Families of zinc metalloproteases

1994/10/31 by Nigel M. Hooper · 791 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Health Professions · Medicine · #Amino acid #Aminopeptidase #Biochemistry #Carboxypeptidase #Carboxypeptidase A #Chemistry #Endopeptidase #Enzyme #Metalloproteinase #Oral and gingival health research #Peptidase Inhibition and Analysis #Signaling Pathways in Disease #Thermolysin #Trypsin #Zinc

paper · doi:10.1016/0014-5793(94)01079-x

published in FEBS Letters 354(1), 1-6 (Wiley)

openalex publication_date 1994/10/31 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/30

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.

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