Regulation of the activity of intracellular alanylaminopeptidase synthesized by Pseudomonas sp.
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.
Jankiewicz
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U
Department of Biochemistry, Warsaw Agricultural University, 02-528 Warsaw, Poland. jankiewicz@delta.sggw.waw.pl
Bielawski
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W
D018826:CD13 Antigens / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003545:Cysteine; D004795:Enzyme Stability; D015964:Gene Expression Regulation, Bacterial; D006863:Hydrogen-Ion Concentration; D011549:Pseudomonas / Q000201:enzymology* / Q000378:metabolism; D013696:Temperature
D018826:CD13 Antigens; D003545:Cysteine