|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 188.8.131.52
Enzymes and Genes:
|Rhodococcus rhodochrous :||aliphatic nitrilase
In Pathway: acrylonitrile degradation II
Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Mass balance status: Balanced.
Enzyme Commission Primary Name: aliphatic nitrilase
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -3.7801266 [Latendresse13]
The enzyme preferentially hydrolyses aliphatic nitriles, some of which are apparently not substrates for other known nitrilases (EC 184.108.40.206). Substrates include crotononitrile, acrylonitrile and glutaronitrile.
This reaction is different from EC 220.127.116.11 in that the substrates for this reaction must be aliphatic.
Enzyme Commission Summary:
Preferentially hydrolyses aliphatic nitriles, some of which are apparently not substrates for other known nitrilases (EC 18.104.22.168). Substrates include crotononitrile, acrylonitrile and glutaronitrile.
Unification Links: KEGG:R05358
Kobayashi92: Kobayashi M, Yanaka N, Nagasawa T, Yamada H (1992). "Primary structure of an aliphatic nitrile-degrading enzyme, aliphatic nitrilase, from Rhodococcus rhodochrous K22 and expression of its gene and identification of its active site residue." Biochemistry 1992;31(37);9000-7. PMID: 1390687
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