Enzyme

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EC Tree
     4. Lyases
        4.1 Carbon-carbon lyases
            4.1.2 Aldehyde-lyases
ID:4.1.2.46
Description:Aliphatic (R)-hydroxynitrile lyase.
Alternative Name: (R)-oxynitrilase.
(R)-hydroxynitrile lyase.
Cath: 1.20.5.2390; 3.40.50.11320; 3.40.50.1820;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.1.2.46
BRENDA Enzyme Link: BRENDA 4.1.2.46
KEGG Enzyme Link: KEGG4.1.2.46
BioCyc Enzyme Link: BioCyc 4.1.2.46
ExPASy Enzyme Link: ExPASy4.1.2.46
EC2PDB Enzyme Link: EC2PDB 4.1.2.46
ExplorEnz Enzyme Link: ExplorEnz 4.1.2.46
PRIAM enzyme-specific profiles Link: PRIAM 4.1.2.46
IntEnz Enzyme Link: IntEnz 4.1.2.46
MEDLINE Enzyme Link: MEDLINE 4.1.2.46
MSA:

4.1.2.46;

Phylogenetic Tree:

4.1.2.46;

Uniprot:
M-CSA:
RHEA:28170 (2R)-2-hydroxy-2-methylbutanenitrile = butan-2-one + hydrogen cyanide
RULE(radius=1) [*:1]#[C;H0;+0:2]-[C;H0;+0:3](-[*:4])(-[*:5])-[OH;+0:6]>>[*:1]#[CH;+0:2].[*:4]-[C;H0;+0:3](-[*:5])=[O;H0;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Molecular cloning of acetone cyanohydrin lyase from flax (Linum usitatissimum). Definition of a novel class of hydroxynitrile lyases.Trummler K, Wajant H1997 Feb 219030531
Purification and characterization of acetone cyanohydrin lyase from Linum usitatissimum.Xu LL, Singh BK, Conn EE1988 Jun3377504