2.0 2012-05-31 13:00:16 -0600 2015-09-13 12:56:08 -0600 ECMDB00687 M2MDB000170 L-Leucine Leucine (abbreviated as Leu or L) is an amino acid with the chemical formula HO2CCH(NH2)CH2CH(CH3)2. It is synthesized in plants and microorganisms via several steps starting from pyruvic acid. The initial part of the pathway also leads to valine. The intermediate alpha-ketovalerate is converted to alpha-isopropylmalate and then beta-isopropylmalate, which is dehydrogenated to alpha-ketoisocaproate, which in the final step undergoes reductive amination. (2S)-&alpha;-2-amino-4-methylvalerate (2S)-&alpha;-2-amino-4-methylvaleric acid (2S)-&alpha;-leucine (2S)-2-Amino-4-methylpentanoate (2S)-2-Amino-4-methylpentanoic acid (2S)-a-2-amino-4-Methylvalerate (2S)-a-2-amino-4-Methylvaleric acid (2S)-a-Leucine (2S)-alpha-2-amino-4-methylvalerate (2S)-alpha-2-amino-4-methylvaleric acid (2S)-alpha-leucine (2S)-α-2-amino-4-Methylvalerate (2S)-α-2-amino-4-Methylvaleric acid (2S)-α-Leucine (S)-(+)-Leucine (S)-2-Amino-4-methylpentanoate (S)-2-Amino-4-methylpentanoic acid (S)-2-Amino-4-methylvalerate (S)-2-Amino-4-methylvaleric acid (S)-Leucine 2-Amino-4-methylvalerate 2-Amino-4-methylvaleric acid 4-Methyl-L-Norvaline L L-(+)-Leucine L-a-Aminoisocaproate L-a-Aminoisocaproic acid L-alpha-Aminoisocaproate L-alpha-Aminoisocaproic acid L-α-Aminoisocaproate L-α-Aminoisocaproic acid Leu Leucine C6H13NO2 131.1729 131.094628665 (2S)-2-amino-4-methylpentanoic acid L-leucine 61-90-5 CC(C)C[C@H](N)C(O)=O InChI=1S/C6H13NO2/c1-4(2)3-5(7)6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)/t5-/m0/s1 ROHFNLRQFUQHCH-YFKPBYRVSA-N Solid Cytosol Extra-organism Periplasm logp -1.82 ALOGPS logs -0.27 ALOGPS solubility 6.98e+01 g/l ALOGPS melting_point 268-288 logp -1.6 ChemAxon pka_strongest_acidic 2.79 ChemAxon pka_strongest_basic 9.52 ChemAxon iupac (2S)-2-amino-4-methylpentanoic acid ChemAxon average_mass 131.1729 ChemAxon mono_mass 131.094628665 ChemAxon smiles CC(C)C[C@H](N)C(O)=O ChemAxon formula C6H13NO2 ChemAxon inchi InChI=1S/C6H13NO2/c1-4(2)3-5(7)6(8)9/h4-5H,3,7H2,1-2H3,(H,8,9)/t5-/m0/s1 ChemAxon inchikey ROHFNLRQFUQHCH-YFKPBYRVSA-N ChemAxon polar_surface_area 63.32 ChemAxon refractivity 34.17 ChemAxon polarizability 14.16 ChemAxon rotatable_bond_count 3 ChemAxon acceptor_count 3 ChemAxon donor_count 2 ChemAxon physiological_charge 0 ChemAxon formal_charge 0 ChemAxon 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 Valine, leucine and isoleucine degradation ec00280 ABC transporters ec02010 Glucosinolate biosynthesis ec00966 Metabolic pathways eco01100 Leucine Biosynthesis Leucine biosynthesis involves a five-step conversion process starting with the valine precursor 2-keto-isovalerate interacting with acetyl-CoA and water through a 2-isopropylmalate synthase resulting in Coenzyme A, hydrogen Ion and 2-isopropylmalic acid. The latter compound reacts with isopropylmalate isomerase which dehydrates the compound resulting in a Isopropylmaleate. This compound reacts with water through a isopropylmalate isomerase resulting in 3-isopropylmalate. This compound interacts with a NAD-driven D-malate / 3-isopropylmalate dehydrogenase results in 2-isopropyl-3-oxosuccinate. This compound interacts spontaneously with hydrogen resulting in the release of carbon dioxide and ketoleucine. Ketoleucine interacts in a reversible reaction with L-glutamic acid through a branched-chain amino-acid aminotransferase resulting in Oxoglutaric acid and L-leucine L-leucine can then be exported outside the cytoplasm through a transporter: L-amino acid efflux transporter. The final step in this pathway is catalyzed by two transaminases of broad specificity, IlvE and TyrB. Both the first enzyme in the pathway, 2-isopropylmalate synthase, and the terminal transaminase TyrB are suppressed by leucine. TyrB is subject to inhibition by the pathway's starting compound, 2-keto-isovalerate, and by one of its off-pathway products, tyrosine. One consequence of this inhibition by 2-keto-isovalerate is that in the absence of IlvE activity, mutations in earlier steps in the pathway cannot be compensated for by any alternate method of introducing 2-ketoisocaproate for conversion to leucine. PW000811 Metabolic Operon: acetolactate synthase III inactivation The ilvIH operon of Escherichia coli encodes acetohydroxyacid synthase III. The IHB protein binds to two sites upstream of the ilvlH promoter. Expresion of this operon is repressed by the presence of Leucine, but not no other branched amino acids PW001882 Signaling Secondary Metabolite: Leucine biosynthesis Leucine biosynthesis involves a five-step conversion process starting with a 3-methyl-2-oxovaleric acid interacting with acetyl-CoA and a water molecule through a 2-isopropylmalate synthase resulting in Coenzyme A, hydrogen Ion and 2-isopropylmalic acid. The latter compound reacts with isopropylmalate isomerase which dehydrates the compound resulting in a Isopropylmaleate. This compound reacts with water through a isopropylmalate isomerase resulting in 3-isopropylmalate. This compound interacts with a NAD-driven D-malate / 3-isopropylmalate dehydrogenase results in 2-isopropyl-3-oxosuccinate. This compound interacts spontaneously with hydrogen resulting in the release of carbon dioxide and ketoleucine. Ketoleucine interacts in a reversible reaction with L-glutamic acid through a branched-chain amino-acid aminotransferase resulting in Oxoglutaric acid and L-leucine Both the first enzyme in the pathway, 2-isopropylmalate synthase, and the terminal transaminase TyrB are suppressed by leucine. TyrB is subject to inhibition by the pathway's starting compound, 2-keto-isovalerate, and by one of its off-pathway products, tyrosine. One consequence of this inhibition by 2-keto-isovalerate is that in the absence of IlvE activity, mutations in earlier steps in the pathway cannot be compensated for by any alternate method of introducing 2-ketoisocaproate for conversion to leucine. PW000980 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 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 isoleucine biosynthesis I (from threonine) LEUSYN-PWY Specdb::CMs 604 Specdb::CMs 605 Specdb::CMs 606 Specdb::CMs 607 Specdb::CMs 608 Specdb::CMs 2748 Specdb::CMs 28003 Specdb::CMs 30023 Specdb::CMs 30207 Specdb::CMs 30312 Specdb::CMs 30313 Specdb::CMs 30594 Specdb::CMs 30726 Specdb::CMs 30769 Specdb::CMs 37697 Specdb::CMs 131297 Specdb::CMs 139031 Specdb::CMs 1072453 Specdb::CMs 1072455 Specdb::CMs 1072456 Specdb::EiMs 1983 Specdb::NmrOneD 1251 Specdb::NmrOneD 1477 Specdb::NmrOneD 4877 Specdb::NmrOneD 144830 Specdb::NmrOneD 144831 Specdb::NmrOneD 144832 Specdb::NmrOneD 144833 Specdb::NmrOneD 144834 Specdb::NmrOneD 144835 Specdb::NmrOneD 144836 Specdb::NmrOneD 144837 Specdb::NmrOneD 144838 Specdb::NmrOneD 144839 Specdb::NmrOneD 144840 Specdb::NmrOneD 144841 Specdb::NmrOneD 144842 Specdb::NmrOneD 144843 Specdb::NmrOneD 144844 Specdb::NmrOneD 144845 Specdb::NmrOneD 144846 Specdb::NmrOneD 144847 Specdb::NmrOneD 144848 Specdb::NmrOneD 144849 Specdb::NmrOneD 166492 Specdb::MsMs 951 Specdb::MsMs 952 Specdb::MsMs 953 Specdb::MsMs 4393 Specdb::MsMs 4394 Specdb::MsMs 4395 Specdb::MsMs 4396 Specdb::MsMs 4397 Specdb::MsMs 4398 Specdb::MsMs 4399 Specdb::MsMs 4400 Specdb::MsMs 4401 Specdb::MsMs 4402 Specdb::MsMs 4403 Specdb::MsMs 4404 Specdb::MsMs 4405 Specdb::MsMs 4406 Specdb::MsMs 4407 Specdb::MsMs 4408 Specdb::MsMs 4409 Specdb::MsMs 4410 Specdb::MsMs 4416 Specdb::MsMs 4417 Specdb::MsMs 4418 Specdb::MsMs 178782 Specdb::NmrTwoD 1423 HMDB00687 6106 5880 C00123 15603 LEU LEU_LFZW Leucine Keseler, I. 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Annals of the New York Academy of Sciences (1984), 434(Enzyme Eng.), 78-86. http://hmdb.ca/system/metabolites/msds/000/000/606/original/HMDB00687.pdf?1358894679 Aromatic-amino-acid aminotransferase P04693 TYRB_ECOLI tyrB http://ecmdb.ca/proteins/P04693.xml Leucyl-tRNA synthetase P07813 SYL_ECOLI leuS http://ecmdb.ca/proteins/P07813.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 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 Leucine-specific-binding protein P04816 LIVK_ECOLI livK http://ecmdb.ca/proteins/P04816.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 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 Outer membrane protein C P06996 OMPC_ECOLI ompC http://ecmdb.ca/proteins/P06996.xml Leucine-specific-binding protein P04816 LIVK_ECOLI livK http://ecmdb.ca/proteins/P04816.xml Adenosine triphosphate + Water + L-Leucine > ADP + Hydrogen ion + L-Leucine + Phosphate ABC-35-RXN Adenosine triphosphate + Water + L-Leucine > ADP + Hydrogen ion + L-Leucine + Phosphate ABC-35-RXN Ketoleucine + L-Glutamate > alpha-Ketoglutarate + L-Leucine Adenosine triphosphate + L-Leucine + tRNA(Leu) > Adenosine monophosphate + L-Leucyl-tRNA(Leu) + Pyrophosphate L-Leucine + alpha-Ketoglutarate <> 4-Methyl-2-oxopentanoate + L-Glutamate + Ketoleucine R01090 Adenosine triphosphate + L-Leucine + tRNA(Leu) + tRNA(Leu) <> Adenosine monophosphate + Pyrophosphate + L-Leucyl-tRNA + L-Leucyl-tRNA R03657 Adenosine triphosphate + L-Leucine + Water > ADP + Phosphate + L-Leucine + Hydrogen ion ABC-35-RXN Adenosine triphosphate + L-Leucine + Water > ADP + Phosphate + L-Leucine + Hydrogen ion ABC-35-RXN L-Leucine + Oxoglutaric acid <> Ketoleucine + L-Glutamate BRANCHED-CHAINAMINOTRANSFERLEU-RXN ala-leu + Water > L-Alanine + L-Leucine RXN0-6979 L-Leucine + Oxoglutaric acid > Ketoleucine + L-Glutamate L-Leucine + Adenosine triphosphate + Hydrogen ion + tRNA(Leu) > Adenosine monophosphate + Pyrophosphate + L-Leucyl-tRNA(Leu) PW_R002830 Ketoleucine + L-Glutamic acid + L-Glutamate > Oxoglutaric acid + L-Leucine PW_R002881 L-Leucine + Adenosine triphosphate + Water > L-Leucine + Adenosine diphosphate + Phosphate + Hydrogen ion + ADP PW_RCT000103 L-Leucine + Adenosine triphosphate + Water > L-Leucine + Adenosine diphosphate + Phosphate + Hydrogen ion + ADP PW_RCT000103 Adenosine triphosphate + L-Leucine + tRNA(Leu) <> Adenosine monophosphate + Pyrophosphate + L-Leucyl-tRNA Adenosine triphosphate + L-Leucine + tRNA(Leu) <> Adenosine monophosphate + Pyrophosphate + L-Leucyl-tRNA 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 150.0 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 600000 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 220.0 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 880000 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 170.0 uM 0.0 37 oC K12 NCM3722 Mid-Log Phase 680000 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 120.0 uM 0.0 37 oC BW25113 Stationary Phase, glucose limited 480000 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 202.0 uM true 26.0 37 oC BL21 DE3 Stationary phase cultures (overnight culture) 809200 104000 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 224.33 uM true 24.42 37 oC BL21 DE3 Stationary phase cultures (overnight culture) 897333 97680 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