Family M72
Summary for family M72
| Family type peptidase | M72.001 - peptidyl-Asp metallopeptidase (Pseudomonas aeruginosa), MEROPS Accession MER0022935 (peptidase unit: 27-267) |
| Content of family | Family M72 contains metallo-endopeptidases. |
| History |
Identifier created: MEROPS 6.3 (23 June 2003)
Although peptidyl-Asp metalloendopeptidase (M72.001) from Pseudomonas fragi has been known for many years, only fragments of amino acid sequence had been determined. The sequencing of two Xanthomonas genomes established the first complete sequence of a member of family M72. |
| Catalytic type | Metallo |
| Active site residues | H167 E168 H171 H177 |
| Active site | One zinc ion is predicted to be bound by three histidine residues within the motif HEXXHXXGXXH, and the glutamate is assumed to be a catalytic residue. |
| Activities and specificities | Peptidyl-Asp metalloendopeptidase has a restricted specificity, cleaving peptide bonds at the amino side of aspartate or cysteic acid (Drapeau, 1980). Cleavage at the amino side of glutamate can occur under certain conditions (Ingrosso et al., 1989; Tetaz et al., 1990). A similar specificity is shown by flavastacin (M12.066) from Flavobacterium meningosepticum. |
| Inhibitors | Metal chelators such as 1,10-phenanthroline, EDTA and EGTA are effective inhibitors. |
| Molecular structure | Peptidyl-Asp metalloendopeptidase is a secreted enzyme and is synthesized with an N-terminal signal peptide. The peptidase unit is the N-terminal half of the mature protein; the C-terminal half contains two carbohydrate binding domains. |
| Clan | MA |
| Subclan | MA(M) |
| Basis of clan assignment | Predicted active site residues for members of this family and thermolysin, the type example for clan MA, occur in the motif HEXXH |
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Distribution of family
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