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:4.99.1.5
Description:Aliphatic aldoxime dehydratase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.99.1.5
BRENDA Enzyme Link: BRENDA 4.99.1.5
KEGG Enzyme Link: KEGG4.99.1.5
BioCyc Enzyme Link: BioCyc 4.99.1.5
ExPASy Enzyme Link: ExPASy4.99.1.5
EC2PDB Enzyme Link: EC2PDB 4.99.1.5
ExplorEnz Enzyme Link: ExplorEnz 4.99.1.5
PRIAM enzyme-specific profiles Link: PRIAM 4.99.1.5
IntEnz Enzyme Link: IntEnz 4.99.1.5
MEDLINE Enzyme Link: MEDLINE 4.99.1.5
MSA:

4.99.1.5;

Phylogenetic Tree:

4.99.1.5;

Uniprot:
M-CSA:
RHEA:11316 an aliphatic aldoxime = a nitrile + H2O
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
Aldoxime dehydratase co-existing with nitrile hydratase and amidase in the iron-type nitrile hydratase-producer Rhodococcus sp. N-771.Kato Y, Yoshida S, Xie SX, Asano Y200416233624
Novel aldoxime dehydratase involved in carbon-nitrogen triple bond synthesis of Pseudomonas chlororaphis B23. Sequencing, gene expression, purification, and characterization.Oinuma K, Hashimoto Y, Konishi K, Goda M, Noguchi T, Higashibata H, Kobayashi M2003 Aug 812773527