J Biol Chem. 2009 Jun 5;284(23):15353-7. doi: 10.1074/jbc.R800069200. Epub 2009 Feb 5.Catalytic domain architecture of metzincin metalloproteases.
Gomis-Rüth FX1. Abstract
Metalloproteases
cleave proteins and peptides, and deregulation of their function leads
to pathology. An understanding of their structure and mechanisms of
action is necessary to the development of strategies for their
regulation. Among metallopeptidases are the metzincins, which are mostly
multidomain proteins with approximately 130-260-residue globular
catalytic domains showing a common core architecture characterized by a
long zinc-binding consensus motif, HEXXHXXGXX(H/D), and a
methionine-containing Met-turn.
Metzincins participate in unspecific protein degradation such as digestion of intake proteins and tissue development, maintenance, and remodeling, but they are also involved in highly specific cleavage events to activate or inactivate themselves or other (pro)enzymes and bioactive peptides. Metzincins are subdivided into families, and seven such families have been analyzed at the structural level:
the astacins,
ADAMs/adamalysins/reprolysins,
serralysins,
matrix metalloproteinases,
snapalysins,
leishmanolysins, and
pappalysins.
These families are reviewed from a structural point of view.
Metzincins participate in unspecific protein degradation such as digestion of intake proteins and tissue development, maintenance, and remodeling, but they are also involved in highly specific cleavage events to activate or inactivate themselves or other (pro)enzymes and bioactive peptides. Metzincins are subdivided into families, and seven such families have been analyzed at the structural level:
the astacins,
ADAMs/adamalysins/reprolysins,
serralysins,
matrix metalloproteinases,
snapalysins,
leishmanolysins, and
pappalysins.
These families are reviewed from a structural point of view.
- [Indexed for MEDLINE]
- 2020 katson uusinta tietoa serralysiineistä.
- 2013 tietoa
Serralysin and Related Enzymes
Ulrich Baumann, in Handbook of Proteolytic Enzymes (Third Edition), 2013
Name and History
Serralysin was first discovered in the culture medium of Serratia sp. E-15 [1] and was named from the genus name Serratia+lysin. Similar proteases have been found to be secreted by other Gram-negative bacteria, e.g. Pseudomonas aeruginosa [2] and Erwinia chrysanthemi [3–6], Ps. fluorescens [7,8], or Photorhabdus luminescens [9]. These proteases are quite similar in their physicochemical properties and are grouped together in the serralysin subfamily. Later, it was established on evidence from three-dimensional structures that serralysins, together with matrix metalloproteases, astacins and snake venom proteinases, belong to clan MA (the metzincins) [10].
