Literature DB >> 1628849

Cloning and primary structure of the wide-spectrum amidase from Brevibacterium sp. R312: high homology to the amiE product from Pseudomonas aeruginosa.

F Soubrier1, S Lévy-Schil, J F Mayaux, D Pétré, A Arnaud, J Crouzet.   

Abstract

A Brevibacterium sp. R312 DNA fragment encoding the wide-spectrum amidase (EC 3.5.1.4) has been cloned and sequenced, using limited amino acid (aa) sequence information obtained from the purified enzyme. The deduced aa sequence showed more than 80% strict identity with the Pseudomonas aeruginosa aliphatic amidase, the product of the amiE gene, suggesting a horizontal transfer of the gene during evolution between Gram+ and Gram- bacteria.

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Year:  1992        PMID： 1628849     DOI： 10.1016/0378-1119(92)90635-3

Source DB:  PubMed          Journal:  Gene        ISSN： 0378-1119            Impact factor:   3.688


  9 in total

1.  Purification and properties of an amidase from Rhodococcus erythropolis MP50 which enantioselectively hydrolyzes 2-arylpropionamides.

Authors:  B Hirrlinger; A Stolz; H J Knackmuss
Journal:  J Bacteriol       Date:  1996-06       Impact factor: 3.490

2.  Characterization of the Rhodococcus sp. NI86/21 gene encoding alcohol: N,N'-dimethyl-4-nitrosoaniline oxidoreductase inducible by atrazine and thiocarbamate herbicides.

Authors:  I Nagy; S Verheijen; A De Schrijver; J Van Damme; P Proost; G Schoofs; J Vanderleyden; R De Mot
Journal:  Arch Microbiol       Date:  1995-06       Impact factor: 2.552

3.  Sizing of the Rhodococcus sp. R312 genome by pulsed-field gel electrophoresis. Localization of genes involved in nitrile degradation.

Authors:  F Bigey; G Janbon; A Arnaud; P Galzy
Journal:  Antonie Van Leeuwenhoek       Date:  1995-08       Impact factor: 2.271

4.  Purification and characterization of an amidase from an acrylamide-degrading Rhodococcus sp.

Authors:  M S Nawaz; A A Khan; J E Seng; J E Leakey; P H Siitonen; C E Cerniglia
Journal:  Appl Environ Microbiol       Date:  1994-09       Impact factor: 4.792

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.  Subdivision of Burkholderia pseudomallei ribotypes into multiple types by random amplified polymorphic DNA analysis provides new insights into epidemiology.

Authors:  A Haase; H Smith-Vaughan; A Melder; Y Wood; A Janmaat; J Gilfedder; D Kemp; B Currie
Journal:  J Clin Microbiol       Date:  1995-07       Impact factor: 5.948

7.  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

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

9.  New nucleotide sequence data on the EMBL File Server.

Authors: 
Journal:  Nucleic Acids Res       Date:  1992-11-11       Impact factor: 16.971
  9 in total

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