5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase

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In enzymology, a 5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase (EC 1.2.1.60) is an enzyme that catalyzes the chemical reaction

5-carboxymethyl-2-hydroxymuconate semialdehyde + H₂O + NAD⁺ $\rightleftharpoons$ 5-carboxymethyl-2-hydroxymuconate + NADH + 2 H⁺

The 3 substrates of this enzyme are 5-carboxymethyl-2-hydroxymuconate semialdehyde, H₂O, and NAD⁺, whereas its 3 products are 5-carboxymethyl-2-hydroxymuconate, NADH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 5-carboxymethyl-2-hydroxymuconic-semialdehyde:NAD+ oxidoreductase. This enzyme is also called carboxymethylhydroxymuconic semialdehyde dehydrogenase. This enzyme participates in tyrosine metabolism.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2D4E.

[edit] References

IUBMB entry for 1.2.1.60
BRENDA references for 1.2.1.60 (Recommended.)
PubMed references for 1.2.1.60
PubMed Central references for 1.2.1.60
Google Scholar references for 1.2.1.60
Blakley ER (1977). "The catabolism of L-tyrosine by an Arthrobacter sp". Can. J. Microbiol. 23: 1128–39. PMID 20216.
Alonso JM, Garrido-Pertierra A (1982). "Carboxymethylhydroxymuconic semialdehyde dehydrogenase in the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli". Biochim. Biophys. Acta. 719: 165–7. PMID 6756482.
Cooper RA, Skinner MA (1980). "Catabolism of 3- and 4-hydroxyphenylacetate by the 3,4-dihydroxyphenylacetate pathway in Escherichia coli". J. Bacteriol. 143: 302–6. PMID 6995433.
Garrido-Pertierra A and Cooper RA (1981). "Identification and purification of distinct isomerase and decarboxylase enzymes involved in the 4-hydroxyphenylacetate pathway of Escherichia coli". Eur. J. Biochem. 117: 581–584.