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Pathway Description
L-Threonine Degradation to Methylglyoxal
Escherichia coli
Category:
Metabolite Pathway
Sub-Category:
Metabolic
Created: 2015-10-14
Last Updated: 2025-02-08
L-threonine is degrade into methylglyoxal (pyruvaldehyde) by first reacting with a NDA dependent threonine dehydrogenase resulting in the release of a hydrogen ion, an NADH and a 2-amino-3-oxobutanoate. The latter compound reacts spontaneously with a hydrogen ion resulting in the release of a carbon dioxide and a aminoacetone. The aminoacetone in turn reacts with an oxygen and a water molecule through an aminoacetone oxidase resulting in the release of a hydrogen peroxide, ammonium and a methylglyoxal which can then be incorporated in the methylglyoxal degradation pathways.
References
L-Threonine Degradation to Methylglyoxal References
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Pubmed: 6413491
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Pubmed: 4362743
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Pubmed: 5721463
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Pubmed: 4292865
Kelley JJ, Dekker EE: Identity of Escherichia coli D-1-amino-2-propanol:NAD+ oxidoreductase with E. coli glycerol dehydrogenase but not with Neisseria gonorrhoeae 1,2-propanediol:NAD+ oxidoreductase. J Bacteriol. 1985 Apr;162(1):170-5.
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Kim YM, Ogawa W, Tamai E, Kuroda T, Mizushima T, Tsuchiya T: Purification, reconstitution, and characterization of Na(+)/serine symporter, SstT, of Escherichia coli. J Biochem. 2002 Jul;132(1):71-6.
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Kim I, Kim E, Yoo S, Shin D, Min B, Song J, Park C: Ribose utilization with an excess of mutarotase causes cell death due to accumulation of methylglyoxal. J Bacteriol. 2004 Nov;186(21):7229-35. doi: 10.1128/JB.186.21.7229-7235.2004.
Pubmed: 15489434
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Pubmed: 355220
Lyles GA: Mammalian plasma and tissue-bound semicarbazide-sensitive amine oxidases: biochemical, pharmacological and toxicological aspects. Int J Biochem Cell Biol. 1996 Mar;28(3):259-74.
Pubmed: 8920635
Potter R, Kapoor V, Newman EB: Role of threonine dehydrogenase in Escherichia coli threonine degradation. J Bacteriol. 1977 Nov;132(2):385-91.
Pubmed: 334738
Rahhal DA, Turner JM, Willetts AJ: The role of aminoacetone in L-threonine metabolism by Bacillus subtilis. Biochem J. 1967 Jun;103(3):73P.
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Pubmed: 4583203
Sumantran VN, Schweizer HP, Datta P: A novel membrane-associated threonine permease encoded by the tdcC gene of Escherichia coli. J Bacteriol. 1990 Aug;172(8):4288-94.
Pubmed: 2115866
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Pubmed: 4334917
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Aronson BD, Somerville RL, Epperly BR, Dekker EE: The primary structure of Escherichia coli L-threonine dehydrogenase. J Biol Chem. 1989 Mar 25;264(9):5226-32.
Pubmed: 2647748
Sofia HJ, Burland V, Daniels DL, Plunkett G 3rd, Blattner FR: Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes. Nucleic Acids Res. 1994 Jul 11;22(13):2576-86. doi: 10.1093/nar/22.13.2576.
Pubmed: 8041620
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
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Pubmed: 8591028
Steinebach V, Benen JA, Bader R, Postma PW, De Vries S, Duine JA: Cloning of the maoA gene that encodes aromatic amine oxidase of Escherichia coli W3350 and characterization of the overexpressed enzyme. Eur J Biochem. 1996 May 1;237(3):584-91. doi: 10.1111/j.1432-1033.1996.0584p.x.
Pubmed: 8647101
Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kasai H, Kashimoto K, 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, Horiuchi T, et al.: A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map. DNA Res. 1996 Dec 31;3(6):363-77. doi: 10.1093/dnares/3.6.363.
Pubmed: 9097039
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 SMP0002118
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