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Appl Environ Microbiol. 1990 July; 56(7): 2174-2179
Copyright © 1990, American Society for Microbiology. All Rights Reserved.

X-Prolyl-Dipeptidyl Aminopeptidase of Lactobacillus delbrueckii subsp. bulgaricus: Characterization of the Enzyme and Isolation of Deficient Mutants

Danièle Atlan*, Patrick Laloi and Raymond Portalier

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

ABSTRACT

Lactobacillus delbrueckii subsp. bulgaricus CNRZ 397 is able to hydrolyze X-proline-para-nitroanilides and X-proline-ß-naphthylamides (X for alanyl- or glycyl-). A single metal-independent cytoplasmic enzyme with a molecular weight estimated to be 82,000 is responsible for these activities and was named X-prolyl-dipeptidyl aminopeptidase (X-Pro-DPAP). Isolation and analysis of mutants totally deficient for X-Pro-DPAP activity showed that a total lack of this enzyme induces (i) a decrease in the growth rate; (ii) an increase in cell wall proteinase activity; (iii) the loss of three cell wall proteins with respective molecular masses of 16, 40, and 52 kilodaltons; and (iv) enhancement of a cell wall protein with a molecular mass of 150 kilodaltons. The involvement of X-Pro-DPAP in casein catabolism is discussed.

FOOTNOTES

* Corresponding author.

Appl Environ Microbiol. 1990 July; 56(7): 2174-2179
Copyright © 1990, American Society for Microbiology. All Rights Reserved.



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Copyright © 1990 by the American Society for Microbiology. All rights reserved.