2.0 2012-05-31 09:56:16 -0600 2015-09-13 12:56:05 -0600 ECMDB00056 M2MDB000019 beta-Alanine Beta-alanine is the only naturally occurring beta-amino acid. However, it is not used in the biosynthesis of any major proteins or enzymes. It is formed in vivo by the degradation of dihydrouracil and carnosine. It is a component of pantothenic acid (vitamin B5), which itself is a component of coenzyme A. Under normal conditions, beta-alanine is metabolized into acetic acid. 2-Carboxyethylamine 3-Amino-Propanoate 3-Amino-Propanoic acid 3-Aminopropanoate 3-Aminopropanoic acid 3-Aminopropionate 3-Aminopropionic acid Abufene b Alanine B-Ala B-Alanine B-Aminopropanoate B-Aminopropanoic acid B-Aminopropionate B-Aminopropionic acid Beta Alanine Beta-Alanine Beta-Aminopropanoate Beta-Aminopropanoic acid Beta-Aminopropionate Beta-Aminopropionic acid Omega-Aminopropionate Omega-Aminopropionic acid β Alanine β-Alanine β-Aminopropanoate β-Aminopropanoic acid β-Aminopropionate β-Aminopropionic acid C3H7NO2 89.0932 89.047678473 3-aminopropanoic acid β alanine 107-95-9 NCCC(O)=O InChI=1S/C3H7NO2/c4-2-1-3(5)6/h1-2,4H2,(H,5,6) UCMIRNVEIXFBKS-UHFFFAOYSA-N Solid Cytosol Extra-organism Periplasm logp -3.26 ALOGPS logs 0.74 ALOGPS solubility 4.94e+02 g/l ALOGPS melting_point 200 oC logp -3.2 ChemAxon pka_strongest_acidic 4.08 ChemAxon pka_strongest_basic 10.31 ChemAxon iupac 3-aminopropanoic acid ChemAxon average_mass 89.0932 ChemAxon mono_mass 89.047678473 ChemAxon smiles NCCC(O)=O ChemAxon formula C3H7NO2 ChemAxon inchi InChI=1S/C3H7NO2/c4-2-1-3(5)6/h1-2,4H2,(H,5,6) ChemAxon inchikey UCMIRNVEIXFBKS-UHFFFAOYSA-N ChemAxon polar_surface_area 63.32 ChemAxon refractivity 20.7 ChemAxon polarizability 8.62 ChemAxon rotatable_bond_count 2 ChemAxon acceptor_count 3 ChemAxon donor_count 2 ChemAxon physiological_charge 0 ChemAxon formal_charge 0 ChemAxon Pyrimidine metabolism The 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. PW000942 ec00240 Metabolic Pantothenate and CoA biosynthesis The CoA biosynthesis requires compounds from two other pathways: aspartate metabolism and valine biosynthesis. It requires a Beta-Alanine and R-pantoate. The compound (R)-pantoate is generated in two reactions, as shown by the interaction of alpha-ketoisovaleric acid, 5,10 methylene-THF and water through a 3-methyl-2-oxobutanoate hydroxymethyltransferase resulting in a tetrahydrofolic acid and a 2-dehydropantoate. This compound interacts with hydrogen through a NADPH driven acetohydroxy acid isomeroreductase resulting in the release of NADP and R-pantoate. On the other hand L-aspartic acid interacts with a hydrogen ion and gets decarboxylated through an Aspartate 1- decarboxylase resulting in a carbon dioxide and a Beta-alanine. Beta-alanine and R-pantoate interact with an ATP driven pantothenate synthetase resulting in pyrophosphate, AMP, hydrogen ion and pantothenic acid. Pantothenic acid is phosphorylated through a ATP-driven pantothenate kinase resulting in a ADP, a hydrogen ion and D-4'-Phosphopantothenate. This compound interacts with a CTP and a L-cysteine resulting in a fused 4'-phosphopantothenoylcysteine decarboxylase and phosphopantothenoylcysteine synthetase resulting in a hydrogen ion, a pyrophosphate, a CMP and 4-phosphopantothenoylcysteine. The latter compound interacts with a hydrogen ion through a fused 4'-phosphopantothenoylcysteine decarboxylase and phosphopantothenoylcysteine synthetase resulting in a carbon dioxide release and a 4-phosphopantetheine. This compound interacts with an ATP, hydrogen ion and an phosphopantetheine adenylyltransferase resulting in a release of pyrophosphate, and dephospho-CoA. Dephospho-CoA reacts with an ATP driven dephospho-CoA kinase resulting in a ADP , a hydrogen ion and a Coenzyme A. . The latter is converted into (R)-4'-phosphopantothenate is two steps, involving a β-alanine ligase and a kinase. In most organsims the ligase acts before the kinase (EC 6.3.2.1, pantoate—β-alanine ligase (AMP-forming) followed by EC 2.7.1.33, pantothenate kinase, as described in phosphopantothenate biosynthesis I and phosphopantothenate biosynthesis II. However, in archaea the order is reversed, and EC 2.7.1.169, pantoate kinase acts before EC 6.3.2.36, 4-phosphopantoate—β-alanine ligase, as described in phosphopantothenate biosynthesis III. The kinases are feedback inhibited by CoA itself, accounting for the primary regulatory mechanism of CoA biosynthesis. The addition of L-cysteine to (R)-4'-phosphopantothenate, resulting in the formation of R-4'-phosphopantothenoyl-L-cysteine (PPC), is followed by decarboxylation of PPC to 4'-phosphopantetheine. The ultimate reaction is catalyzed by EC 2.7.1.24, dephospho-CoA kinase, which converts 4'-phosphopantetheine to CoA. All enzymes of this pathway are essential for growth. The reactions in the biosynthetic route towards CoA are identical in most organisms, although there are differences in the functionality of the involved enzymes. In plants every step is catalyzed by single monofunctional enzymes, whereas in bacteria and mammals bifunctional enzymes are often employed [Rubio06]. PW000828 ec00770 Metabolic beta-Alanine metabolism The Beta-Alanine Metabolism starts with a product of Aspartate metabolism. Aspartate is decarboxylated by aspartate 1-decarboxylase, releasing carbon dioxide and Beta-alanine. Beta alanine is then metabolized through a pantothenate synthetase resulting in Pantothenic acid undergoes phosphorylation through a ATP driven pantothenate kinase, resulting in D-4-phosphopantothenate. Pantothenate (vitamin B5) is the universal precursor for the synthesis of the 4'-phosphopantetheine moiety of coenzyme A and acyl carrier protein. Only plants and microorganismscan synthesize pantothenate de novo - animals require a dietary supplement. The enzymes of this pathway are therefore considered to be antimicrobial drug targets. PW000896 ec00410 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 Metabolic pathways eco01100 phosphopantothenate biosynthesis I PANTO-PWY &beta;-alanine biosynthesis III PWY-5155 Specdb::CMs 301 Specdb::CMs 302 Specdb::CMs 303 Specdb::CMs 304 Specdb::CMs 305 Specdb::CMs 896 Specdb::CMs 957 Specdb::CMs 1128 Specdb::CMs 2904 Specdb::CMs 30065 Specdb::CMs 30239 Specdb::CMs 30265 Specdb::CMs 30266 Specdb::CMs 30720 Specdb::CMs 30806 Specdb::CMs 30973 Specdb::CMs 30974 Specdb::CMs 30975 Specdb::CMs 31735 Specdb::CMs 31736 Specdb::CMs 37270 Specdb::CMs 145902 Specdb::CMs 1049377 Specdb::CMs 1049379 Specdb::CMs 1049381 Specdb::EiMs 1050 Specdb::NmrOneD 1058 Specdb::NmrOneD 1133 Specdb::NmrOneD 2113 Specdb::NmrOneD 2806 Specdb::NmrOneD 166486 Specdb::MsMs 90 Specdb::MsMs 91 Specdb::MsMs 92 Specdb::MsMs 2679 Specdb::MsMs 2680 Specdb::MsMs 2681 Specdb::MsMs 2682 Specdb::MsMs 2683 Specdb::MsMs 2684 Specdb::MsMs 2685 Specdb::MsMs 2686 Specdb::MsMs 2692 Specdb::MsMs 11999 Specdb::MsMs 12000 Specdb::MsMs 12001 Specdb::MsMs 18671 Specdb::MsMs 18672 Specdb::MsMs 18673 Specdb::MsMs 20624 Specdb::MsMs 20625 Specdb::MsMs 20626 Specdb::MsMs 22175 Specdb::MsMs 22176 Specdb::MsMs 22177 Specdb::MsMs 437109 Specdb::NmrTwoD 945 Specdb::NmrTwoD 1116 HMDB00056 239 234 C00099 16958 B-ALANINE BAL beta-Alanine Keseler, I. 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Journal of the American Chemical Society (1945), 67 92-4. http://hmdb.ca/system/metabolites/msds/000/000/041/original/HMDB00056.pdf?1358893572 Aspartate 1-decarboxylase P0A790 PAND_ECOLI panD http://ecmdb.ca/proteins/P0A790.xml 4-aminobutyrate aminotransferase P22256 GABT_ECOLI gabT http://ecmdb.ca/proteins/P22256.xml Pantothenate synthetase P31663 PANC_ECOLI panC http://ecmdb.ca/proteins/P31663.xml 4-aminobutyrate aminotransferase_ P50457 PUUE_ECOLI puuE http://ecmdb.ca/proteins/P50457.xml Glutamate decarboxylase alpha P69908 DCEA_ECOLI gadA http://ecmdb.ca/proteins/P69908.xml Glutamate decarboxylase beta P69910 DCEB_ECOLI gadB http://ecmdb.ca/proteins/P69910.xml D-serine/D-alanine/glycine transporter P0AAE0 CYCA_ECOLI cycA http://ecmdb.ca/proteins/P0AAE0.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 L-Aspartic acid + Hydrogen ion <> beta-Alanine + Carbon dioxide R00489 ASPDECARBOX-RXN beta-Alanine + Adenosine triphosphate + (R)-Pantoate <> Adenosine monophosphate + Hydrogen ion + Pantothenic acid + Pyrophosphate R02473 PANTOATE-BETA-ALANINE-LIG-RXN L-Aspartic acid <> beta-Alanine + Carbon dioxide R00489 beta-Alanine + alpha-Ketoglutarate <> Malonic semialdehyde + L-Glutamate R00908 Adenosine triphosphate + (R)-Pantoate + beta-Alanine <> Adenosine monophosphate + Pyrophosphate + Pantothenic acid R02473 PANTOATE-BETA-ALANINE-LIG-RXN Hydrogen ion + L-Aspartic acid > beta-Alanine + Carbon dioxide ASPDECARBOX-RXN beta-Alanine + (R)-Pantoate + Adenosine triphosphate > Hydrogen ion + Pantothenic acid + Pyrophosphate + Adenosine monophosphate PANTOATE-BETA-ALANINE-LIG-RXN Adenosine triphosphate + (R)-Pantoate + beta-Alanine > Adenosine monophosphate + Pyrophosphate + (R)-pantothenate L-Aspartic acid > beta-Alanine + Carbon dioxide L-Aspartic acid + Hydrogen ion + L-Aspartic acid Carbon dioxide + beta-Alanine PW_R002998 L-Aspartic acid + Hydrogen ion + L-Aspartic acid > Carbon dioxide + beta-Alanine PW_R003364 beta-Alanine + Adenosine triphosphate + (R)-pantoate + (R)-Pantoate > Adenosine monophosphate + Pyrophosphate + Hydrogen ion + Pantothenic acid + Pantothenic acid PW_R003001 beta-Alanine + Adenosine triphosphate > Adenosine monophosphate + Pyrophosphate + Hydrogen ion PW_R003383 beta-Alanine + alpha-Ketoglutarate <> Malonic semialdehyde + L-Glutamate beta-Alanine + Adenosine triphosphate + (R)-Pantoate <> Adenosine monophosphate + Hydrogen ion + Pantothenic acid + Pyrophosphate Adenosine triphosphate + (R)-Pantoate + beta-Alanine <> Adenosine monophosphate + Pyrophosphate L-Aspartic acid + Hydrogen ion <> beta-Alanine + Carbon dioxide beta-Alanine + Adenosine triphosphate + (R)-Pantoate <> Adenosine monophosphate + Hydrogen ion + Pantothenic acid + Pyrophosphate 48 mM Na2HPO4, 22 mM KH2PO4, 10 mM NaCl, 45 mM (NH4)2SO4, supplemented with 1 mM MgSO4, 1 mg/l thiamine·HCl, 5.6 mg/l CaCl2, 8 mg/l FeCl3, 1 mg/l MnCl2·4H2O, 1.7 mg/l ZnCl2, 0.43 mg/l CuCl2·2H2O, 0.6 mg/l CoCl2·2H2O and 0.6 mg/l Na2MoO4·2H2O. 4 g/L Gluco Bioreactor, pH controlled, O2 and CO2 controlled, dilution rate: 0.2/h 11.5 uM 0.0 37 oC BW25113 Stationary Phase, glucose limited 46000 0 Ishii, N., Nakahigashi, K., Baba, T., Robert, M., Soga, T., Kanai, A., Hirasawa, T., Naba, M., Hirai, K., Hoque, A., Ho, P. Y., Kakazu, Y., Sugawara, K., Igarashi, S., Harada, S., Masuda, T., Sugiyama, N., Togashi, T., Hasegawa, M., Takai, Y., Yugi, K., Arakawa, K., Iwata, N., Toya, Y., Nakayama, Y., Nishioka, T., Shimizu, K., Mori, H., Tomita, M. (2007). "Multiple high-throughput analyses monitor the response of E. coli to perturbations." Science 316:593-597. 17379776