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

FEBS Letters

Brown, Paul R.²  Novo, Carkos¹  Clemente, Alda¹  Tata, Renée² 

[1] Instituto Nacional de Engenharia e Tecnologia Industrial/IBQTA, Queluz de Baixo, 2745 Queluz, Portugal;Molecular Biology and Biophysics Section, Division of Biomedical Sciences, King's College London, Strand, London WC2R 2LS, UK

关键词: Amidase;    Nitrilase;    Phylogenetic tree;    Active site prediction;    Pseudomonas aeruginosa;    Rhodococcus erythropolis;    PDOC;    Prosite documentation;    PS;    PROSITE;    PAM probability matrix;    corresponds to one accepted amino acid substitution per hundred sites;   

DOI  :  10.1016/0014-5793(95)00585-W

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown