In enzymology, a 2-hydroxymuconate-semialdehyde hydrolase (EC 3.7.1.9) is an enzyme that catalyzes the chemical reaction
2-hydroxymuconate-semialdehyde hydrolase | |||||||||
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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 | ||||||||
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- 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
editAs 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.