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Pseudomonas aeruginosa aliphatic amidase is related to the nitrilase/cyanide hydratase enzyme family and Cys 166 is predicted to be the active site nucleophile of the catalytic mechanism
Author(s) -
Novo Carkos,
Tata Renée,
Clemente Alda,
Brown Paul R.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00585-w
Subject(s) - nitrilase , amidase , nitrile hydratase , chemistry , nucleophile , cyanide , enzyme , catalysis , active site , stereochemistry , pseudomonas , biochemistry , organic chemistry , bacteria , biology , genetics
A database search indicated homology between some members of the nitrilase/cyanide hydratase family, Pseudomonas aeruginosa and Rhodococcus erythropolis amidases and several other proteins, some of unknown function. BLOCK and PROFILE searches confirmed these relationships and showed that four regions of the P. aeruginosa amidase had significant homology with corresponding regions of nitrilases. A phylogenetic tree placed the P. aeruginosa and R. erythropolis amidases in a group with nitrilases but separated other amidases into three groups. The active site cysteine in nitrilases is conserved in the P. aeruginosa amidase indicating that Cys 166 is the active site nucleophile.