EC number:4.99.1.7

Enzyme

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     4. Lyases
        4.99 Other lyases
            4.99.1 Sole sub-subclass for lyases that do not belong in the other subclasses
ID:4.99.1.7
Description:Phenylacetaldoxime dehydratase.
Alternative Name: PAOx dehydratase.
Arylacetaldoxime dehydratase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.99.1.7
BRENDA Enzyme Link: BRENDA 4.99.1.7
KEGG Enzyme Link: KEGG4.99.1.7
BioCyc Enzyme Link: BioCyc 4.99.1.7
ExPASy Enzyme Link: ExPASy4.99.1.7
EC2PDB Enzyme Link: EC2PDB 4.99.1.7
ExplorEnz Enzyme Link: ExplorEnz 4.99.1.7
PRIAM enzyme-specific profiles Link: PRIAM 4.99.1.7
IntEnz Enzyme Link: IntEnz 4.99.1.7
MEDLINE Enzyme Link: MEDLINE 4.99.1.7

EC number:4.99.1.7

MSA:

4.99.1.7;
Phylogenetic Tree:

4.99.1.7;
Uniprot:
M-CSA:
RHEA:20069 (Z)-phenylacetaldehyde oxime = H2O + phenylacetonitrile
RULE(radius=1) [*:1]-[CH;+0:2]=[N;H0;+0:3]-[OH;+0:4]>>[*:1]-[C;H0;+0:2]#[N;H0;+0:3].[OH2;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Identification and characterization of CYP79D16 and CYP71AN24 catalyzing the first and second steps in L-phenylalanine-derived cyanogenic glycoside biosynthesis in the Japanese apricot, Prunus mume Sieb. et Zucc.Yamaguchi T, Yamamoto K, Asano Y2014 Sep25015725
Regulation of aldoxime dehydratase activity by redox-dependent change in the coordination structure of the aldoxime-heme complex.Kobayashi K, Yoshioka S, Kato Y, Asano Y, Aono S2005 Feb 1815596434
Novel heme-containing lyase, phenylacetaldoxime dehydratase from Bacillus sp. strain OxB-1: purification, characterization, and molecular cloning of the gene.Kato Y, Nakamura K, Sakiyama H, Mayhew SG, Asano Y2000 Feb 110651646