Biology:2-hydroxymuconate-semialdehyde hydrolase
| 2-hydroxymuconate-semialdehyde hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.7.1.9 | ||||||||
| CAS number | 54004-61-4 | ||||||||
| 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 2-hydroxymuconate-semialdehyde hydrolase (EC 3.7.1.9) is an enzyme that catalyzes the chemical reaction
- 2-hydroxymuconate semialdehyde + H2O [math]\displaystyle{ \rightleftharpoons }[/math] formate + 2-oxopent-4-enoate
Thus, the two substrates of this enzyme are 2-hydroxymuconate semialdehyde and H2O, whereas its two products are formate and 2-oxopent-4-enoate.
This enzyme belongs to the family of hydrolases, specifically those acting on carbon-carbon bonds in ketonic substances. The systematic name of this enzyme class is 2-hydroxymuconate-semialdehyde formylhydrolase. Other names in common use include 2-hydroxy-6-oxohepta-2,4-dienoate hydrolase, 2-hydroxymuconic semialdehyde hydrolase, HMSH, and HOD hydrolase. This enzyme participates in 5 metabolic pathways: benzoate degradation via hydroxylation, toluene and xylene degradation, 1,4-dichlorobenzene degradation, carbazole degradation, and styrene degradation.
Structural studies
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1IUN, 1IUO, 1IUP, 1UK6, 1UK7, 1UK8, 1UK9, 1UKA, 1UKB, and 2D0D.
References
- "Evolutionary relationships between catabolic pathways for aromatics: conservation of gene order and nucleotide sequences of catechol oxidation genes of pWW0 and NAH7 plasmids". MGG Mol. Gen. Genet. 210 (2): 241–247. 1987. doi:10.1007/BF00325689. PMID 3481421.
- "The meta cleavage of catechol by Azotobacter species 4-Oxalocrotonate pathway". Eur. J. Biochem. 20 (3): 400–13. 1971. doi:10.1111/j.1432-1033.1971.tb01406.x. PMID 4325686.
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