Summary for clan MF
| Clan type peptidase | M17.001 - leucyl aminopeptidase 3 (Bos taurus), MEROPS Accession MER0001235 (peptidase unit: 33-519); PDB accession 1BLL |
| History | PEPTIDAS.TXT (SwissProt document) |
| Description | Water nucleophile; water bound by two zinc ions ligated by Lys, Asp, Asp, Asp, Glu |
| Contents of clan | Clan MF contains only family M17, the peptidases in which are predominantly aminopeptidases. |
| Evidence | The C-terminal domain of leucyl aminopeptidase (M17.001), which contains the active site, shows some structural resemblance to carboxypeptidase A (family M14) and peptidases from families M20 and M28; the four families are therefore suggested to be homologous (Artymiuk et al., 1992). It is unlikely that the common ancestor was a metallopeptidase, however, because the positions of the metal ligands are not conserved between families. Peptidase activity is assumed to have evolved independently in each family. For this reason, family M17 is placed in its own clan (MF), separate from family M14 (in clan MC) and families M20 and M28 (both in clan MH). |
| Protein fold | The structure of leucyl aminopeptidase was determined by Burley et al., 1990 and shows two structural domains, the C-terminal of which contains the active site. The N-terminal domain is an alpha/beta/alpha sandwich, with a six-stranded beta sheet (in the order 165243, with strand 3 antiparallel to the rest). The C-terminal domain also contains an alpha/beta/alpha sandwich with a five-stranded beta sheet (in the order 21354, with strand 4 antiparallel to the rest) and shows some similarites to the structures of peptidases in clans MC and MH, but the positions of the metal ligands are not conserved between the clans. |
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Other databases
| PFAM | CL0035 |
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| SCOP | 53187 |
Families
| M17 |
leucyl aminopeptidase 3 (Bos taurus) |
Yes |
Distribution of clan MF among Kingdoms of Organisms
