Families of metalloendopeptidases and their relationships

• Published in: FEBS Letters Vol. 312; no. 2; pp. 110 - 114
• Main Authors: Jiang, Weiping, Bond, Judith S.
• Format: Book Review Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 09.11.1992; Elsevier
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Astacin family; Bacterial neutral protease; Biological and medical sciences; Collagenase; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Humans; Hydrolases; Metalloendopeptidase; Metalloendopeptidases - chemistry; Metalloendopeptidases - metabolism; Molecular Sequence Data; Sequence Homology, Amino Acid; Snake venom metalloproteinase; Zinc - metabolism; Zinc ligand; Metalloendopeptidase; Snake venom metalloproteinase; Collagenase; Bacterial neutral protease; Zinc ligand; Astacin family; Enzyme; Sequence alignment; Classification; Metalloproteinase; Binding site; Review; Aminoacid sequence; Zinc
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(92)80916-5

Crystal structures available for four metalloendopeptidases have revealed zinc ligands for these enzymes. New sequence information has made it possible to compare the primary structures of the zinc-binding site in metalloendopeptidases. A scheme based on the zinc-binding site is proposed to classify metalloendopeptidases into five distinct families: thermolysin, astacin, serratia, matrixin, and snake venom metalloproteinases. Two histidines and one glutamate are zinc-ligands in the thermolysin family. Three histidines and one tyrosine are zinc ligands in other four families, which are further distinguished by the identity of the residue following the third histidine and by the environment surrounding the tyrosine.