The Enzyme Database

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EC 4.2.1.80     
Accepted name: 2-oxopent-4-enoate hydratase
Reaction: (S)-4-hydroxy-2-oxopentanoate = (2Z)-2-hydroxypenta-2,4-dienoate + H2O
For diagram of 3-phenylpropanoate catabolism, click here, for diagram of catechol catabolism (meta ring cleavage), click here and for diagram of cinnamate catabolism, click here
Other name(s): 2-keto-4-pentenoate hydratase; OEH; 2-keto-4-pentenoate (vinylpyruvate)hydratase; 4-hydroxy-2-oxopentanoate hydro-lyase; 4-hydroxy-2-oxopentanoate hydro-lyase (2-oxopent-4-enoate-forming); mhpD (gene name); ahdF (gene name); todG (gene name); cmtF (gene name); xylJ (gene name); cnbE (gene name)
Systematic name: (S)-4-hydroxy-2-oxopentanoate hydro-lyase ((2Z)-2-hydroxypenta-2,4-dienoate-forming)
Comments: The enzyme is involved in the catechol meta-cleavage pathway, a major mechanism for degradation of aromatic compounds. Also acts, more slowly, on cis-2-oxohex-4-enoate, but not on the trans-isomer. The enzyme was named when it was thought that the substrate is 2-oxopent-4-enoate. However, it was later found that the actual substrate is its tautomer (2Z)-2-hydroxypenta-2,4-dienoate. In some organisms the enzyme forms a complex with EC 4.1.1.77, 2-oxo-3-hexenedioate decarboxylase (previously named 4-oxalocrotonate decarboxylase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 64427-80-1
References:
1.  Kunz, D.A., Ribbons, D.W. and Chapman, P.J. Metabolism of allylglycine and cis-crotylglycine by Pseudomonas putida (arvilla) mt-2 harboring a TOL plasmid. J. Bacteriol. 148 (1981) 72–82. [PMID: 7287632]
2.  Harayama, S., Rekik, M., Ngai, K.L. and Ornston, L.N. Physically associated enzymes produce and metabolize 2-hydroxy-2,4-dienoate, a chemically unstable intermediate formed in catechol metabolism via meta cleavage in Pseudomonas putida. J. Bacteriol. 171 (1989) 6251–6258. [PMID: 2681159]
3.  Pollard, J.R. and Bugg, T.D. Purification, characterisation and reaction mechanism of monofunctional 2-hydroxypentadienoic acid hydratase from Escherichia coli. Eur. J. Biochem. 251 (1998) 98–106. [PMID: 9492273]
[EC 4.2.1.80 created 1984]
 
 


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