2.02012-05-31 13:49:28 -06002015-09-18 09:21:20 -0600ECMDB01303M2MDB000330ZincZinc is an essential element, necessary for sustaining all life. It is an essential trace element, necessary for plants, animals, and microorganisms. Zinc is found in nearly 100 specific enzymes (other sources say 300), serves as structural ions in transcription factors and is stored and transferred in metallothioneins. It is "typically the second most abundant transition metal in organisms" after iron and it is the only metal which appears in all enzyme classes. (Wikipedia)ZincZinc ionZnZn(II)ZN++ZN+2ZN2+Zn<SUP>++</SUP>Zn<SUP>+2</SUP>Zn65.40963.929146578zinc(2+) ionzinc(2+) ion7440-66-6[Zn]InChI=1S/ZnHCHKCACWOHOZIP-UHFFFAOYSA-NSolidCytosolExtra-organismPeriplasmmelting_point419.5 oClogp0.16pka_strongest_acidic3.09iupaczinc(2+) ionaverage_mass65.409mono_mass63.929146578smiles[Zn]formulaZninchiInChI=1S/ZninchikeyHCHKCACWOHOZIP-UHFFFAOYSA-Npolar_surface_area0refractivity0polarizability1.78rotatable_bond_count0acceptor_count0donor_count0physiological_charge2formal_charge2Pyrimidine metabolismThe metabolism of pyrimidines begins with L-glutamine interacting with water molecule and a hydrogen carbonate through an ATP driven carbamoyl phosphate synthetase resulting in a hydrogen ion, an ADP, a phosphate, an L-glutamic acid and a carbamoyl phosphate. The latter compound interacts with an L-aspartic acid through a aspartate transcarbamylase resulting in a phosphate, a hydrogen ion and a N-carbamoyl-L-aspartate. The latter compound interacts with a hydrogen ion through a dihydroorotase resulting in the release of a water molecule and a 4,5-dihydroorotic acid. This compound interacts with an ubiquinone-1 through a dihydroorotate dehydrogenase, type 2 resulting in a release of an ubiquinol-1 and an orotic acid. The orotic acid then interacts with a phosphoribosyl pyrophosphate through a orotate phosphoribosyltransferase resulting in a pyrophosphate and an orotidylic acid. The latter compound then interacts with a hydrogen ion through an orotidine-5 '-phosphate decarboxylase, resulting in an release of carbon dioxide and an Uridine 5' monophosphate. The Uridine 5' monophosphate process to get phosphorylated by an ATP driven UMP kinase resulting in the release of an ADP and an Uridine 5--diphosphate.
Uridine 5-diphosphate can be metabolized in multiple ways in order to produce a Deoxyuridine triphosphate.
1.-Uridine 5-diphosphate interacts with a reduced thioredoxin through a ribonucleoside diphosphate reductase 1 resulting in the release of a water molecule and an oxidized thioredoxin and an dUDP. The dUDP is then phosphorylated by an ATP through a nucleoside diphosphate kinase resulting in the release of an ADP and a DeoxyUridine triphosphate.
2.-Uridine 5-diphosphate interacts with a reduced NrdH glutaredoxin-like protein through a Ribonucleoside-diphosphate reductase 1 resulting in a release of a water molecule, an oxidized NrdH glutaredoxin-like protein and a dUDP. The dUDP is then phosphorylated by an ATP through a nucleoside diphosphate kinase resulting in the release of an ADP and a DeoxyUridine triphosphate.
3.-Uridine 5-diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and an Uridinetriphosphate. The latter compound interacts with a reduced flavodoxin through ribonucleoside-triphosphate reductase resulting in the release of an oxidized flavodoxin, a water molecule and a Deoxyuridine triphosphate
4.-Uridine 5-diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and an Uridinetriphosphate The uridine triphosphate interacts with a L-glutamine and a water molecule through an ATP driven CTP synthase resulting in an ADP, a phosphate, a hydrogen ion, an L-glutamic acid and a cytidine triphosphate. The cytidine triphosphate interacts with a reduced flavodoxin through a ribonucleoside-triphosphate reductase resulting in the release of a water molecule, an oxidized flavodoxin and a dCTP. The dCTP interacts with a water molecule and a hydrogen ion through a dCTP deaminase resulting in a release of an ammonium molecule and a Deoxyuridine triphosphate.
5.-Uridine 5-diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and an Uridinetriphosphate The uridine triphosphate interacts with a L-glutamine and a water molecule through an ATP driven CTP synthase resulting in an ADP, a phosphate, a hydrogen ion, an L-glutamic acid and a cytidine triphosphate. The cytidine triphosphate then interacts spontaneously with a water molecule resulting in the release of a phosphate, a hydrogen ion and a CDP. The CDP then interacts with a reduced NrdH glutaredoxin-like protein through a ribonucleoside-diphosphate reductase 2 resulting in the release of a water molecule, an oxidized NrdH glutaredoxin-like protein and a dCDP. The dCDP is then phosphorylated through an ATP driven nucleoside diphosphate kinase resulting in an ADP and a dCTP. The dCTP interacts with a water molecule and a hydrogen ion through a dCTP deaminase resulting in a release of an ammonium molecule and a Deoxyuridine triphosphate.
6.-Uridine 5-diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and an Uridinetriphosphate The uridine triphosphate interacts with a L-glutamine and a water molecule through an ATP driven CTP synthase resulting in an ADP, a phosphate, a hydrogen ion, an L-glutamic acid and a cytidine triphosphate. The cytidine triphosphate then interacts spontaneously with a water molecule resulting in the release of a phosphate, a hydrogen ion and a CDP. The CDP interacts with a reduced thioredoxin through a ribonucleoside diphosphate reductase 1 resulting in a release of a water molecule, an oxidized thioredoxin and a dCDP. The dCDP is then phosphorylated through an ATP driven nucleoside diphosphate kinase resulting in an ADP and a dCTP. The dCTP interacts with a water molecule and a hydrogen ion through a dCTP deaminase resulting in a release of an ammonium molecule and a Deoxyuridine triphosphate.
The deoxyuridine triphosphate then interacts with a water molecule through a nucleoside triphosphate pyrophosphohydrolase resulting in a release of a hydrogen ion, a phosphate and a dUMP. The dUMP then interacts with a methenyltetrahydrofolate through a thymidylate synthase resulting in a dihydrofolic acid and a 5-thymidylic acid. Then 5-thymidylic acid is then phosphorylated through a nucleoside diphosphate kinase resulting in the release of an ADP and thymidine 5'-triphosphate.PW000942ec00240MetabolicABC transportersec02010Two-component systemec02020Collection of Reactions without pathwaysPW001891MetabolicPorphyrin metabolismThe metabolism of porphyrin begins with with glutamic acid being processed by an ATP-driven glutamyl-tRNA synthetase by interacting with hydrogen ion and tRNA(Glu), resulting in amo, pyrophosphate and L-glutamyl-tRNA(Glu) Glutamic acid. Glutamic acid can be obtained as a result of L-glutamate metabolism pathway, glutamate / aspartate : H+ symporter GltP, glutamate:sodium symporter or a glutamate / aspartate ABC transporter .
L-glutamyl-tRNA(Glu) Glutamic acid interacts with a NADPH glutamyl-tRNA reductase resulting in a NADP, a tRNA(Glu) and a (S)-4-amino-5-oxopentanoate.
This compound interacts with a glutamate-1-semialdehyde aminotransferase resulting a 5-aminolevulinic acid. This compound interacts with a porphobilinogen synthase resulting in a hydrogen ion, water and porphobilinogen. The latter compound interacts with water resulting in hydroxymethylbilane synthase resulting in ammonium, and hydroxymethylbilane.
Hydroxymethylbilane can either be dehydrated to produce uroporphyrinogen I or interact with a uroporphyrinogen III synthase resulting in a water molecule and a uroporphyrinogen III.
Uroporphyrinogen I interacts with hydrogen ion through a uroporphyrinogen decarboxylase resulting in a carbon dioxide and a coproporphyrinogen I
Uroporphyrinogen III can be metabolized into precorrin by interacting with a S-adenosylmethionine through a siroheme synthase resulting in hydrogen ion, an s-adenosylhomocysteine and a precorrin-1. On the other hand, Uroporphyrinogen III interacts with hydrogen ion through a uroporphyrinogen decarboxylase resulting in a carbon dioxide and a Coproporphyrinogen III.
Precorrin-1 reacts with a S-adenosylmethionine through a siroheme synthase resulting in a S-adenosylhomocysteine and a Precorrin-2. The latter compound is processed by a NAD dependent uroporphyrin III C-methyltransferase [multifunctional] resulting in a NADH and a sirohydrochlorin. This compound then interacts with Fe 2+
uroporphyrin III C-methyltransferase [multifunctional] resulting in a hydrogen ion and a siroheme. The siroheme is then processed in sulfur metabolism pathway.
Uroporphyrinogen III can be processed in anaerobic or aerobic condition.
Anaerobic:
Uroporphyrinogen III interacts with an oxygen molecule, a hydrogen ion through a coproporphyrinogen III oxidase resulting in water, carbon dioxide and protoporphyrinogen IX. The latter compound then interacts with an 3 oxygen molecule through a protoporphyrinogen oxidase resulting in 3 hydrogen peroxide and a Protoporphyrin IX
Aerobic:
Uroporphyrinogen III reacts with S-adenosylmethionine through a coproporphyrinogen III dehydrogenase resulting in carbon dioxide, 5-deoxyadenosine, L-methionine and protoporphyrinogen IX. The latter compound interacts with a meanquinone through a protoporphyrinogen oxidase resulting in protoporphyrin IX.
The protoporphyrin IX interacts with Fe 2+ through a ferrochelatase resulting in a hydrogen ion and a ferroheme b. The ferroheme b can either be incorporated into the oxidative phosphorylation as a cofactor of the enzymes involved in that pathway or it can interact with hydrogen peroxide through a catalase HPII resulting in a heme D. Heme D can then be incorporated into the oxidative phosphyrlation pathway as a cofactor of the enzymes involved in that pathway. Ferroheme b can also interact with water and a farnesyl pyrophosphate through a heme O synthase resulting in a release of pyrophosphate and heme O. Heme O is then incorporated into the Oxidative phosphorylation pathway.
PW000936MetabolicSecondary Metabolites: Ubiquinol biosynthesisThe biosynthesis of ubiquinol starts the interaction of 4-hydroxybenzoic acid interacting with an octaprenyl diphosphate. The former compound comes from the chorismate interacting with a chorismate lyase resulting in the release of a pyruvic acid and a 4-hydroxybenzoic acid. On the other hand, the latter compound, octaprenyl diphosphate is the result of a farnesyl pyrophosphate interacting with an isopentenyl pyrophosphate through an octaprenyl diphosphate synthase resulting in the release of a pyrophosphate and an octaprenyl diphosphate.
The 4-hydroxybenzoic acid interacts with octaprenyl diphosphate through a 4-hydroxybenzoate octaprenyltransferase resulting in the release of a pyrophosphate and a 3-octaprenyl-4-hydroxybenzoate. The latter compound then interacts with a hydrogen ion through a 3-octaprenyl-4-hydroxybenzoate carboxy-lyase resulting in the release of a carbon dioxide and a 2-octaprenylphenol. The latter compound interacts with an oxygen molecule and a hydrogen ion through a NADPH driven 2-octaprenylphenol hydroxylase resulting in a NADP, a water molecule and a 2-octaprenyl-6-hydroxyphenol.
The 2-octaprenyl-6-hydroxyphenol interacts with an S-adenosylmethionine through a bifunctional 3-demethylubiquinone-8 3-O-methyltransferase and 2-octaprenyl-6-hydroxyphenol methylase resulting in the release of a hydrogen ion, an s-adenosylhomocysteine and a 2-methoxy-6-(all-trans-octaprenyl)phenol. The latter compound then interacts with an oxygen molecule and a hydrogen ion through a NADPH driven 2-octaprenyl-6-methoxyphenol hydroxylase resulting in a NADP, a water molecule and a 2-methoxy-6-all trans-octaprenyl-2-methoxy-1,4-benzoquinol.
The latter compound interacts with a S-adenosylmethionine through a bifunctional 2-octaprenyl-6-methoxy-1,4-benzoquinone methylase and S-adenosylmethionine:2-DMK methyltransferase resulting in a s-adenosylhomocysteine, a hydrogen ion and a 6-methoxy-3-methyl-2-all-trans-octaprenyl-1,4-benzoquinol. The 6-methoxy-3-methyl-2-all-trans-octaprenyl-1,4-benzoquinol. interacts with a reduced acceptor, an oxygen molecule through a 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone hydroxylase resulting in the release of a water molecule, an oxidized electron acceptor and a 3-demethylubiquinol-8. The latter compound then interacts with a S-adenosylmethionine through a bifunctional 3-demethylubiquinone-8 3-O-methyltransferase and 2-octaprenyl-6-hydroxyphenol methylase resulting in a hydrogen ion, a S-adenosylhomocysteine and a ubiquinol 8.
PW000981MetabolicSecondary metabolites: isoprenoid biosynthesis (nonmevalonate pathway)The biosynthesis of isoprenoids starts with a D-glyceraldehyde 3-phosphate interacting with a hydrogen ion through a 1-deoxyxylulose-5-phosphate synthase resulting in a carbon dioxide and 1-Deoxy-D-xylulose. The latter compound then interacts with a hydrogen ion through a NADPH driven 1-deoxy-D-xylulose 5-phosphate reductoisomerase resulting in a NADP and a 2-C-methyl-D-erythritol 4-phosphate. The latter compound then interacts with a cytidine triphosphate and a hydrogen ion through a 4-diphosphocytidyl-2C-methyl-D-erythritol synthase resulting in a pyrophosphate and a 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. The latter compound is then phosphorylated through an ATP driven
4-diphosphocytidyl-2-C-methylerythritol kinase resulting in a release of an ADP, a hydrogen ion and a 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. The latter compound then interacts with a
2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase resulting in the release of a 2-C-methyl-D-erythritol-2,4-cyclodiphosphate resulting in the release of a cytidine monophosphate and 2-C-methyl-D-erythritol-2,4-cyclodiphosphate. The latter compound then interacts with a reduced flavodoxin through a
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase resulting in the release of a water molecule, a hydrogen ion, an oxidized flavodoxin and a 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
The compound 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate can interact with an NADPH,a hydrogen ion through a 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase resulting in a NADP, a water molecule and either a Dimethylallylpyrophosphate or a Isopentenyl pyrophosphate. These two last compounds can be are isomers that can be produced through a isopentenyl diphosphate isomerase.and then get incorporated into the methylerythritol phosphate and polyisoprenoid biosynthesis pathwayPW000975MetabolicSecondary metabolites: methylerythritol phosphate and polyisoprenoid biosynthesisThe biosynthesis of isoprenoids starts with a D-glyceraldehyde 3-phosphate interacting with a hydrogen ion through a 1-deoxyxylulose-5-phosphate synthase resulting in a carbon dioxide and 1-Deoxy-D-xylulose. The latter compound then interacts with a hydrogen ion through a NADPH driven 1-deoxy-D-xylulose 5-phosphate reductoisomerase resulting in a NADP and a 2-C-methyl-D-erythritol 4-phosphate. The latter compound then interacts with a cytidine triphosphate and a hydrogen ion through a 4-diphosphocytidyl-2C-methyl-D-erythritol synthase resulting in a pyrophosphate and a 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. The latter compound is then phosphorylated through an ATP driven
4-diphosphocytidyl-2-C-methylerythritol kinase resulting in a release of an ADP, a hydrogen ion and a 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. The latter compound then interacts with a
2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase resulting in the release of a 2-C-methyl-D-erythritol-2,4-cyclodiphosphate resulting in the release of a cytidine monophosphate and 2-C-methyl-D-erythritol-2,4-cyclodiphosphate. The latter compound then interacts with a reduced flavodoxin through a
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase resulting in the release of a water molecule, a hydrogen ion, an oxidized flavodoxin and a 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
The compound 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate can interact with an NADPH,a hydrogen ion through a 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase resulting in a NADP, a water molecule and either a Dimethylallylpyrophosphate or a Isopentenyl pyrophosphate. These two last compounds can be are isomers that can be produced through a isopentenyl diphosphate isomerase.
Dimethylallylpyrophosphate interacts with the isopentenyl pyrophosphate through a geranyl diphosphate synthase / farnesyl diphosphate synthase resulting in a pyrophosphate and a geranyl--PP. The latter compound interacts with a Isopentenyl pyrophosphate through a geranyl diphosphate synthase / farnesyl diphosphate synthase resulting in the release of a pyrophosphate and a farnesyl pyrophosphate. The latter compound interacts with isopentenyl pyrophosphate either through a undecaprenyl diphosphate synthase resulting in a release of a pyrophosphate and a di-trans,octa-cis-undecaprenyl diphosphate or through a octaprenyl diphosphate synthase resulting in a pyrophosphate and an octaprenyl diphosphatePW000958Metabolicinner membrane transportlist of inner membrane transport complexes, transporting compounds from the periplasmic space to the cytosol
This pathway should be updated regularly with the new inner membrae transports addedPW000786MetabolicpreQ0 metabolismPreQ0 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 epoxyqueuosinePW001893Metabolicpurine nucleotides de novo biosynthesisThe 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
PW000910Metabolicpurine nucleotides de novo biosynthesis 1435709748PW000960Metabolicthreonine biosynthesisThe biosynthesis of threonine starts with oxalacetic acid interacting with an L-glutamic acid through an aspartate aminotransferase resulting in a oxoglutaric acid and an L-aspartic acid. The latter compound is then phosphorylated by an ATP driven Aspartate kinase resulting in an a release of an ADP and an L-aspartyl-4-phosphate. This compound interacts with a hydrogen ion through an NADPH driven aspartate semialdehyde dehydrogenase resulting in the release of a phosphate, an NADP and a L-aspartate-semialdehyde.The latter compound interacts with a hydrogen ion through a NADPH driven aspartate kinase / homoserine dehydrogenase resulting in the release of an NADP and a L-homoserine. L-homoserine is phosphorylated through an ATP driven homoserine kinase resulting in the release of an ADP, a hydrogen ion and a O-phosphohomoserine. The latter compound then interacts with a water molecule threonine synthase resulting in the release of a phosphate and an L-threonine. PW000817MetabolicSecondary Metabolites: Ubiquinol biosynthesis 2The biosynthesis of ubiquinol starts the interaction of 4-hydroxybenzoic acid interacting with an octaprenyl diphosphate. The former compound comes from the chorismate interacting with a chorismate lyase resulting in the release of a pyruvic acid and a 4-hydroxybenzoic acid. On the other hand, the latter compound, octaprenyl diphosphate is the result of a farnesyl pyrophosphate interacting with an isopentenyl pyrophosphate through an octaprenyl diphosphate synthase resulting in the release of a pyrophosphate and an octaprenyl diphosphate. The 4-hydroxybenzoic acid interacts with octaprenyl diphosphate through a 4-hydroxybenzoate octaprenyltransferase resulting in the release of a pyrophosphate and a 3-octaprenyl-4-hydroxybenzoate. The latter compound then interacts with a hydrogen ion through a 3-octaprenyl-4-hydroxybenzoate carboxy-lyase resulting in the release of a carbon dioxide and a 2-octaprenylphenol. The latter compound interacts with an oxygen molecule and a hydrogen ion through a NADPH driven 2-octaprenylphenol hydroxylase resulting in a NADP, a water molecule and a 2-octaprenyl-6-hydroxyphenol. The 2-octaprenyl-6-hydroxyphenol interacts with an S-adenosylmethionine through a bifunctional 3-demethylubiquinone-8 3-O-methyltransferase and 2-octaprenyl-6-hydroxyphenol methylase resulting in the release of a hydrogen ion, an s-adenosylhomocysteine and a 2-methoxy-6-(all-trans-octaprenyl)phenol. The latter compound then interacts with an oxygen molecule and a hydrogen ion through a NADPH driven 2-octaprenyl-6-methoxyphenol hydroxylase resulting in a NADP, a water molecule and a 2-methoxy-6-all trans-octaprenyl-2-methoxy-1,4-benzoquinol. The latter compound interacts with a S-adenosylmethionine through a bifunctional 2-octaprenyl-6-methoxy-1,4-benzoquinone methylase and S-adenosylmethionine:2-DMK methyltransferase resulting in a s-adenosylhomocysteine, a hydrogen ion and a 6-methoxy-3-methyl-2-all-trans-octaprenyl-1,4-benzoquinol. The 6-methoxy-3-methyl-2-all-trans-octaprenyl-1,4-benzoquinol. interacts with a reduced acceptor, an oxygen molecule through a 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone hydroxylase resulting in the release of a water molecule, an oxidized electron acceptor and a 3-demethylubiquinol-8. The latter compound then interacts with a S-adenosylmethionine through a bifunctional 3-demethylubiquinone-8 3-O-methyltransferase and 2-octaprenyl-6-hydroxyphenol methylase resulting in a hydrogen ion, a S-adenosylhomocysteine and a ubiquinol 8.PW002036MetabolicSpecdb::MsMs27887Specdb::MsMs27888Specdb::MsMs27889Specdb::MsMs34445Specdb::MsMs34446Specdb::MsMs34447HMDB013032399429723C0003830185ZN+2ZN2ZincKeseler, 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-D590.21097882Kanehisa, 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-D114.22080510Rakicioglu N, Samur G, Topcu A, Topcu AA: The effect of Ramadan on maternal nutrition and composition of breast milk. Pediatr Int. 2006 Jun;48(3):278-83.16732795Cominetti C, Garrido AB Jr, Cozzolino SM: Zinc nutritional status of morbidly obese patients before and after Roux-en-Y gastric bypass: a preliminary report. Obes Surg. 2006 Apr;16(4):448-53.16608609Religa D, Strozyk D, Cherny RA, Volitakis I, Haroutunian V, Winblad B, Naslund J, Bush AI: Elevated cortical zinc in Alzheimer disease. Neurology. 2006 Jul 11;67(1):69-75.16832080Batista MN, Cuppari L, de Fatima Campos Pedrosa L, Almeida MG, de Almeida JB, de Medeiros AC, Canziani ME: Effect of end-stage renal disease and diabetes on zinc and copper status. Biol Trace Elem Res. 2006 Jul;112(1):1-12.16943612Scheplyagina LA: Impact of the mother's zinc deficiency on the woman's and newborn's health status. J Trace Elem Med Biol. 2005;19(1):29-35.16240669Mocchegiani E, Costarelli L, Giacconi R, Cipriano C, Muti E, Rink L, Malavolta M: Zinc homeostasis in aging: two elusive faces of the same "metal". Rejuvenation Res. 2006 Summer;9(2):351-4.16706668de Sena KC, Arrais RF, das Gracas Almeida M, de Araujo DM, dos Santos MM, de Lima VT, de Fatima Campos Pedrosa L: Effects of zinc supplementation in patients with type 1 diabetes. Biol Trace Elem Res. 2005 Summer;105(1-3):1-9.16034148Tsuruoka S, Wakaumi M, Ioka T, Yamamoto H, Ando H, Sugimoto K, Fujimura A: Angiotensin II receptor blocker-induces blunted taste sensitivity: comparison of candesartan and valsartan. Br J Clin Pharmacol. 2005 Aug;60(2):204-7.16042674Arnold LE, DiSilvestro RA: Zinc in attention-deficit/hyperactivity disorder. J Child Adolesc Psychopharmacol. 2005 Aug;15(4):619-27.16190793An WL, Pei JJ, Nishimura T, Winblad B, Cowburn RF: Zinc-induced anti-apoptotic effects in SH-SY5Y neuroblastoma cells via the extracellular signal-regulated kinase 1/2. Brain Res Mol Brain Res. 2005 Apr 27;135(1-2):40-7. Epub 2005 Jan 8.15857667Shea-Budgell M, Dojka M, Nimmo M, Lee D, Xu Z: Marginal zinc deficiency increased the susceptibility to acute lipopolysaccharide-induced liver injury in rats. Exp Biol Med (Maywood). 2006 May;231(5):553-8.16636303Cutinha D, Vaja S, Treacher D, Swaminathan R: Erythrocyte zinc content in critically ill patients. Clin Chem Lab Med. 2005;43(9):930-3.16176172Santarelli L, Di Lorenzo L, Valentino M, Bracci M, Rapisarda V, Cassano F, Elia G, Martino MG, Neri G, Apostoli P, Soleo L: [Reduced thymulin production during occupational exposure to lead] G Ital Med Lav Ergon. 2005 Jan-Mar;27 Suppl 1:68-72.15915658Kaczmarek A, Robak-Cholubek D, Sowa I, Jakiel G: Comparison of the levels of copper, zinc and iron in cervical mucus and in blood serum of women of childbearing age. Ann Univ Mariae Curie Sklodowska [Med]. 2004;59(1):72-5.16145958Kouremenou-Dona E, Dona A, Papoutsis J, Spiliopoulou C: Copper and zinc concentrations in serum of healthy Greek adults. Sci Total Environ. 2006 Apr 15;359(1-3):76-81. Epub 2005 Jun 13.15955548Mankad M, Sathawara NG, Doshi H, Saiyed HN, Kumar S: Seminal plasma zinc concentration and alpha-glucosidase activity with respect to semen quality. Biol Trace Elem Res. 2006 May;110(2):97-106.16757839Ishikawa Y, Kudo H, Kagawa Y, Sakamoto S: Increased plasma levels of zinc in obese adult females on a weight-loss program based on a hypocaloric balanced diet. In Vivo. 2005 Nov-Dec;19(6):1035-7.16277018Skarupskiene I, Kuzminskis V, Abdrachmanovas O, Ryselis S, Smalinskiene A: [Zinc and aluminum concentrations in blood of hemodialysis patients and its impact on the frequency of infections] Medicina (Kaunas). 2005;41 Suppl 1:65-8.15901979Lukaski HC: Low dietary zinc decreases erythrocyte carbonic anhydrase activities and impairs cardiorespiratory function in men during exercise. Am J Clin Nutr. 2005 May;81(5):1045-51.15883427Gupta SK, Singh SP, Shukla VK: Copper, zinc, and Cu/Zn ratio in carcinoma of the gallbladder. J Surg Oncol. 2005 Sep 1;91(3):204-8.16118778http://hmdb.ca/system/metabolites/msds/000/001/165/original/Zinc_Metal_MSDS.pdf?1368653943Lead, cadmium, zinc and mercury-transporting ATPaseP37617ATZN_ECOLIzntAhttp://ecmdb.ca/proteins/P37617.xmlZinc import ATP-binding protein ZnuCP0A9X1ZNUC_ECOLIznuChttp://ecmdb.ca/proteins/P0A9X1.xmlHigh-affinity zinc uptake system membrane protein znuBP39832ZNUB_ECOLIznuBhttp://ecmdb.ca/proteins/P39832.xmlHigh-affinity zinc uptake system protein znuAP39172ZNUA_ECOLIznuAhttp://ecmdb.ca/proteins/P39172.xmlZinc transporter zupTB1XG45ZUPT_ECODHzupThttp://ecmdb.ca/proteins/B1XG45.xmlZinc transporter zupTC4ZQV8ZUPT_ECOBWzupThttp://ecmdb.ca/proteins/C4ZQV8.xmlZinc transporter zupTP0A8H3ZUPT_ECOLIzupThttp://ecmdb.ca/proteins/P0A8H3.xmlZinc transporter zitBP75757ZITB_ECOLIzitBhttp://ecmdb.ca/proteins/P75757.xmlZinc import ATP-binding protein ZnuCP0A9X1ZNUC_ECOLIznuChttp://ecmdb.ca/proteins/P0A9X1.xmlOuter membrane protein NP77747OMPN_ECOLIompNhttp://ecmdb.ca/proteins/P77747.xmlFerrous-iron efflux pump fieFP69380FIEF_ECOLIfieFhttp://ecmdb.ca/proteins/P69380.xmlOuter membrane pore protein EP02932PHOE_ECOLIphoEhttp://ecmdb.ca/proteins/P02932.xmlHigh-affinity zinc uptake system membrane protein znuBP39832ZNUB_ECOLIznuBhttp://ecmdb.ca/proteins/P39832.xmlOuter membrane protein FP02931OMPF_ECOLIompFhttp://ecmdb.ca/proteins/P02931.xmlHigh-affinity zinc uptake system protein znuAP39172ZNUA_ECOLIznuAhttp://ecmdb.ca/proteins/P39172.xmlOuter membrane protein CP06996OMPC_ECOLIompChttp://ecmdb.ca/proteins/P06996.xmlAdenosine triphosphate + Water + Zinc > ADP + Hydrogen ion + Phosphate + ZincABC-63-RXNAdenosine triphosphate + Water + Zinc > ADP + Hydrogen ion + Phosphate + ZincABC-63-RXNZinc + Adenosine triphosphate + Water > ADP + Phosphate + Hydrogen ionPW_RCT0001824000.0uM0.0K-121600000001. Cybercell Database: <a href='http://ccdb.wishartlab.com/CCDB/cgi-bin/STAT_NEW.cgi'>http://ccdb.wishartlab.com/CCDB/cgi-bin/STAT_NEW.cgi</a> <br>
2. Phillips R., Kondev, J., Theriot, J. (2008) “Physical Biology of the Cell” Garland Science, New York, NY.