Literature DB >> 3108029

The amino acid sequence of the aliphatic amidase from Pseudomonas aeruginosa.

R P Ambler, A D Auffret, P H Clarke.   

Abstract

Amino acid sequence studies show that the aliphatic amidase (EC 3.5.1.4) from Pseudomonas aeruginosa PAC142 consists of a single polypeptide chain of 346 residues, giving an Mr of 38,400. The evidence from the amino acid studies is in complete agreement with that deduced from the DNA sequence of the amiE gene. Studies of the protein from Pseudomonas putida A87 show that it differs from the Ps. aeruginosa protein by about 30 amino acid substitutions. It now becomes possible to relate changes in the enzyme which result in altered specificity to structural changes in the protein.

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Year:  1987        PMID： 3108029     DOI： 10.1016/0014-5793(87)80163-1

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  11 in total

1.  N-terminal amino acid sequence of Brevibacterium sp. R312 wide-spectrum amidase.

Authors:  C K Chion; R Duran; A Arnaud; P Galzy
Journal:  Appl Microbiol Biotechnol       Date:  1991-11       Impact factor: 4.813

2.  The quaternary structure of the amidase from Geobacillus pallidus RAPc8 is revealed by its crystal packing.

Authors:  Vinod B Agarkar; Serah W Kimani; Donald A Cowan; Muhammed F-R Sayed; B Trevor Sewell
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2006-11-04

3.  Unique aliphatic amidase from a psychrotrophic and haloalkaliphilic nesterenkonia isolate.

Authors:  A J M Nel; I M Tuffin; B T Sewell; D A Cowan
Journal:  Appl Environ Microbiol       Date:  2011-04-15       Impact factor: 4.792

4.  Evidence that cysteine-166 is the active-site nucleophile of Pseudomonas aeruginosa amidase: crystallization and preliminary X-ray diffraction analysis of the enzyme.

Authors:  S Farnaud; R Tata; M K Sohi; T Wan; P R Brown; B J Sutton
Journal:  Biochem J       Date:  1999-06-15       Impact factor: 3.857

5.  Support for a three-dimensional structure predicting a Cys-Glu-Lys catalytic triad for Pseudomonas aeruginosa amidase comes from site-directed mutagenesis and mutations altering substrate specificity.

Authors:  Carlos Novo; Sebastien Farnaud; Renée Tata; Alda Clemente; Paul R Brown
Journal:  Biochem J       Date:  2002-08-01       Impact factor: 3.857

6.  Purification and Characterization of an Enantioselective Amidase from Pseudomonas chlororaphis B23.

Authors:  L M Ciskanik; J M Wilczek; R D Fallon
Journal:  Appl Environ Microbiol       Date:  1995-03       Impact factor: 4.792

7.  Cloning and DNA sequence of amiC, a new gene regulating expression of the Pseudomonas aeruginosa aliphatic amidase, and purification of the amiC product.

Authors:  S Wilson; R Drew
Journal:  J Bacteriol       Date:  1991-08       Impact factor: 3.490

8.  Cloning and heterologous expression of an enantioselective amidase from Rhodococcus erythropolis strain MP50.

Authors:  Sandra Trott; Sibylle Bürger; Carsten Calaminus; Andreas Stolz
Journal:  Appl Environ Microbiol       Date:  2002-07       Impact factor: 4.792

Review 9.  The nitrilase superfamily: classification, structure and function.

Authors:  H C Pace; C Brenner
Journal:  Genome Biol       Date:  2001-01-15       Impact factor: 13.583

10.  Comparative analysis of amino acid sequences from mesophiles and thermophiles in respective of carbon-nitrogen hydrolase family.

Authors:  Sarita Devi; Nikhil Sharma; Tek Chand Bhalla
Journal:  3 Biotech       Date:  2013-01-16       Impact factor: 2.406
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