| Autor: |
NOVO, Carlos, FARNAUD, Sebastien, TATA, Renée, CLEMENTE, Alda, BROWN, Paul R. |
| Zdroj: |
Biochemical Journal; August 2002, Vol. 365 Issue: 3 p731-738, 8p |
| Abstrakt: |
The aliphatic amidase from Pseudomonas aeruginosa belongs to the nitrilase superfamily, and Cys166 is the nucleophile of the catalytic mechanism. A model of amidase was built by comparative modelling using the crystal structure of the worm nitrilase—fragile histidine triad fusion protein (NitFhit; Protein Data Bank accession number 1EMS) as a template. The amidase model predicted a catalytic triad (Cys-Glu-Lys) situated at the bottom of a pocket and identical with the presumptive catalytic triad of NitFhit. Three-dimensional models for other amidases belonging to the nitrilase superfamily also predicted Cys-Glu-Lys catalytic triads. Support for the structure for the P. aeruginosa amidase came from site-direct mutagenesis and from the locations of amino acid residues that altered substrate specificity or binding when mutated. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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