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5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase

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5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase
Identifiers
EC no.1.2.1.60
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

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+ 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

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

References

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  • 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.