Regulation of the activity of intracellular alanylaminopeptidase synthesized by Pseudomonas sp.

Abstract:

:Activity of purified alanylaminopeptidase of Pseudomonas sp. measured in the presence of the alanine derivative of 2-naphthoic acid (NA-Ala) is inhibited by 1,10-phenanthroline, EDTA, bestatin and amastatin; this finding supports the conclusion that this enzyme is a metallo-aminopeptidase. A decrease of its activity in the presence of iodoacetamide and its activation by thiols points to the significant role of -SH groups in the regulation of its activity. Co2+, Ca2+ and Mg2+ ions increased the enzyme activity while Zn2+, Cd2+ and Pb2+ markedly inhibited the enzyme even at low concentrations. A high thermal stability of alanylaminopeptidase depended on the presence of 1 mmol/L Co2+ and of 1 mmol/L L-cysteine in the incubation mixture.

journal_title

Folia microbiologica

authors

Jankiewicz U,Bielawski W

doi

10.1007/BF02817643

keywords:

subject

Has Abstract

pub_date

2002-01-01 00:00:00

pages

230-4

issue

3

eissn

0015-5632

issn

1874-9356

journal_volume

47

pub_type

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