2.0 2012-05-31 13:01:47 -0600 2015-09-13 12:56:09 -0600 ECMDB00883 M2MDB000196 L-Valine Valine is an alpha-amino acid with the chemical formula HO2CCH(NH2)CH(CH3)2. L-Valine is one of 20 proteinogenic amino acids. Its codons are GUU, GUC, GUA, and GUG. This amino acid is classified as nonpolar. Along with leucine and isoleucine, valine is a branched-chain amino acid. It is named after the plant valerian. (Wikipedia) (2S)-2-Amino-3-methylbutanoate (2S)-2-Amino-3-methylbutanoic acid (S)-2-amino-3-methyl-Butanoate (S)-2-amino-3-methyl-Butanoic acid (S)-2-Amino-3-methylbutanoate (S)-2-Amino-3-methylbutanoic acid (S)-2-Amino-3-methylbutyrate (S)-2-Amino-3-methylbutyric acid (S)-a-Amino-b-methylbutyrate (S)-a-Amino-b-methylbutyric acid (S)-alpha-Amino-beta-methylbutyrate (S)-alpha-Amino-beta-methylbutyric acid (S)-Valine (S)-α-amino-β-Methylbutyrate (S)-α-amino-β-Methylbutyric acid 2-Amino-3-methylbutanoate 2-Amino-3-methylbutanoic acid 2-Amino-3-methylbutyrate 2-Amino-3-methylbutyric acid L-(+)-a-Aminoisovalerate L-(+)-a-Aminoisovaleric acid L-(+)-alpha-Aminoisovalerate L-(+)-alpha-Aminoisovaleric acid L-(+)-α-Aminoisovalerate L-(+)-α-Aminoisovaleric acid L-a-Amino-b-methylbutyrate L-a-Amino-b-methylbutyric acid L-alpha-Amino-beta-methylbutyrate L-alpha-Amino-beta-methylbutyric acid L-Valine L-α-amino-β-Methylbutyrate L-α-amino-β-Methylbutyric acid V Val Valine C5H11NO2 117.1463 117.078978601 (2S)-2-amino-3-methylbutanoic acid L-valine 72-18-4 CC(C)[C@H](N)C(O)=O InChI=1S/C5H11NO2/c1-3(2)4(6)5(7)8/h3-4H,6H2,1-2H3,(H,7,8)/t4-/m0/s1 KZSNJWFQEVHDMF-BYPYZUCNSA-N Solid Cytosol Extra-organism Periplasm logp -2.29 ALOGPS logs 0.26 ALOGPS solubility 2.14e+02 g/l ALOGPS melting_point 295-300 oC logp -2 ChemAxon pka_strongest_acidic 2.72 ChemAxon pka_strongest_basic 9.6 ChemAxon iupac (2S)-2-amino-3-methylbutanoic acid ChemAxon average_mass 117.1463 ChemAxon mono_mass 117.078978601 ChemAxon smiles CC(C)[C@H](N)C(O)=O ChemAxon formula C5H11NO2 ChemAxon inchi InChI=1S/C5H11NO2/c1-3(2)4(6)5(7)8/h3-4H,6H2,1-2H3,(H,7,8)/t4-/m0/s1 ChemAxon inchikey KZSNJWFQEVHDMF-BYPYZUCNSA-N ChemAxon polar_surface_area 63.32 ChemAxon refractivity 29.49 ChemAxon polarizability 12.19 ChemAxon rotatable_bond_count 2 ChemAxon acceptor_count 3 ChemAxon donor_count 2 ChemAxon physiological_charge 0 ChemAxon formal_charge 0 ChemAxon Alanine, aspartate and glutamate metabolism ec00250 Valine, leucine and isoleucine biosynthesis ec00290 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 Aminoacyl-tRNA biosynthesis ec00970 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 Valine, leucine and isoleucine degradation ec00280 ABC transporters ec02010 Metabolic pathways eco01100 L-alanine metabolism L-alanine is an essential component of proteins and peptidoglycan. The latter also contains about three molecules of D-alanine for every L-alanine. Only about 10 percent of the total alanine synthesized flows into peptidoglycan. There are at least 3 ways to begin the biosynthesis of alanine. The first method for alanine biosynthesis begins with L-cysteine produced from L-cysteine biosynthesis pathway. L-cysteine reacts with an [L-cysteine desulfurase] L-cysteine persulfide through a cysteine desulfurase resulting in a release of [L-cysteine desulfurase] l-cysteine persulfide and L-alanine. The second method starts with pyruvic acid reacting with L-glutamic acid through a glutamate-pyruvate aminotransferase resulting in a oxoglutaric acid and L-alanine. The third method starts with L-glutamic acid interacting with Alpha-ketoisovaleric acid through a valine transaminase resulting in an oxoglutaric acid and L-valine. L-valine reacts with pyruvic acid through a valine-pyruvate aminotransferase resulting Alpha-ketoisovaleric acid and L-alanine. This first step of the pathway, which can be catalyzed by either of two racemases( biosynthetic or catabolic), also serves an essential role in biosynthesis because its product, D-alanine, is an essential component of cell wall peptidoglycan (murein). D-alanine is metabolized by an ATP driven D-alanine ligase A and B resulting in D-alanyl-D-alanine. This product is incorporated into the peptidoglycan biosynthesis. L-alanine is metabolized with alanine racemase, either catabolic or metabolic resulting in a D-alanine. This compound reacts with water and a quinone through a D-amino acid dehydrogenase resulting in Pyruvic acid, hydroquinone and ammonium, thus entering the central metabolism and thereby can serve as a total source of carbon and energy. This pathway is unique among those through which L-amino acids are degraded, in that the L form must first be converted to the D form. D-alanine, is an essential component of cell wall peptidoglycan (murein). The role of the alr racemase is predominately biosynthetic: it is produced constitutively in small amounts. The role of the dadX racemase is degradative: it is induced to high levels by alanine and is subject to catabolite repression. PW000788 Metabolic Secondary Metabolites: Valine and I-leucine biosynthesis from pyruvate The biosynthesis of Valine and L-leucine from pyruvic acid starts with pyruvic acid interacting with a hydrogen ion through a acetolactate synthase / acetohydroxybutanoate synthase resulting in a release of a carbon dioxide, a (S)-2-acetolactate. The latter compound then interacts with a hydrogen ion through a NADPH-driven acetohydroxy acid isomeroreductase resulting in the release of a NADP, a (R) 2,3-dihydroxy-3-methylvalerate. The latter compound is then dehydrated by a dihydroxy acid dehydratase resulting in the release of a water molecule an 3-methyl-2-oxovaleric acid. The 3-methyl-2-oxovaleric acid can produce an L-valine by interacting with a L-glutamic acid through a Valine Transaminase resulting in the release of a Oxoglutaric acid and a L-valine. The 3-methyl-2-oxovaleric acid then interacts with an acetyl-CoA and a water molecule through a 2-isopropylmalate synthase resulting in the release of a hydrogen ion, a Coenzyme A and a 2-Isopropylmalic acid. The isopropylimalic acid is then hydrated by interacting with a isopropylmalate isomerase resulting in a 3-isopropylmalate. This compound then interacts with an NAD driven 3-isopropylmalate dehydrogenase resulting in a NADH, a hydrogen ion and a 2-isopropyl-3-oxosuccinate. The latter compound then interacts with hydrogen ion spontaneously resulting in a carbon dioxide and a ketoleucine. The ketoleucine then interacts with a L-glutamic acid through a branched-chain amino-acid aminotransferase resulting in the oxoglutaric acid and L-leucine. PW000978 Metabolic Valine Biosynthesis The pathway of valine biosynthesis starts with pyruvic acid interacting with a hydrogen ion through a acetolactate synthase / acetohydroxybutanoate synthase or a acetohydroxybutanoate synthase / acetolactate synthase resulting in the release of carbon dioxide and (S)-2-acetolactate. The latter compound then interacts with a hydrogen ion through an NADPH driven acetohydroxy acid isomeroreductase resulting in the release of a NADP and an (R) 2,3-dihydroxy-3-methylvalerate. The latter compound is then dehydrated by a dihydroxy acid dehydratase resulting in the release of water and isovaleric acid. Isovaleric acid interacts with an L-glutamic acid through a Valine Transaminase resulting in a oxoglutaric acid and an L-valine. L-valine is then transported into the periplasmic space through a L-valine efflux transporter. PW000812 Metabolic tRNA Charging 2 This pathway groups together all E. coli tRNA charging reactions. PW000803 Metabolic tRNA charging This pathway groups together all E. coli tRNA charging reactions. PW000799 Metabolic tRNA charging TRNA-CHARGING-PWY alanine biosynthesis I ALANINE-VALINESYN-PWY valine biosynthesis VALSYN-PWY Specdb::CMs 662 Specdb::CMs 663 Specdb::CMs 664 Specdb::CMs 665 Specdb::CMs 666 Specdb::CMs 912 Specdb::CMs 967 Specdb::CMs 2760 Specdb::CMs 30029 Specdb::CMs 30030 Specdb::CMs 30383 Specdb::CMs 30384 Specdb::CMs 30615 Specdb::CMs 30616 Specdb::CMs 30725 Specdb::CMs 30802 Specdb::CMs 31254 Specdb::CMs 31255 Specdb::CMs 37823 Specdb::CMs 134289 Specdb::CMs 142023 Specdb::CMs 1080931 Specdb::CMs 1080933 Specdb::CMs 1080935 Specdb::EiMs 1986 Specdb::NmrOneD 1279 Specdb::NmrOneD 1582 Specdb::NmrOneD 4778 Specdb::NmrOneD 7862 Specdb::NmrOneD 7863 Specdb::NmrOneD 7864 Specdb::NmrOneD 7865 Specdb::NmrOneD 7866 Specdb::NmrOneD 7867 Specdb::NmrOneD 7868 Specdb::NmrOneD 7869 Specdb::NmrOneD 7870 Specdb::NmrOneD 7871 Specdb::NmrOneD 7872 Specdb::NmrOneD 7873 Specdb::NmrOneD 7874 Specdb::NmrOneD 7875 Specdb::NmrOneD 7876 Specdb::NmrOneD 7877 Specdb::NmrOneD 7878 Specdb::NmrOneD 7879 Specdb::NmrOneD 7880 Specdb::NmrOneD 7881 Specdb::NmrOneD 166439 Specdb::MsMs 1244 Specdb::MsMs 1245 Specdb::MsMs 1246 Specdb::MsMs 4762 Specdb::MsMs 4763 Specdb::MsMs 4764 Specdb::MsMs 4765 Specdb::MsMs 4766 Specdb::MsMs 4767 Specdb::MsMs 4768 Specdb::MsMs 4769 Specdb::MsMs 4770 Specdb::MsMs 4771 Specdb::MsMs 4772 Specdb::MsMs 4773 Specdb::MsMs 4774 Specdb::MsMs 4775 Specdb::MsMs 4776 Specdb::MsMs 4777 Specdb::MsMs 4783 Specdb::MsMs 4784 Specdb::MsMs 4785 Specdb::MsMs 178806 Specdb::MsMs 178807 Specdb::MsMs 178808 Specdb::NmrTwoD 1041 Specdb::NmrTwoD 1524 HMDB00883 1182 6050 C00183 16414 VAL VAL_LFZW valine Keseler, I. 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J Invest Dermatol. 2005 Aug;125(2):256-63. 16098035 Jensen PK, Jacobsen NO: Studies of D-amino acid oxidase activity in human epidermis and cultured human epidermal cells. Arch Dermatol Res. 1984;276(1):57-64. 6142701 Kurpad AV, Regan MM, Raj TD, Gnanou JV, Rao VN, Young VR: The daily valine requirement of healthy adult Indians determined by the 24-h indicator amino acid balance approach. Am J Clin Nutr. 2005 Aug;82(2):373-9. 16087981 Kinoshita, Shukuo; Udaka, Shigezo. L-Valine production by fermentation. (1962), 2 pp. http://hmdb.ca/system/metabolites/msds/000/000/797/original/HMDB00883.pdf?1358894699 Valyl-tRNA synthetase P07118 SYV_ECOLI valS http://ecmdb.ca/proteins/P07118.xml Valine--pyruvate aminotransferase P09053 AVTA_ECOLI avtA http://ecmdb.ca/proteins/P09053.xml High-affinity branched-chain amino acid transport system permease protein livH P0AEX7 LIVH_ECOLI livH http://ecmdb.ca/proteins/P0AEX7.xml High-affinity branched-chain amino acid transport system permease protein livM P22729 LIVM_ECOLI livM http://ecmdb.ca/proteins/P22729.xml Uncharacterized aminotransferase yfbQ P0A959 YFBQ_ECOLI yfbQ http://ecmdb.ca/proteins/P0A959.xml Branched-chain-amino-acid aminotransferase P0AB80 ILVE_ECOLI ilvE http://ecmdb.ca/proteins/P0AB80.xml High-affinity branched-chain amino acid transport ATP-binding protein livG P0A9S7 LIVG_ECOLI livG http://ecmdb.ca/proteins/P0A9S7.xml Leu/Ile/Val-binding protein P0AD96 LIVJ_ECOLI livJ http://ecmdb.ca/proteins/P0AD96.xml High-affinity branched-chain amino acid transport ATP-binding protein livF P22731 LIVF_ECOLI livF http://ecmdb.ca/proteins/P22731.xml Uncharacterized amino-acid ABC transporter ATP-binding protein yecC P37774 YECC_ECOLI yecC http://ecmdb.ca/proteins/P37774.xml Inner membrane amino-acid ABC transporter permease protein yecS P0AFT2 YECS_ECOLI yecS http://ecmdb.ca/proteins/P0AFT2.xml High-affinity branched-chain amino acid transport system permease protein livH P0AEX7 LIVH_ECOLI livH http://ecmdb.ca/proteins/P0AEX7.xml High-affinity branched-chain amino acid transport system permease protein livM P22729 LIVM_ECOLI livM http://ecmdb.ca/proteins/P22729.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 High-affinity branched-chain amino acid transport ATP-binding protein livG P0A9S7 LIVG_ECOLI livG http://ecmdb.ca/proteins/P0A9S7.xml Leu/Ile/Val-binding protein P0AD96 LIVJ_ECOLI livJ http://ecmdb.ca/proteins/P0AD96.xml High-affinity branched-chain amino acid transport ATP-binding protein livF P22731 LIVF_ECOLI livF http://ecmdb.ca/proteins/P22731.xml Uncharacterized protein ygaH P43667 YGAH_ECOLI ygaH http://ecmdb.ca/proteins/P43667.xml Outer membrane protein F P02931 OMPF_ECOLI ompF http://ecmdb.ca/proteins/P02931.xml Branched-chain amino acid transport system 2 carrier protein P0AD99 BRNQ_ECOLI brnQ http://ecmdb.ca/proteins/P0AD99.xml Inner membrane protein ygaZ P76630 YGAZ_ECOLI ygaZ http://ecmdb.ca/proteins/P76630.xml Outer membrane protein C P06996 OMPC_ECOLI ompC http://ecmdb.ca/proteins/P06996.xml Adenosine triphosphate + Water + L-Valine > ADP + Hydrogen ion + Phosphate + L-Valine ABC-36-RXN Adenosine triphosphate + Water + L-Valine > ADP + Hydrogen ion + Phosphate + L-Valine ABC-36-RXN alpha-Ketoisovaleric acid + L-Alanine <> Pyruvic acid + L-Valine + a-Ketoisovaleric acid R01215 VALINE-PYRUVATE-AMINOTRANSFER-RXN alpha-Ketoglutarate + L-Valine <> alpha-Ketoisovaleric acid + L-Glutamate R01214 Adenosine triphosphate + tRNA(Val) + L-Valine + tRNA(Val) <> Adenosine monophosphate + Pyrophosphate + L-Valyl-tRNA(Val) + L-Valyl-tRNA(Val) R03665 L-Valine + Pyruvic acid <> alpha-Ketoisovaleric acid + L-Alanine R01215 Adenosine triphosphate + L-Valine + tRNA(Val) <> Adenosine monophosphate + Pyrophosphate + L-Valyl-tRNA(Val) R03665 Adenosine triphosphate + L-Valine + Water > ADP + Phosphate + L-Valine + Hydrogen ion ABC-36-RXN Adenosine triphosphate + L-Valine + Water > ADP + Phosphate + L-Valine + Hydrogen ion ABC-36-RXN L-Valine + Oxoglutaric acid <> alpha-Ketoisovaleric acid + L-Glutamate BRANCHED-CHAINAMINOTRANSFERVAL-RXN L-Valine + Pyruvic acid > a-Ketoisovaleric acid + L-Alanine L-Valine + Oxoglutaric acid > a-Ketoisovaleric acid + L-Glutamate Adenosine triphosphate + L-Valine + tRNA(Val) > Adenosine monophosphate + Pyrophosphate + L-valyl-tRNA(Val) L-Valine + Pyruvic acid + L-Valine > L-Alanine + a-Ketoisovaleric acid + L-Alanine PW_R002662 a-Ketoisovaleric acid + L-Glutamic acid + L-Glutamate > Oxoglutaric acid + L-Valine + L-Valine PW_R002663 Isovaleric acid + L-Glutamic acid + L-Glutamate > Oxoglutaric acid + L-Valine + L-Valine PW_R002886 3-Methyl-2-oxovaleric acid + L-Glutamic acid + 3-Methyl-2-oxovaleric acid + L-Glutamate > Oxoglutaric acid + L-Valine + L-Valine PW_R003714 L-Valine + Adenosine triphosphate + Hydrogen ion + tRNA(Val) + L-Valine > Adenosine monophosphate + Pyrophosphate + L-Valyl-tRNA(Val) PW_R002831 L-Valine + Adenosine triphosphate + Water + L-Valine > L-Valine + Adenosine diphosphate + Pyrophosphate + Hydrogen ion + ADP PW_RCT000104 Adenosine triphosphate + tRNA(Val) + L-Valine <> Adenosine monophosphate + Pyrophosphate + L-Valyl-tRNA(Val) Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glucose Shake flask and filter culture 4020.0 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 16080000 0 Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. 19561621 Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glycerol Shake flask and filter culture 2290.0 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 9160000 0 Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. 19561621 Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L acetate Shake flask and filter culture 1070.0 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 4280000 0 Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599. 19561621 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 181.0 uM 0.0 37 oC BW25113 Stationary Phase, glucose limited 724000 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 Luria-Bertani (LB) media Shake flask 1645.0 uM true 134.0 37 oC BL21 DE3 Stationary phase cultures (overnight culture) 6580000 536000 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 Luria-Bertani (LB) media Shake flask 1623.33 uM true 107.86 37 oC BL21 DE3 Stationary phase cultures (overnight culture) 6493333 431432 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