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Appl Environ Microbiol. 1989 July; 55(7): 1717-1723
Copyright © 1989, American Society for Microbiology. All Rights Reserved.

Isolation and Characterization of Aminopeptidase-Deficient Lactobacillus bulgaricus Mutants

Danièle Atlan*, Patrick Laloi and Raymond Portalier

Laboratoire de Microbiologie et Génétique Moléculaire (UMR 106), Bât. 405, Université Claude Bernard-Lyon I, F-69622 Villeurbanne Cedex, France

ABSTRACT

Lactobacillus bulgaricus CNRZ 397 is able to hydrolyze many amino-acyl- and dipeptidyl-ß-naphthylamides. Analysis of heat inactivation kinetics, protease inhibitor effects, and the subcellular location of aminopeptidase (AP) activities from the parental strain and mutant derivatives dificient in alanyl- or leucyl-ß-naphthylamide hydrolysis pointed out the existence of four APs. All mutants isolated were totally deficient in AP II, a cell wall metallo-enzyme with a broad substrate specificity but that is specifically responsible for lysyl-AP activity and is characterized by a molecular mass of 95,000 daltons. AP I and AP III are cytoplasmic enzymes that exhibit arginyl-AP activity; both enzymes are inducible during growth in rich peptide MRS medium (Difco Laboratories, Detroit, Mich.). The existence of a fourth AP (AP IV) that is involved in leucyl-AP activity was suggested. Moreover, we showed that X-prolyl-dipeptidyl-AP activity, which was not catalyzed by an AP, involved an enzyme(s) that is controlled by a regulatory mechanism that is common to that of AP II.

FOOTNOTES

* Corresponding author.

Appl Environ Microbiol. 1989 July; 55(7): 1717-1723
Copyright © 1989, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Chervaux, C., Ehrlich, S. D., Maguin, E. (2000). Physiological Study of Lactobacillus delbrueckii subsp. bulgaricus Strains in a Novel Chemically Defined Medium. Appl. Environ. Microbiol. 66: 5306-5311 [Abstract] [Full Text]  
  • Chavagnat, F., Casey, M. G., Meyer, J. (1999). Purification, Characterization, Gene Cloning, Sequencing, and Overexpression of Aminopeptidase N from Streptococcus thermophilus A. Appl. Environ. Microbiol. 65: 3001-3007 [Abstract] [Full Text]  


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