From Wikipedia, the free encyclopedia
aliphatic nitrilase
Identifiers
EC no. 3.5.5.7
CAS no. 9024-90-2
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

In enzymology, an aliphatic nitrilase also known as aliphatic nitrile aminohydrolase ( EC 3.5.5.7) is an enzyme that catalyzes the hydrolysis of nitriles to carboxylic acids:

R-CN + 2 H2O R-COOH + NH3

Thus, the two substrates of this enzyme are an aliphatic nitrile (R-CN) and H2O, whereas its two products are a carboxylic acid (R-COOH) and NH3.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in nitriles. This enzyme participates in styrene degradation.

References

* 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. 31 (37): 9000–7. doi: 10.1021/bi00152a042. PMID  1390687.


From Wikipedia, the free encyclopedia
aliphatic nitrilase
Identifiers
EC no. 3.5.5.7
CAS no. 9024-90-2
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

In enzymology, an aliphatic nitrilase also known as aliphatic nitrile aminohydrolase ( EC 3.5.5.7) is an enzyme that catalyzes the hydrolysis of nitriles to carboxylic acids:

R-CN + 2 H2O R-COOH + NH3

Thus, the two substrates of this enzyme are an aliphatic nitrile (R-CN) and H2O, whereas its two products are a carboxylic acid (R-COOH) and NH3.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in nitriles. This enzyme participates in styrene degradation.

References

* 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. 31 (37): 9000–7. doi: 10.1021/bi00152a042. PMID  1390687.



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