Literature DB >> 157234

[Spectrum of amidase activity in a mutant of Brevibacterium].

J C Jallageas, A Arnaud, P Galzy.   

Abstract

Brevibacterium R 312 has a fairly non-specific amidase. Following the loss of this enzyme by mutation, the following enzymatic activities could be demonstrated: hydrolysis of urea, formamide, nicotinamide, L-glutamine, glycinamide and L-alpha-amino amids.

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Year:  1979        PMID: 157234

Source DB:  PubMed          Journal:  C R Seances Acad Sci D        ISSN: 0567-655X


  2 in total

1.  Purification, cloning, and primary structure of an enantiomer-selective amidase from Brevibacterium sp. strain R312: structural evidence for genetic coupling with nitrile hydratase.

Authors:  J F Mayaux; E Cerebelaud; F Soubrier; D Faucher; D Pétré
Journal:  J Bacteriol       Date:  1990-12       Impact factor: 3.490

2.  Regulation of nitrile-hydratase synthesis in a Brevibacterium species.

Authors:  D Tourneix; A Thiéry; M Maestracci; A Arnaud; P Galzy
Journal:  Antonie Van Leeuwenhoek       Date:  1986       Impact factor: 2.271

  2 in total

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