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Pathway Description
Leucine Biosynthesis
Escherichia coli
Category:
Metabolite Pathway
Sub-Category:
Metabolic
Created: 2015-03-16
Last Updated: 2025-05-08
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. In the final step, ketoleucine can be catalyzed to form L-leucine by branched-chain amino-acid aminotransferase (IlvE) and tyrosine aminotransferase (TryB). L-Glutamic acid can also be transformed into oxoglutaric acid by these two enzymes. Tyrosine aminotransferase can be suppressed by lecuine, and inhibited by 2-keto-isovarlerate and its end product, tyrosine. 2-ketoisocaproate can not be introduced if 2-keto-isovarlerate inhibit TyrB and IlvE is absent.
References
Leucine Biosynthesis References
Wessler SR, Calvo JM: Control of leu operon expression in Escherichia coli by a transcription attenuation mechanism. J Mol Biol. 1981 Jul 15;149(4):579-97.
Pubmed: 6171647
Powell JT, Morrison JF: Role of the Escherichia coli aromatic amino acid aminotransferase in leucine biosynthesis. J Bacteriol. 1978 Oct;136(1):1-4.
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Yura T, Mori H, Nagai H, Nagata T, Ishihama A, Fujita N, Isono K, Mizobuchi K, Nakata A: Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region. Nucleic Acids Res. 1992 Jul 11;20(13):3305-8. doi: 10.1093/nar/20.13.3305.
Pubmed: 1630901
Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. doi: 10.1126/science.277.5331.1453.
Pubmed: 9278503
Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. doi: 10.1038/msb4100049. Epub 2006 Feb 21.
Pubmed: 16738553
Chen H, Lawrence CB, Bryan SK, Moses RE: Aphidicolin inhibits DNA polymerase II of Escherichia coli, an alpha-like DNA polymerase. Nucleic Acids Res. 1990 Dec 11;18(23):7185-6. doi: 10.1093/nar/18.23.7185.
Pubmed: 2124684
Wallon G, Yamamoto K, Kirino H, Yamagishi A, Lovett ST, Petsko GA, Oshima T: Purification, catalytic properties and thermostability of 3-isopropylmalate dehydrogenase from Escherichia coli. Biochim Biophys Acta. 1997 Jan 4;1337(1):105-12. doi: 10.1016/s0167-4838(96)00157-4.
Pubmed: 9003442
Magyar C, Szilagyi A, Zavodszky P: Relationship between thermal stability and 3-D structure in a homology model of 3-isopropylmalate dehydrogenase from Escherichia coli. Protein Eng. 1996 Aug;9(8):663-70.
Pubmed: 8875643
Wallon G, Kryger G, Lovett ST, Oshima T, Ringe D, Petsko GA: Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus. J Mol Biol. 1997 Mar 14;266(5):1016-31. doi: 10.1006/jmbi.1996.0797.
Pubmed: 9086278
Itoh T, Aiba H, Baba T, Hayashi K, Inada T, Isono K, Kasai H, Kimura S, Kitakawa M, Kitagawa M, Makino K, Miki T, Mizobuchi K, Mori H, Mori T, Motomura K, Nakade S, Nakamura Y, Nashimoto H, Nishio Y, Oshima T, Saito N, Sampei G, Seki Y, Horiuchi T, et al.: A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map. DNA Res. 1996 Dec 31;3(6):379-92. doi: 10.1093/dnares/3.6.379.
Pubmed: 9097040
Kuramitsu S, Ogawa T, Ogawa H, Kagamiyama H: Branched-chain amino acid aminotransferase of Escherichia coli: nucleotide sequence of the ilvE gene and the deduced amino acid sequence. J Biochem. 1985 Apr;97(4):993-9. doi: 10.1093/oxfordjournals.jbchem.a135176.
Pubmed: 3897211
Lawther RP, Nichols B, Zurawski G, Hatfield GW: The nucleotide sequence preceding and including the beginning of the ilvE gene of the ilvGEDA operon of Escherichia coli K12. Nucleic Acids Res. 1979 Dec 20;7(8):2289-301. doi: 10.1093/nar/7.8.2289.
Pubmed: 392469
Lawther RP, Wek RC, Lopes JM, Pereira R, Taillon BE, Hatfield GW: The complete nucleotide sequence of the ilvGMEDA operon of Escherichia coli K-12. Nucleic Acids Res. 1987 Mar 11;15(5):2137-55. doi: 10.1093/nar/15.5.2137.
Pubmed: 3550695
Fotheringham IG, Dacey SA, Taylor PP, Smith TJ, Hunter MG, Finlay ME, Primrose SB, Parker DM, Edwards RM: The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes. Biochem J. 1986 Mar 15;234(3):593-604. doi: 10.1042/bj2340593.
Pubmed: 3521591
Kuramitsu S, Inoue K, Ogawa T, Ogawa H, Kagamiyama H: Aromatic amino acid aminotransferase of Escherichia coli: nucleotide sequence of the tyrB gene. Biochem Biophys Res Commun. 1985 Nov 27;133(1):134-9. doi: 10.1016/0006-291x(85)91851-0.
Pubmed: 3907634
Yang J, Pittard J: Molecular analysis of the regulatory region of the Escherichia coli K-12 tyrB gene. J Bacteriol. 1987 Oct;169(10):4710-5. doi: 10.1128/jb.169.10.4710-4715.1987.
Pubmed: 3308851
This pathway was propagated using PathWhiz -
Pon, A. et al. Pathways with PathWhiz (2015) Nucleic Acids Res. 43(Web Server issue): W552–W559.
Propagated from SMP0000831
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