Families of zinc metalloproteases

1994/10/31 by Nigel M. Hooper · 28 citations
Medicine · Health Professions · Biochemistry, Genetics and Molecular Biology · #Peptidase Inhibition and Analysis #Oral and gingival health research #Signaling Pathways in Disease

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

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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