Inhibition of Streptomyces griseus aminopeptidase and effects of calcium ions on catalysis and binding - Comparisons with the homologous enzyme Aeromonas proteolytica aminopeptidase

Galia Papir, Anya Spungin-Bialik, Daniella Ben-Meir, Ella Fudim, Rotem Gilboa, Harry M. Greenblatt, Gil Shoham, Uta Lessel, Dietmar Schomburg, Ruth Ashkenazi, Shmaryahu Blumberg*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

27 Scopus citations

Abstract

Streptomyces griseus aminopeptidase is a zinc metalloenzyme containing 2 mol zinc/mol protein, similar to the homologous enzyme Aeromonas proteolytica aminopeptidase. In addition, a unique Ca2+-binding site has been identified in the Streptomyces enzyme, which is absent in the Aeromonas enzyme. Binding of Ca2+ enhances stability of the Streptomyces enzyme and modulates its activity and affinity towards substrates and inhibitors in a structure- dependent manner. Among the three hydrophobic 4-nitroanilides of alanine, valine and leucine, the latter displays the largest overall activation (increase in k(cat)/K(m)). Large enhancements in affinity (1/K(i)) upon Ca2+ binding have been observed for inhibitors with flexible (leucine- like) residues at their N-termini and smaller enhancements for inhibitors with rigid (phenylalanine-like) residues.

Original languageAmerican English
Pages (from-to)313-319
Number of pages7
JournalEuropean Journal of Biochemistry
Volume258
Issue number2
DOIs
StatePublished - 1 Dec 1998

Keywords

  • Aeromonas proteolytica
  • Aminopeptidase
  • Calcium modulation
  • Double-zinc metalloenzyme
  • Streptomyces griseus

Fingerprint

Dive into the research topics of 'Inhibition of Streptomyces griseus aminopeptidase and effects of calcium ions on catalysis and binding - Comparisons with the homologous enzyme Aeromonas proteolytica aminopeptidase'. Together they form a unique fingerprint.

Cite this