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PMID: 7957888 Published · ppublish English Journal Article Review

Families of zinc metalloproteases.

FEBS letters ·Vol. 354 ·No. 1 ·1994-10-31 ·Pages 1-6

Hooper NM

Abstract

A scheme based on the zinc binding site [1992, FEBS Lett. 312, 110-114] has been extended to classify zinc metalloproteases into distinct families. The gluzincins, defined by the HEXXH motif and a glutamic acid as the third zinc ligand, include the thermolysin, endopeptidase-24.11, aminopeptidase, angiotensin converting enzyme, endopeptidase-24.15, and tetanus and botulinum neurotoxin families. The metzincins, defined by the HEXXH motif, a histidine as the third zinc ligand and a Met-turn, include the astacin, serralysin, reprolysin and matrixin families. The inverted zincin motif, HXXEH, defines the inverzincin family of insulin-degrading enzymes, the HXXE motif defines the carboxypeptidase family, and the HXH motif DD-carboxypeptidase.

MeSH Terms
Amino Acid Sequence Animals Consensus Sequence Humans Metalloendopeptidases/chemistry,genetics,metabolism Molecular Sequence Data Zinc/metabolism
Chemicals
Metalloendopeptidases Zinc
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Hooper N M
Department of Biochemistry and Molecular Biology, University of Leeds, UK.
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1994-10-31
Pages
1-6
Language
English
Region
England
NLM ID
0155157
Subset
IM
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