5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase

5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase
Identifiers
EC no.	1.2.1.60
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

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⁺ ${\displaystyle \rightleftharpoons }$ 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.

Structural studies

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

References

• Blakley ER (1977). "The catabolism of L-tyrosine by an Arthrobacter sp". Can. J. Microbiol. 23 (9): 1128–39. doi:10.1139/m77-169. PMID 20216.
• Alonso JM, Garrido-Pertierra A (1982). "Carboxymethylhydroxymuconic semialdehyde dehydrogenase in the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli". Biochim. Biophys. Acta. 719 (1): 165–7. doi:10.1016/0304-4165(82)90322-1. 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 (1): 302–6. doi:10.1128/JB.143.1.302-306.1980. PMC 294232. PMID 6995433.
• Garrido-Pertierra A, 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 (3): 581–584. doi:10.1111/j.1432-1033.1981.tb06377.x. PMID 7026235.