Standard Article

Zinc-Dependent Metalloprotease-1 (Zmp1)

  1. Davide M Ferraris,
  2. Menico Rizzi

Published Online: 23 SEP 2013

DOI: 10.1002/9781119951438.eibc2171

Encyclopedia of Inorganic and Bioinorganic Chemistry

Encyclopedia of Inorganic and Bioinorganic Chemistry

How to Cite

Ferraris, D. M. and Rizzi, M. 2013. Zinc-Dependent Metalloprotease-1 (Zmp1). Encyclopedia of Inorganic and Bioinorganic Chemistry. 1–7.

Author Information

  1. Università del Piemonte Orientale A. Avogadro, Novara, Italy

Publication History

  1. Published Online: 23 SEP 2013

Abstract

M13 endopeptidases are single-pass, transmembrane zinc-metallopeptidases responsible for the regulation of the biological activity of many hormones and peptides in humans and are involved in many important processes such as blood pressure regulation (neprilysin or NEP), cardiovascular development (endothelin converting enzyme-1 or ECE-1), and prevention of hemolytic reaction (KELL) and phosphate homeostasis (PHEX). Zmp1 is a soluble enzyme member of the M13 endopetidases family, which plays a key role in Mycobacterium tuberculosis pathogenicity through a still to be elucidated mechanism that likely initiates on enzyme secretion.

3D Structure

  • original image

    Ribbon representation of Zmp1 structure. Red and green: α-helices; yellow: β-sheets; dark gray: loops. Phosphoramidon and N′,N″,N‴-Triethanolamine are shown in sticks. Zn2+ is shown as a blue sphere. Helices are coloured in red and green; strands in yellow; loops in dark gray. PDB code: 3ZUK. The structural figures were prepared with program PyMOL (DeLano Scientific; www.pymol.org).

Keywords:

  • hydrolase;
  • metalloprotease;
  • zinc-dependent enzymes;
  • mycobacterial M13 metalloendopeptidases;
  • Mycobacterium tuberculosis ;
  • Phagosome maturation