosphorylated by a nucleoside diphosphate kinase resulting in the release of ADP and a dATP PW000910 Metabolic purine nucleotides de novo biosynthesis 1435709748 PW000960 Metabolic Flavin biosynthesis The process of flavin biosynthesis starts with GTP being metabolized by interacting with 3 molecules of water through a GTP cyclohydrolase resulting in a release of formic acid, a pyrophosphate, two hydrog ions and 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one or 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine. Either of these compounds interacts with a water molecule and a hydrogen ion through a fused diaminohydroxyphosphoribosylaminopyrimidine deaminase / 5-amino-6-(5-phosphoribosylamino)uracil reductase resulting in an ammonium and 5-amino-6-(5-phospho-D-ribosylamino)uracil. This compound then interacts with a hydrogen ion through a NADPH dependent fused diaminohydroxyphosphoribosylaminopyrimidine deaminase / 5-amino-6-(5-phosphoribosylamino)uracil reductase resulting in the release of a NADP and a 5-amino-6-(5-phospho-D-ribitylamino)uracil. This compound then interacts with a water molecule through a 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase resulting in a release of a phosphate, and a 5-amino-6-(D-ribitylamino)uracil. D-ribulose 5-phosphate interacts with a3,4-dihydroxy-2-butanone 4-phosphate synthase resulting in the release of formic acid, a hydrogen ion and 1-deoxy-L-glycero-tetrulose 4-phosphate. A 5-amino-6-(D-ribitylamino)uracil and 1-deoxy-L-glycero-tetrulose 4-phosphate interact through a 6,7-dimethyl-8-ribityllumazine synthase resulting in the release of 2 water molecules, a phosphate, a hydrogen ion and a 6,7-dimethyl-8-(1-D-ribityl)lumazine. The latter compound then interacts with a hydrogen ion through a riboflavin synthase resulting in the release of a riboflavin and a 5-amino-6-(d-ribitylamino)uracil. The riboflavin is then phosphorylated through an ATP dependent riboflavin kinase resulting in the release of a ADP, a hydrogen ion and a FLAVIN MONONUCLEOTIDE. The flavin mononucleotide interad with a hydrogen ion and an ATP through the riboflavin kinase resulting in the release of a pyrophosphate and Flavin Adenine dinucleotide. This compound is then exported into the periplasm through a FMN/FAD exporter. PW001971 Metabolic Thiamin diphosphate biosynthesis PW002028 Metabolic polymyxin resistance UDP-glucuronic acid compound undergoes a NAD dependent reaction through a bifunctional polymyxin resistance protein to produce UDP-Beta-L-threo-pentapyranos-4-ulose. This compound then reacts with L-glutamic acid through a UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase to produce an oxoglutaric acid and UDP-4-amino-4-deoxy-beta-L-arabinopyranose The latter compound interacts with a N10-formyl-tetrahydrofolate through a bifunctional polymyxin resistance protein ArnA, resulting in a tetrahydrofolate, a hydrogen ion and a UDP-4-deoxy-4-formamido-beta-L-arabinopyranose, which in turn reacts with a product of the methylerythritol phosphate and polysoprenoid biosynthesis pathway, di-trans,octa-cis-undecaprenyl phosphate to produce a 4-deoxy-4-formamido-alpha-L-arabinopyranosyl ditrans, octacis-undecaprenyl phosphate. The compound 4-deoxy-4-formamido-alpha-L-arabinopyranosyl ditrans, octacis-undecaprenyl phosphate hypothetically reacts with water and results in the release of a formic acid and 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate which in turn reacts with a KDO2-lipid A through a 4-amino-4-deoxy-L-arabinose transferase resulting in the release of a di-trans,octa-cis-undecaprenyl phosphate and a L-Ara4N-modified KDO2-Lipid A PW002052 Metabolic purine nucleotides de novo biosynthesis 2 The biosynthesis of purine nucleotides is a complex process that begins with a phosphoribosyl pyrophosphate. This compound interacts with water and L-glutamine through a amidophosphoribosyl transferase resulting in a pyrophosphate, L-glutamic acid and a 5-phosphoribosylamine. The latter compound proceeds to interact with a glycine through an ATP driven phosphoribosylamine-glycine ligase resulting in the addition of glycine to the compound. This reaction releases an ADP, a phosphate, a hydrogen ion and a N1-(5-phospho-β-D-ribosyl)glycinamide. The latter compound interacts with formic acid, through an ATP driven phosphoribosylglycinamide formyltransferase 2 resulting in a phosphate, an ADP, a hydrogen ion and a 5-phosphoribosyl-N-formylglycinamide. The latter compound interacts with L-glutamine, and water through an ATP-driven phosphoribosylformylglycinamide synthetase resulting in a release of a phosphate, an ADP, a hydrogen ion, a L-glutamic acid and a 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine. The latter compound interacts with an ATP driven phosphoribosylformylglycinamide cyclo-ligase resulting in a release of ADP, a phosphate, a hydrogen ion and a 5-aminoimidazole ribonucleotide. The latter compound interacts with a hydrogen carbonate through an ATP driven N5-carboxyaminoimidazole ribonucleotide synthetase resulting in a release of a phosphate, an ADP, a hydrogen ion and a N5-carboxyaminoimidazole ribonucleotide(5-Phosphoribosyl-5-carboxyaminoimidazole).The latter compound then interacts with a N5-carboxyaminoimidazole ribonucleotide mutase resulting in a 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate. This compound interacts with an L-aspartic acid through an ATP driven phosphoribosylaminoimidazole-succinocarboxamide synthase resulting in a phosphate, an ADP, a hydrogen ion and a SAICAR. SAICAR interacts with an adenylosuccinate lyase resulting in a fumaric acid and an AICAR. AICAR interacts with a formyltetrahydrofolate through a AICAR transformylase / IMP cyclohydrolase resulting in a release of a tetrahydropterol mono-l-glutamate and a FAICAR. The latter compound, FAICAR, interacts in a reversible reaction through a AICAR transformylase / IMP cyclohydrolase resulting in a release of water and Inosinic acid. Inosinic acid can be metabolized to produce dGTP and dATP three different methods each. dGTP: Inosinic acid, water and NAD are processed by IMP dehydrogenase resulting in a release of NADH, a hydrogen ion and Xanthylic acid. Xanthylic acid interacts with L-glutamine, and water through an ATP driven GMP synthetase resulting in pyrophosphate, AMP, L-glutamic acid, a hydrogen ion and Guanosine monophosphate. The latter compound is the phosphorylated by reacting with an ATP driven guanylate kinase resulting in a release of ADP and a Gaunosine diphosphate. Guanosine diphosphate can be metabolized in three different ways: 1.-Guanosine diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and a Guanosine triphosphate. This compound interacts with a reduced flavodoxin protein through a ribonucleoside-triphosphate reductase resulting in a oxidized flavodoxin a water moleculer and a dGTP 2.-Guanosine diphosphate interacts with a reduced NrdH glutaredoxin-like proteins through a ribonucleoside-diphosphate reductase 2 resulting in the release of an oxidized NrdH glutaredoxin-like protein, a water molecule and a dGDP. The dGDP is then phosphorylated by interacting with an ATP-driven nucleoside diphosphate kinase resulting in an ADP and dGTP. 3.-Guanosine diphosphate interacts with a reduced thioredoxin ribonucleoside diphosphate reductase 1 resulting in a release of a water molecule, an oxidized thioredoxin and a dGDP. The dGDP is then phosphorylated by interacting with an ATP-driven nucleoside diphosphate kinase resulting in an ADP and dGTP. dATP: Inosinic acid interacts with L-aspartic acid through an GTP driven adenylosuccinate synthase results in the release of GDP, a hydrogen ion, a phosphate and N(6)-(1,2-dicarboxyethyl)AMP. The latter compound is then cleaved by a adenylosuccinate lyase resulting in a fumaric acid and an Adenosine monophosphate. This compound is then phosphorylated by an adenylate kinase resulting in the release of ATP and an adenosine diphosphate. Adenosine diphosphate can be metabolized in three different ways: 1.-Adenosine diphosphate is involved in a reversible reaction by interacting with a hydrogen ion and a phosphate through a ATP synthase / thiamin triphosphate synthase resulting in a hydrogen ion, a water molecule and an Adenosine triphosphate. The adenosine triphosphate interacts with a reduced flavodoxin through a ribonucleoside-triphosphate reductase resulting in an oxidized flavodoxin, a water molecule and a dATP 2.- Adenosine diphosphate interacts with an reduced thioredoxin through a ribonucleoside diphosphate reductase 1 resulting in a release of a water molecule, a oxidized thioredoxin and a dADP. The dADP is then phosphorylated by a nucleoside diphosphate kinase resulting in the release of ADP and a dATP 3.- Adenosine diphosphate interacts with an reduced NrdH glutaredoxin-like protein through a ribonucleoside diphosphate reductase 2 resulting in a release of a water molecule, a oxidized glutaredoxin-like protein and a dADP. The dADP is then phosphorylated by a nucleoside diphosphate kinase resulting in the release of ADP and a dATP PW002033 Metabolic Tetrahydromonapterin Biosynthesis 5,6,7,8-tetrahydromonapterin is the major tetrahydropterin in E. coli, although the biological role of tetrahydromonapterin in E. coli is currently unknown. It was shown to be a cofactor for the phenylalanine hydroxylase PhhA of Pseudomonas aeruginosa, but no enzyme requiring tetrahydromonapterin as a cofactor has yet been discovered in E. coli. Production of tetrahydromonapterin far exceeds production of folate, indicating that the majority of 7,8-dihydroneopterin 3'-triphosphate, the product of the first committed step of the superpathway of tetrahydrofolate biosynthesis and salvage pathway, is diverted from folate biosynthesis to this pathway. High levels of monapterin are found in the growth medium. PW002043 Metabolic threonine degradation I PWY-5437 mixed acid fermentation FERMENTATION-PWY 6-hydroxymethyl-dihydropterin diphosphate biosynthesis I PWY-6147 formylTHF biosynthesis I 1CMET2-PWY flavin biosynthesis I (bacteria and plants) RIBOSYN2-PWY preQ₀ biosynthesis PWY-6703 respiration (anaerobic) ANARESP1-PWY folate polyglutamylation PWY-2161 superpathway of 5-aminoimidazole ribonucleotide biosynthesis PWY-6277 5-aminoimidazole ribonucleotide biosynthesis II PWY-6122 formaldehyde oxidation II (glutathione-dependent) PWY-1801 polymyxin resistance PWY0-1338 nitrate reduction III (dissimilatory) PWY0-1321 formate to trimethylamine N-oxide electron transfer PWY0-1355 formate to dimethyl sulfoxide electron transfer PWY0-1356 4-amino-2-methyl-5-diphosphomethylpyrimidine biosynthesis PWY-6890 Specdb::CMs 2475 Specdb::CMs 37317 Specdb::CMs 152571 Specdb::CMs 1051446 Specdb::EiMs 1848 Specdb::NmrOneD 1107 Specdb::NmrOneD 1165 Specdb::NmrOneD 3951 Specdb::NmrOneD 4233 Specdb::NmrOneD 4875 Specdb::NmrOneD 4876 Specdb::NmrOneD 142510 Specdb::NmrOneD 142511 Specdb::NmrOneD 142512 Specdb::NmrOneD 142513 Specdb::NmrOneD 142514 Specdb::NmrOneD 142515 Specdb::NmrOneD 142516 Specdb::NmrOneD 142517 Specdb::NmrOneD 142518 Specdb::NmrOneD 142519 Specdb::NmrOneD 142520 Specdb::NmrOneD 142521 Specdb::NmrOneD 142522 Specdb::NmrOneD 142523 Specdb::NmrOneD 142524 Specdb::NmrOneD 142525 Specdb::NmrOneD 142526 Specdb::NmrOneD 142527 Specdb::NmrOneD 142528 Specdb::MsMs 11477 Specdb::MsMs 11478 Specdb::MsMs 11479 Specdb::MsMs 18149 Specdb::MsMs 18150 Specdb::MsMs 18151 Specdb::MsMs 1474060 Specdb::MsMs 1474061 Specdb::MsMs 1474062 Specdb::MsMs 1474063 Specdb::MsMs 1474064 Specdb::MsMs 1474065 Specdb::MsMs 2401142 Specdb::MsMs 2401143 Specdb::MsMs 2401144 Specdb::MsMs 2538101 Specdb::MsMs 2538102 Specdb::MsMs 2538103 Specdb::NmrTwoD 967 Specdb::NmrTwoD 1165 HMDB00142 284 278 C00058 15740 FORMATE FMT Formic acid Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. 21097882 Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114. 22080510 van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25. 17765195 Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948. 18331064 Nicholson JK, Foxall PJ, Spraul M, Farrant RD, Lindon JC: 750 MHz 1H and 1H-13C NMR spectroscopy of human blood plasma. Anal Chem. 1995 Mar 1;67(5):793-811. 7762816 Dunne VG, Bhattachayya S, Besser M, Rae C, Griffin JL: Metabolites from cerebrospinal fluid in aneurysmal subarachnoid haemorrhage correlate with vasospasm and clinical outcome: a pattern-recognition 1H NMR study. NMR Biomed. 2005 Feb;18(1):24-33. 15455468 Bales JR, Higham DP, Howe I, Nicholson JK, Sadler PJ: Use of high-resolution proton nuclear magnetic resonance spectroscopy for rapid multi-component analysis of urine. Clin Chem. 1984 Mar;30(3):426-32. 6321058 Ohmori S, Sumii I, Toyonaga Y, Nakata K, Kawase M: High-performance liquid chromatographic determination of formate as benzimidazole in biological samples. J Chromatogr. 1988 Apr 8;426(1):15-24. 3384868 Dal Pra I, Chiarini A, Boschi A, Freddi G, Armato U: Novel dermo-epidermal equivalents on silk fibroin-based formic acid-crosslinked three-dimensional nonwoven devices with prospective applications in human tissue engineering/regeneration/repair. Int J Mol Med. 2006 Aug;18(2):241-7. 16820930 Igeta Y, Kawarabayashi T, Sato M, Yamada N, Matsubara E, Ishiguro K, Kanai M, Tomidokoro Y, Osuga J, Okamoto K, Hirai S, Shoji M: Apolipoprotein E accumulates with the progression of A beta deposition in transgenic mice. J Neuropathol Exp Neurol. 1997 Nov;56(11):1228-35. 9370233 Kerns W 2nd, Tomaszewski C, McMartin K, Ford M, Brent J: Formate kinetics in methanol poisoning. J Toxicol Clin Toxicol. 2002;40(2):137-43. 12126185 Nagasawa H, Wada M, Koyama S, Kawanami T, Kurita K, Kato T: [A case of methanol intoxication with optic neuropathy visualized on STIR sequence of MR images] Rinsho Shinkeigaku. 2005 Jul;45(7):527-30. 16119839 Foulon V, Sniekers M, Huysmans E, Asselberghs S, Mahieu V, Mannaerts GP, Van Veldhoven PP, Casteels M: Breakdown of 2-hydroxylated straight chain fatty acids via peroxisomal 2-hydroxyphytanoyl-CoA lyase: a revised pathway for the alpha-oxidation of straight chain fatty acids. J Biol Chem. 2005 Mar 18;280(11):9802-12. Epub 2005 Jan 11. 15644336 Iwamoto N, Nishiyama E, Ohwada J, Arai H: Distribution of amyloid deposits in the cerebral white matter of the Alzheimer's disease brain: relationship to blood vessels. Acta Neuropathol (Berl). 1997 Apr;93(4):334-40. 9113198 Ferrari LA, Arado MG, Nardo CA, Giannuzzi L: Post-mortem analysis of formic acid disposition in acute methanol intoxication. Forensic Sci Int. 2003 Apr 23;133(1-2):152-8. 12742704 Tasaka Y, Nakaya F, Matsumoto H, Iwamoto Y, Omori Y: Pancreatic amylin content in human diabetic subjects and its relation to diabetes. Pancreas. 1995 Oct;11(3):303-8. 8577686 D'Andrea MR, Reiser PA, Polkovitch DA, Gumula NA, Branchide B, Hertzog BM, Schmidheiser D, Belkowski S, Gastard MC, Andrade-Gordon P: The use of formic acid to embellish amyloid plaque detection in Alzheimer's disease tissues misguides key observations. Neurosci Lett. 2003 May 15;342(1-2):114-8. 12727331 Berode M, Sethre T, Laubli T, Savolainen H: Urinary methanol and formic acid as indicators of occupational exposure to methyl formate. Int Arch Occup Environ Health. 2000 Aug;73(6):410-4. 11007345 Lehmann P, Kligman AM: In vivo removal of the horny layer with formic acid. Br J Dermatol. 1983 Sep;109(3):313-20. 6615718 Bloomer JC, Clarke SE, Chenery RJ: Determination of P4501A2 activity in human liver microsomes using [3-14C-methyl]caffeine. Xenobiotica. 1995 Sep;25(9):917-27. 8553685 Grady S, Osterloh J: Improved enzymic assay for serum formate with colorimetric endpoint. J Anal Toxicol. 1986 Jan-Feb;10(1):1-5. 3754027 Baumann K, Angerer J: Occupational chronic exposure to organic solvents. VI. Formic acid concentration in blood and urine as an indicator of methanol exposure. Int Arch Occup Environ Health. 1979 Jan 15;42(3-4):241-9. 422265 Ferry DG, Temple WA, McQueen EG: Methanol monitoring. Comparison of urinary methanol concentration with formic acid excretion rate as a measure of occupational exposure. Int Arch Occup Environ Health. 1980;47(2):155-63. 7440001 Finholt, Albert E.; Jacobson, Eugene C. The reduction of carbon dioxide to formic acid with lithium aluminum hydride. Journal of the American Chemical Society (1952), 74 3943-4. http://hmdb.ca/system/metabolites/msds/000/000/098/original/HMDB00142.pdf?1358461501 Formate dehydrogenase H P07658 FDHF_ECOLI fdhF http://ecmdb.ca/proteins/P07658.xml Formate acetyltransferase 1 P09373 PFLB_ECOLI pflB http://ecmdb.ca/proteins/P09373.xml Peptide deformylase P0A6K3 DEF_ECOLI def http://ecmdb.ca/proteins/P0A6K3.xml GTP cyclohydrolase 1 P0A6T5 GCH1_ECOLI folE http://ecmdb.ca/proteins/P0A6T5.xml GTP cyclohydrolase-2 P0A7I7 RIBA_ECOLI ribA http://ecmdb.ca/proteins/P0A7I7.xml 3,4-dihydroxy-2-butanone 4-phosphate synthase P0A7J0 RIBB_ECOLI ribB http://ecmdb.ca/proteins/P0A7J0.xml Pyruvate formate-lyase 1-activating enzyme P0A9N4 PFLA_ECOLI pflA http://ecmdb.ca/proteins/P0A9N4.xml Formate dehydrogenase, nitrate-inducible, iron-sulfur subunit P0AAJ3 FDNH_ECOLI fdnH http://ecmdb.ca/proteins/P0AAJ3.xml Formate dehydrogenase-O iron-sulfur subunit P0AAJ5 FDOH_ECOLI fdoH http://ecmdb.ca/proteins/P0AAJ5.xml Formate hydrogenlyase subunit 2 P0AAK1 HYCB_ECOLI hycB http://ecmdb.ca/proteins/P0AAK1.xml Formate dehydrogenase, nitrate-inducible, cytochrome b556(fdn) subunit P0AEK7 FDNI_ECOLI fdnI http://ecmdb.ca/proteins/P0AEK7.xml Formate dehydrogenase, cytochrome b556(fdo) subunit P0AEL0 FDOI_ECOLI fdoI http://ecmdb.ca/proteins/P0AEL0.xml Formate hydrogenlyase subunit 5 P16431 HYCE_ECOLI hycE http://ecmdb.ca/proteins/P16431.xml Formate hydrogenlyase subunit 6 P16432 HYCF_ECOLI hycF http://ecmdb.ca/proteins/P16432.xml Formate hydrogenlyase subunit 7 P16433 HYCG_ECOLI hycG http://ecmdb.ca/proteins/P16433.xml Formate dehydrogenase, nitrate-inducible, major subunit P24183 FDNG_ECOLI fdnG http://ecmdb.ca/proteins/P24183.xml Formate dehydrogenase-O major subunit P32176 FDOG_ECOLI fdoG http://ecmdb.ca/proteins/P32176.xml Formate acetyltransferase 2 P32674 PFLD_ECOLI pflD http://ecmdb.ca/proteins/P32674.xml Pyruvate formate-lyase 2-activating enzyme P32675 PFLC_ECOLI pflC http://ecmdb.ca/proteins/P32675.xml S-formylglutathione hydrolase yeiG P33018 SFGH2_ECOLI yeiG http://ecmdb.ca/proteins/P33018.xml Phosphoribosylglycinamide formyltransferase 2 P33221 PURT_ECOLI purT http://ecmdb.ca/proteins/P33221.xml Formyltetrahydrofolate deformylase P37051 PURU_ECOLI purU http://ecmdb.ca/proteins/P37051.xml Keto-acid formate acetyltransferase P42632 TDCE_ECOLI tdcE http://ecmdb.ca/proteins/P42632.xml S-formylglutathione hydrolase frmB P51025 SFGH1_ECOLI frmB http://ecmdb.ca/proteins/P51025.xml Formyl-coenzyme A transferase P69902 FCTA_ECOLI frc http://ecmdb.ca/proteins/P69902.xml Putative formate acetyltransferase 3 P75793 PFLF_ECOLI ybiW http://ecmdb.ca/proteins/P75793.xml 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase Q46893 ISPD_ECOLI ispD http://ecmdb.ca/proteins/Q46893.xml Hydrogenase-4 component J P77453 HYFJ_ECOLI hyfJ http://ecmdb.ca/proteins/P77453.xml Hydrogenase-4 component D P77416 HYFD_ECOLI hyfD http://ecmdb.ca/proteins/P77416.xml Hydrogenase-4 component G P77329 HYFG_ECOLI hyfG http://ecmdb.ca/proteins/P77329.xml Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD P76472 ARND_ECOLI arnD http://ecmdb.ca/proteins/P76472.xml Hydrogenase-4 component F P77437 HYFF_ECOLI hyfF http://ecmdb.ca/proteins/P77437.xml Hydrogenase-4 component E P0AEW1 HYFE_ECOLI hyfE http://ecmdb.ca/proteins/P0AEW1.xml Hydrogenase-4 component C P77858 HYFC_ECOLI hyfC http://ecmdb.ca/proteins/P77858.xml Phosphomethylpyrimidine synthase P30136 THIC_ECOLI thiC http://ecmdb.ca/proteins/P30136.xml Hydrogenase-4 component I P77668 HYFI_ECOLI hyfI http://ecmdb.ca/proteins/P77668.xml Hydrogenase-4 component B P23482 HYFB_ECOLI hyfB http://ecmdb.ca/proteins/P23482.xml Autonomous glycyl radical cofactor P68066 GRCA_ECOLI grcA http://ecmdb.ca/proteins/P68066.xml Formate hydrogenlyase subunit 3 P16429 HYCC_ECOLI hycC http://ecmdb.ca/proteins/P16429.xml Hydrogenase-4 component H P77423 HYFH_ECOLI hyfH http://ecmdb.ca/proteins/P77423.xml Hydrogenase-4 component A P23481 HYFA_ECOLI hyfA http://ecmdb.ca/proteins/P23481.xml Formate hydrogenlyase subunit 4 P16430 HYCD_ECOLI hycD http://ecmdb.ca/proteins/P16430.xml Short-chain fatty acids transporter P76460 ATOE_ECOLI atoE http://ecmdb.ca/proteins/P76460.xml Probable formate transporter 2 P77733 FOCB_ECOLI focB http://ecmdb.ca/proteins/P77733.xml Probable formate transporter 1 P0AC23 FOCA_ECOLI focA http://ecmdb.ca/proteins/P0AC23.xml Outer membrane protein N P77747 OMPN_ECOLI ompN http://ecmdb.ca/proteins/P77747.xml Outer membrane pore protein E P02932 PHOE_ECOLI phoE http://ecmdb.ca/proteins/P02932.xml Outer membrane protein F P02931 OMPF_ECOLI ompF http://ecmdb.ca/proteins/P02931.xml Outer membrane protein C P06996 OMPC_ECOLI ompC http://ecmdb.ca/proteins/P06996.xml Coenzyme A + Pyruvic acid <> Acetyl-CoA + Formic acid R00212 PYRUVFORMLY-RXN 2 Hydrogen ion + Menaquinone 8 + Formic acid > Menaquinol 8 + Carbon dioxide + Hydrogen ion 2 Hydrogen ion + Ubiquinone-8 + Formic acid > Ubiquinol-8 + Carbon dioxide + Hydrogen ion Formic acid + Hydrogen ion > Carbon dioxide + Hydrogen (gas) FHLMULTI-RXN S-Formylglutathione + Water <> Formic acid + Glutathione + Hydrogen ion R00527 S-FORMYLGLUTATHIONE-HYDROLASE-RXN N10-Formyl-THF + Water <> Formic acid + Hydrogen ion + Tetrahydrofolic acid R00944 FORMYLTHFDEFORMYL-RXN Guanosine triphosphate + 3 Water <> 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + Formic acid +2 Hydrogen ion + Pyrophosphate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine R00425 GTP-CYCLOHYDRO-II-RXN Adenosine triphosphate + Formic acid + Glycineamideribotide > ADP + 5'-Phosphoribosyl-N-formylglycineamide + Hydrogen ion + Phosphate GARTRANSFORMYL2-RXN Guanosine triphosphate + Water > Dihydroneopterin triphosphate + Formic acid + Hydrogen ion GTP-CYCLOHYDRO-I-RXN Water + Undecaprenyl phosphate-4-amino-4-formyl-L-arabinose > Formic acid + undecaprenyl phosphate-4-amino-4-deoxy-L-arabinose Formyl-CoA + Oxalic acid <> Formic acid + Oxalyl-CoA RXN0-1382 D-Ribulose 5-phosphate <> 3,4-Dihydroxy-2-butanone-4-P + Formic acid + Hydrogen ion R07281 DIOHBUTANONEPSYN-RXN 5-Aminoimidazole ribonucleotide + Water + NAD > 4-Amino-2-methyl-5-phosphomethylpyrimidine +2 Formic acid +3 Hydrogen ion + NADH Acetyl-CoA + Formic acid <> Coenzyme A + Pyruvic acid R00212 Guanosine triphosphate + 3 Water <> Formic acid + 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + Pyrophosphate R00425 Formic acid + NAD <> Hydrogen ion + Carbon dioxide + NADH R00519 S-Formylglutathione + Water <> Formic acid + Glutathione R00527 N10-Formyl-THF + Water <> Formic acid + Tetrahydrofolic acid R00944 Formamidopyrimidine nucleoside triphosphate + Water <> 2,5-Diaminopyrimidine nucleoside triphosphate + Formic acid R05046 2-Ketobutyric acid + Coenzyme A <> Propionyl-CoA + Formic acid R06987 D-Ribulose 5-phosphate <> 3,4-Dihydroxy-2-butanone-4-P + Formic acid R07281 Hydrogen ion + Formic acid > Carbon dioxide + Hydrogen (gas) FHLMULTI-RXN 4-deoxy-4-formamido-&alpha;-L-arabinopyranosyl <i>ditrans,octacis</i>-undecaprenyl phosphate + Water > 4-amino-4-deoxy-&alpha;-L-arabinopyranosyl <i>ditrans,octacis</i>-undecaprenyl phosphate + Formic acid RXN0-5409 Water + formyl-L-methionyl peptide > Hydrogen ion + methionyl peptide + Formic acid 3.5.1.88-RXN D-Ribulose 5-phosphate > Hydrogen ion + 3,4-Dihydroxy-2-butanone-4-P + Formic acid DIOHBUTANONEPSYN-RXN Formic acid + Hydrogen ion + a menaquinone > Hydrogen ion + Carbon dioxide + a menaquinol FORMATEDEHYDROG-RXN Adenosine triphosphate + Formic acid + Tetrahydrofolic acid > ADP + Phosphate + N10-Formyl-THF FORMATETHFLIG-RXN Water + N10-Formyl-THF > Hydrogen ion + Tetrahydrofolic acid + Formic acid FORMYLTHFDEFORMYL-RXN Water + Guanosine triphosphate > Hydrogen ion + Pyrophosphate + 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + Formic acid GTP-CYCLOHYDRO-II-RXN 2-Ketobutyric acid + Coenzyme A > Propionyl-CoA + Formic acid KETOBUTFORMLY-RXN 5-Aminoimidazole ribonucleotide + S-Adenosylmethionine 4-Amino-2-methyl-5-phosphomethylpyrimidine + 5'-Deoxyadenosine + L-Methionine + Formic acid + carbon monoxide + Hydrogen ion PYRIMSYN1-RXN Formyl-CoA + Oxalic acid Formic acid + Oxalyl-CoA RXN0-1382 Formic acid + an oxidized electron acceptor + Hydrogen ion > Carbon dioxide + a reduced electron acceptor RXN0-3281 S-Formylglutathione + Water > Hydrogen ion + Formic acid + Glutathione S-FORMYLGLUTATHIONE-HYDROLASE-RXN 4-deoxy-4-formamido-beta-L-arabinose di-trans,poly-cis-undecaprenyl phosphate + Water > 4-amino-4-deoxy-alpha-L-arabinose di-trans,poly-cis-undecaprenyl phosphate + Formic acid Formyl-L-methionyl peptide + Water > Formic acid + methionyl peptide Formyl-CoA + Oxalic acid > Formic acid + Oxalyl-CoA Formic acid + NAD > Carbon dioxide + NADH Formic acid + acceptor > Carbon dioxide + reduced acceptor Guanosine triphosphate + Water > Formic acid + 2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)-dihydropteridine triphosphate Acetyl-CoA + Formic acid > CoA + Pyruvic acid Formic acid + Adenosine triphosphate + 5'-Phospho-ribosylglycinamide > 5'-Phosphoribosyl-N-formylglycineamide + ADP + Pyrophosphate N10-Formyl-THF + Water > Formic acid + Tetrahydrofolic acid Guanosine triphosphate + 3 Water > Formic acid + 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + Pyrophosphate D-Ribulose 5-phosphate > Formic acid + 1-Deoxy-L-glycero-tetrulose 4-phosphate S-Formylglutathione + Water > Glutathione + Formic acid Propionyl-CoA + Formic acid > CoA + 2-Ketobutyric acid 5-Aminoimidazole ribonucleotide + S-adenosyl-L-methionine > 4-Amino-2-methyl-5-phosphomethylpyrimidine + 5'-Deoxyadenosine + L-Methionine + Formic acid + CO Formic acid + Quinone <> Carbon dioxide + Hydroquinone R09494 Formyl-L-methionyl peptide + Water <> Formic acid + Methionyl peptide R05635 Guanosine triphosphate + Water <> Formic acid + Dihydroneopterin triphosphate R00424 4-Amino-5-hydroxymethyl-2-methylpyrimidine + S-Adenosylmethionine <> 5-Aminoimidazole ribonucleotide + 4-Amino-2-methyl-5-phosphomethylpyrimidine + 5'-Deoxyadenosine + L-Methionine + Formic acid + CO R03472 N1-(5-phospho-β-D-ribosyl)glycinamide + Adenosine triphosphate + Formic acid > 5'-Phosphoribosyl-N-formylglycinamide + Adenosine diphosphate + Phosphate + Hydrogen ion + 5'-Phosphoribosyl-N-formylglycineamide + ADP PW_R003412 Formic acid + Tetrahydrofolic acid + Tetrahydrofolic acid > Water + 10-Formyltetrahydrofolate + N10-Formyl-THF PW_R002548 Guanosine triphosphate + Water > Formic acid + Hydrogen ion + 7,8-dihydroneopterin 3'-triphosphate PW_R003396 2-Ketobutyric acid + Coenzyme A > Formic acid + Propionyl-CoA + Propionyl-CoA PW_R003493 D-Ribulose 5-phosphate > 1-Deoxy-L-glycero-tetrulose 4-phosphate + Formic acid + Hydrogen ion PW_R003846 Formic acid + menaquinone-8 + Electron + Hydrogen ion > Carbon dioxide + Hydrogen ion + Menaquinol 8 PW_RCT000175 Guanosine triphosphate + 3 Water > Formic acid + Pyrophosphate +2 Hydrogen ion + 2,5-Diamino-6-(5'-phosphoribosylamino)-4-pyrimidineone PW_R005542 Guanosine triphosphate + Water > 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + Hydrogen ion + Formic acid + Pyrophosphate PW_R005545 5-Aminoimidazole ribonucleotide + S-adenosyl-L-methionine >3 Hydrogen ion + CO + Formic acid + L-Methionine + 5'-Deoxyadenosine + 4-amino-2-methyl-5-phosphomethylpyrimidine PW_R005931 Formyl-L-methionyl peptide + Water <> Formic acid + Methionyl peptide S-Formylglutathione + Water <> Formic acid + Glutathione + Hydrogen ion Guanosine triphosphate + 3 Water <>2 2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + Formic acid +2 Hydrogen ion + Pyrophosphate +2 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine D-Ribulose 5-phosphate <>3 3,4-Dihydroxy-2-butanone-4-P + Formic acid + Hydrogen ion D-Ribulose 5-phosphate <>3 3,4-Dihydroxy-2-butanone-4-P + Formic acid Formic acid + NAD <> Hydrogen ion + Carbon dioxide + NADH 4 4-Amino-5-hydroxymethyl-2-methylpyrimidine + S-Adenosylmethionine <>5 5-Aminoimidazole ribonucleotide +4 4-Amino-2-methyl-5-phosphomethylpyrimidine +5 5'-Deoxyadenosine + L-Methionine + Formic acid + CO Formyl-L-methionyl peptide + Water <> Formic acid + Methionyl peptide D-Ribulose 5-phosphate <>3 3,4-Dihydroxy-2-butanone-4-P + Formic acid + Hydrogen ion Formic acid + NAD <> Hydrogen ion + Carbon dioxide + NADH Formic acid + NAD <> Hydrogen ion + Carbon dioxide + NADH 4 4-Amino-5-hydroxymethyl-2-methylpyrimidine + S-Adenosylmethionine <>5 5-Aminoimidazole ribonucleotide +4 4-Amino-2-methyl-5-phosphomethylpyrimidine +5 5'-Deoxyadenosine + L-Methionine + Formic acid + CO Luria-Bertani (LB) media Shake flask 184.0 uM true 25.0 37 oC BL21 DE3 Stationary phase cultures (overnight culture) 734000 100000 Lin, Z., Johnson, L. C., Weissbach, H., Brot, N., Lively, M. O., Lowther, W. T. (2007). "Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function." Proc Natl Acad Sci U S A 104:9597-9602. 17535911