Pseudomonas aeruginosa aliphatic amidase is related to the nitrilase/cyanide hydratase enzyme family and Cys166 is predicted to be the active site nucleophile of the catalytic mechanism.
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 Cys166 is the active site nucleophile.
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Instituto Nacional de Engenharia e Tecnologia Industrial/IBQTA, Queluz, Portugal.
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Clemente
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Brown
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D000581:Amidohydrolases / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D000619:Aminohydrolases / Q000737:chemistry; D001665:Binding Sites; D003545:Cysteine / Q000737:chemistry; D006836:Hydro-Lyases / Q000737:chemistry; D008969:Molecular Sequence Data; D010802:Phylogeny; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D000581:Amidohydrolases; C019665:amidase; D000619:Aminohydrolases; C021867:nitrilase; D006836:Hydro-Lyases; C076848:cyanide hydratase; D003545:Cysteine