Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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MetaCyc Reaction: 3.5.5.7

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 3.5.5.7

Enzymes and Genes:
aliphatic nitrilase Inferred from experiment ( Rhodococcus rhodochrous )

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 Inferred by computational analysis [Latendresse13]

Summary:
The enzyme preferentially hydrolyses aliphatic nitriles, some of which are apparently not substrates for other known nitrilases (EC 3.5.5.1). Substrates include crotononitrile, acrylonitrile and glutaronitrile.

This reaction is different from EC 3.5.5.1 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 3.5.5.1). Substrates include crotononitrile, acrylonitrile and glutaronitrile.

Citations: [Kobayashi92, Pace01]

Gene-Reaction Schematic: ?

Unification Links: KEGG:R05358

Relationship Links: BRENDA:EC:3.5.5.7 , ENZYME:EC:3.5.5.7 , IUBMB-ExplorEnz:EC:3.5.5.7


References

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

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Pace01: Pace HC, Brenner C (2001). "The nitrilase superfamily: classification, structure and function." Genome Biol 2(1);REVIEWS0001. PMID: 11380987


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, biocyc14.