| Phenylacetaldoxime dehydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.99.1.7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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In enzymology, a phenylacetaldoxime dehydratase (EC 4.99.1.7) is an enzyme that catalyzes the chemical reaction
- (Z)-phenylacetaldehyde oxime phenylacetonitrile + H2O
phenylacetonitrile + H2OHence, this enzyme has one substrate, (Z)-phenylacetaldehyde oxime, and two products, phenylacetonitrile and H2O.
This enzyme belongs to the family of lyases, specifically the "catch-all" class of lyases that do not fit into any other sub-class. The systematic name of this enzyme class is (Z)-phenylacetaldehyde-oxime hydro-lyase (phenylacetonitrile-forming). Other names in common use include PAOx dehydratase, arylacetaldoxime dehydratase, OxdB, and (Z)-phenylacetaldehyde-oxime hydro-lyase. This enzyme participates in styrene degradation.
References
- Kato Y, Nakamura K, Sakiyama H, Mayhew SG, Asano Y (2000). "Novel heme-containing lyase, phenylacetaldoxime dehydratase from Bacillus sp. strain OxB-1: purification, characterization, and molecular cloning of the gene". Biochemistry. 39 (4): 800–9. doi:10.1021/bi991598u. PMID 10651646.
- Kobayashi K, Yoshioka S, Kato Y, Asano Y, Aono S (2005). "Regulation of aldoxime dehydratase activity by redox-dependent change in the coordination structure of the aldoxime-heme complex". J. Biol. Chem. 280 (7): 5486–90. doi:10.1074/jbc.M410474200. PMID 15596434.
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