2.02012-05-31 09:56:16 -06002015-09-13 12:56:05 -0600ECMDB00056M2MDB000019beta-AlanineBeta-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-Carboxyethylamine3-Amino-Propanoate3-Amino-Propanoic acid3-Aminopropanoate3-Aminopropanoic acid3-Aminopropionate3-Aminopropionic acidAbufeneb AlanineB-AlaB-AlanineB-AminopropanoateB-Aminopropanoic acidB-AminopropionateB-Aminopropionic acidBeta AlanineBeta-AlanineBeta-AminopropanoateBeta-Aminopropanoic acidBeta-AminopropionateBeta-Aminopropionic acidOmega-AminopropionateOmega-Aminopropionic acidβ Alanineβ-Alanineβ-Aminopropanoateβ-Aminopropanoic acidβ-Aminopropionateβ-Aminopropionic acidC3H7NO289.093289.0476784733-aminopropanoic acidβ alanine107-95-9NCCC(O)=OInChI=1S/C3H7NO2/c4-2-1-3(5)6/h1-2,4H2,(H,5,6)UCMIRNVEIXFBKS-UHFFFAOYSA-NSolidCytosolExtra-organismPeriplasmlogp-3.26logs0.74solubility4.94e+02 g/lmelting_point200 oClogp-3.2pka_strongest_acidic4.08pka_strongest_basic10.31iupac3-aminopropanoic acidaverage_mass89.0932mono_mass89.047678473smilesNCCC(O)=OformulaC3H7NO2inchiInChI=1S/C3H7NO2/c4-2-1-3(5)6/h1-2,4H2,(H,5,6)inchikeyUCMIRNVEIXFBKS-UHFFFAOYSA-Npolar_surface_area63.32refractivity20.7polarizability8.62rotatable_bond_count2acceptor_count3donor_count2physiological_charge0formal_charge0Pyrimidine 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.PW000942ec00240MetabolicPantothenate and CoA biosynthesisThe 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].PW000828ec00770Metabolicbeta-Alanine metabolismThe 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.PW000896ec00410MetabolicPropanoate 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.PW000940ec00640MetabolicMetabolic pathwayseco01100phosphopantothenate biosynthesis IPANTO-PWYβ-alanine biosynthesis IIIPWY-5155Specdb::CMs301Specdb::CMs302Specdb::CMs303Specdb::CMs304Specdb::CMs305Specdb::CMs896Specdb::CMs957Specdb::CMs1128Specdb::CMs2904Specdb::CMs30065Specdb::CMs30239Specdb::CMs30265Specdb::CMs30266Specdb::CMs30720Specdb::CMs30806Specdb::CMs30973Specdb::CMs30974Specdb::CMs30975Specdb::CMs31735Specdb::CMs31736Specdb::CMs37270Specdb::CMs145902Specdb::CMs1049377Specdb::CMs1049379Specdb::CMs1049381Specdb::EiMs1050Specdb::NmrOneD1058Specdb::NmrOneD1133Specdb::NmrOneD2113Specdb::NmrOneD2806Specdb::NmrOneD166486Specdb::MsMs2679Specdb::MsMs2680Specdb::MsMs2681Specdb::MsMs437109Specdb::MsMs437110Specdb::MsMs437111Specdb::MsMs2245006Specdb::MsMs2245092Specdb::MsMs2251160Specdb::MsMs90Specdb::MsMs91Specdb::MsMs92Specdb::MsMs2682Specdb::MsMs2683Specdb::MsMs2684Specdb::MsMs2685Specdb::MsMs2686Specdb::MsMs2692Specdb::MsMs445546Specdb::MsMs445547Specdb::MsMs445548Specdb::MsMs445549Specdb::MsMs445550Specdb::MsMs448075Specdb::MsMs2230950Specdb::NmrTwoD945Specdb::NmrTwoD1116HMDB00056239234C0009916958B-ALANINEBALbeta-AlanineKeseler, 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-D114.22080510Vijayendran, C., Barsch, A., Friehs, K., Niehaus, K., Becker, A., Flaschel, E. (2008). "Perceiving molecular evolution processes in Escherichia coli by comprehensive metabolite and gene expression profiling." Genome Biol 9:R72.18402659van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). 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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?1358893572Aspartate 1-decarboxylaseP0A790PAND_ECOLIpanDhttp://ecmdb.ca/proteins/P0A790.xml4-aminobutyrate aminotransferaseP22256GABT_ECOLIgabThttp://ecmdb.ca/proteins/P22256.xmlPantothenate synthetaseP31663PANC_ECOLIpanChttp://ecmdb.ca/proteins/P31663.xml4-aminobutyrate aminotransferase_P50457PUUE_ECOLIpuuEhttp://ecmdb.ca/proteins/P50457.xmlGlutamate decarboxylase alphaP69908DCEA_ECOLIgadAhttp://ecmdb.ca/proteins/P69908.xmlGlutamate decarboxylase betaP69910DCEB_ECOLIgadBhttp://ecmdb.ca/proteins/P69910.xmlD-serine/D-alanine/glycine transporterP0AAE0CYCA_ECOLIcycAhttp://ecmdb.ca/proteins/P0AAE0.xmlOuter membrane protein NP77747OMPN_ECOLIompNhttp://ecmdb.ca/proteins/P77747.xmlOuter membrane pore protein EP02932PHOE_ECOLIphoEhttp://ecmdb.ca/proteins/P02932.xmlOuter membrane protein FP02931OMPF_ECOLIompFhttp://ecmdb.ca/proteins/P02931.xmlOuter membrane protein CP06996OMPC_ECOLIompChttp://ecmdb.ca/proteins/P06996.xmlL-Aspartic acid + Hydrogen ion <> beta-Alanine + Carbon dioxideR00489ASPDECARBOX-RXNbeta-Alanine + Adenosine triphosphate + (R)-Pantoate <> Adenosine monophosphate + Hydrogen ion + Pantothenic acid + PyrophosphateR02473PANTOATE-BETA-ALANINE-LIG-RXNL-Aspartic acid <> beta-Alanine + Carbon dioxideR00489beta-Alanine + alpha-Ketoglutarate <> Malonic semialdehyde + L-GlutamateR00908Adenosine triphosphate + (R)-Pantoate + beta-Alanine <> Adenosine monophosphate + Pyrophosphate + Pantothenic acidR02473PANTOATE-BETA-ALANINE-LIG-RXNHydrogen ion + L-Aspartic acid > beta-Alanine + Carbon dioxideASPDECARBOX-RXNbeta-Alanine + (R)-Pantoate + Adenosine triphosphate > Hydrogen ion + Pantothenic acid + Pyrophosphate + Adenosine monophosphatePANTOATE-BETA-ALANINE-LIG-RXNAdenosine triphosphate + (R)-Pantoate + beta-Alanine > Adenosine monophosphate + Pyrophosphate + (R)-pantothenateL-Aspartic acid > beta-Alanine + Carbon dioxideL-Aspartic acid + Hydrogen ion + L-Aspartic acid Carbon dioxide + beta-AlaninePW_R002998L-Aspartic acid + Hydrogen ion + L-Aspartic acid > Carbon dioxide + beta-AlaninePW_R003364beta-Alanine + Adenosine triphosphate + (R)-pantoate + (R)-Pantoate > Adenosine monophosphate + Pyrophosphate + Hydrogen ion + Pantothenic acid + Pantothenic acidPW_R003001beta-Alanine + Adenosine triphosphate > Adenosine monophosphate + Pyrophosphate + Hydrogen ionPW_R003383beta-Alanine + alpha-Ketoglutarate <> Malonic semialdehyde + L-Glutamatebeta-Alanine + Adenosine triphosphate + (R)-Pantoate <> Adenosine monophosphate + Hydrogen ion + Pantothenic acid + PyrophosphateAdenosine triphosphate + (R)-Pantoate + beta-Alanine <> Adenosine monophosphate + PyrophosphateL-Aspartic acid + Hydrogen ion <> beta-Alanine + Carbon dioxidebeta-Alanine + Adenosine triphosphate + (R)-Pantoate <> Adenosine monophosphate + Hydrogen ion + Pantothenic acid + Pyrophosphate48 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 GlucoBioreactor, pH controlled, O2 and CO2 controlled, dilution rate: 0.2/h11.5uM0.037 oCBW25113Stationary Phase, glucose limited460000Ishii, 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