2-hydroxymuconate-semialdehyde hydrolase
| 2-hydroxymuconate-semialdehyde hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.7.1.9 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
In enzymology, a 2-hydroxymuconate-semialdehyde hydrolase (EC 3.7.1.9) is an enzyme that catalyzes the chemical reaction
- 2-hydroxymuconate semialdehyde + H2O 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
[edit]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
[edit]- Harayama S, Rekik M, Wasserfallen A, Bairoch A (1987). "Evolutionary relationships between catabolic pathways for aromatics: conservation of gene order and nucleotide sequences of catechol oxidation genes of pWW0 and NAH7 plasmids". Molecular and General Genetics MGG. 210 (2): 241–247. doi:10.1007/BF00325689. PMID 3481421. S2CID 20302884.
- Sala-Trepat JM, Evans WC (1971). "The meta cleavage of catechol by Azotobacter species 4-Oxalocrotonate pathway". European Journal of Biochemistry. 20 (3): 400–13. doi:10.1111/j.1432-1033.1971.tb01406.x. PMID 4325686.
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