ENZYME entry: EC 4.99.1.7
| Accepted Name |
| Phenylacetaldoxime dehydratase.
|
| Alternative Name(s) |
| Arylacetaldoxime dehydratase. |
| PAOx dehydratase. |
| Reaction catalysed |
| (Z)-phenylacetaldehyde oxime <=> phenylacetonitrile + H(2)O |
| Cofactor(s) |
| Heme.
|
| Comment(s) |
- The enzyme from Bacillus sp. OxB-1 contains protoheme IX, the iron of
which must be in the form Fe(2+) for activity.
- (Z)-phenylacetaldoxime binds to ferric heme (the Fe(3+) form) via the
oxygen atom whereas it binds to the active ferrous form via the
nitrogen atom.
- In this way, the oxidation state of the heme controls the
coordination stucture of the substrate--heme complex, which regulates
enzyme activity.
- The enzyme is active toward several (Z)-arylacetaldoximes and (E/Z)-
alkylaldoximes as well as toward arylalkylaldoximes such as
3-phenylpropionaldoxime and 4-phenylbutyraldoxime.
- However, it is inactive with phenylacetaldoximes that have a
substituent group at an alpha-site of an oxime group, for example,
with (E/Z)-2-phenylpropionaldoxime and (E/Z)-mandelaldoxime.
- The activity of the enzyme is inhibited completely by the heavy-metal
cations Cu(+), Cu(2+), Ag(+) and Hg(+) whereas Fe(2+) and Sn(2+) have
an activatory effect.
|
| Cross-references |
| BRENDA | 4.99.1.7 |
| EC2PDB | 4.99.1.7 |
| ExplorEnz | 4.99.1.7 |
| PRIAM enzyme-specific profiles | 4.99.1.7 |
| KEGG Ligand Database for Enzyme Nomenclature | 4.99.1.7 |
| IUBMB Enzyme Nomenclature | 4.99.1.7 |
| IntEnz | 4.99.1.7 |
| MEDLINE | Find literature relating to 4.99.1.7 |
| MetaCyc | 4.99.1.7 |
| UniProtKB/Swiss-Prot |
|
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