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 | ||||||||
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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+ 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.
