IPR008283
Peptidase M17, leucyl aminopeptidase, N-terminal
InterPro entry
Short name | Peptidase_M17_N |
Overlapping homologous superfamilies |
Description
This group of metallopeptidases belong to the MEROPS peptidase family M17 (leucyl aminopeptidase family, clan MF), the type example being leucyl aminopeptidase from Bos taurus (Bovine).
Over 70 metallopeptidase families have been identified to date. In these enzymes a divalent cation which is usually zinc, but may be cobalt, manganese or copper, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. In some families of co-catalytic metallopeptidases, two metal ions are observed in crystal structures ligated by five amino acids, with one amino acid ligating both metal ions. The known metal ligands are His, Glu, Asp or Lys. At least one other residue is required for catalysis, which may play an electrophillic role.
Many metalloproteases contain an HEXXH motif, which has been shown in crystallographic studies to form part of the metal-binding site
[1]. The HEXXH motif is relatively common, but can be more stringently defined for metalloproteases as 'abXHEbbHbc', where 'a' is most often valine or threonine and forms part of the S1' subsite in thermolysin and neprilysin, 'b' is an uncharged residue, and 'c' a hydrophobic residue. Proline is never found in this site, possibly because it would break the helical structure adopted by this motif in metalloproteases
[1].
References
1.Evolutionary families of metallopeptidases. Rawlings ND, Barrett AJ. Meth. Enzymol. 248, 183-228, (1995). View articlePMID: 7674922
Further reading
2. Leucine aminopeptidase from Arabidopsis thaliana. Molecular evidence for a phylogenetically conserved enzyme of protein turnover in higher plants. Bartling D, Weiler EW. Eur. J. Biochem. 205, 425-31, (1992). View articlePMID: 1555602
3. Molecular structure of leucine aminopeptidase at 2.7-A resolution. Burley SK, David PR, Taylor A, Lipscomb WN. Proc. Natl. Acad. Sci. U.S.A. 87, 6878-82, (1990). View articlePMID: 2395881
GO terms
biological process
molecular function
cellular component
- None
Cross References
Contributing Member Database Entry
- Pfam:PF02789