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Pathway Description
2-Oxopent-4-enoate Metabolism 2
Escherichia coli
Category:
Metabolite Pathway
Sub-Category:
Metabolic
Created: 2015-10-07
Last Updated: 2024-11-18
The pathway starts with trans-cinnamate interacting with a hydrogen ion, an oxygen molecule, and a NADH through a cinnamate dioxygenase resulting in a NAD and a Cis-3-(3-carboxyethyl)-3,5-cyclohexadiene-1,2-diol which then interact together through a 2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase resulting in the release of a hydrogen ion, an NADH molecule and a 2,3 dihydroxy-trans-cinnamate. The second way by which the 2,3 dihydroxy-trans-cinnamate is acquired is through a 3-hydroxy-trans-cinnamate interacting with a hydrogen ion, a NADH and an oxygen molecule through a 3-(3-hydroxyphenyl)propionate 2-hydroxylase resulting in the release of a NAD molecule, a water molecule and a 2,3-dihydroxy-trans-cinnamate. The compound 2,3 dihydroxy-trans-cinnamate then interacts with an oxygen molecule through a 2,3-dihydroxyphenylpropionate 1,2-dioxygenase resulting in a hydrogen ion and a 2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate. The latter compound then interacts with a water molecule through a 2-hydroxy-6-oxononatrienedioate hydrolase resulting in a release of a hydrogen ion, a fumarate molecule and (2Z)-2-hydroxypenta-2,4-dienoate. The latter compound reacts spontaneously to isomerize into a 2-oxopent-4-enoate. This compound is then hydrated through a 2-oxopent-4-enoate hydratase resulting in a 4-hydroxy-2-oxopentanoate. This compound then interacts with a 4-hydroxy-2-ketovalerate aldolase resulting in the release of a pyruvate, and an acetaldehyde. The acetaldehyde then interacts with a coenzyme A and a NAD molecule through a acetaldehyde dehydrogenase resulting in a hydrogen ion, a NADH and an acetyl-coa which can be incorporated into the TCA cycle
References
2-Oxopent-4-enoate Metabolism 2 References
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Pubmed: 3777934
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Pubmed: 9098055
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Pubmed: 16738553
Spence EL, Kawamukai M, Sanvoisin J, Braven H, Bugg TD: Catechol dioxygenases from Escherichia coli (MhpB) and Alcaligenes eutrophus (MpcI): sequence analysis and biochemical properties of a third family of extradiol dioxygenases. J Bacteriol. 1996 Sep;178(17):5249-56. doi: 10.1128/jb.178.17.5249-5256.1996.
Pubmed: 8752345
Pollard JR, Rialland D, Bugg TD: Substrate selectivity and biochemical properties of 4-hydroxy-2-keto-pentanoic acid aldolase from Escherichia coli. Appl Environ Microbiol. 1998 Oct;64(10):4093-4.
Pubmed: 9758851
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Pubmed: 2989782
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Pubmed: 2989781
Burland V, Plunkett G 3rd, Daniels DL, Blattner FR: DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication. Genomics. 1993 Jun;16(3):551-61. doi: 10.1006/geno.1993.1230.
Pubmed: 7686882
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, 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
Pagel JM, Winkelman JW, Adams CW, Hatfield GW: DNA topology-mediated regulation of transcription initiation from the tandem promoters of the ilvGMEDA operon of Escherichia coli. J Mol Biol. 1992 Apr 20;224(4):919-35. doi: 10.1016/0022-2836(92)90460-2.
Pubmed: 1569580
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