| Name | Peptidase family M35 (deuterolysin family) |
|---|
| Family type peptidase | M35.002 - deuterolysin (Aspergillus flavus), MEROPS Accession MER0001394 (peptidase unit: 194-381) |
| Content of family | Peptidase family M35 contains fungal metalloendopeptidases. |
| History |
Identifier created: Proteolysis in Cell Function, pp13-21, IOS Press, Amsterdam (1997)
Penicillolysin (M35.001), deuterolysin (M35.002) and peptidyl-Lys metalloendopeptidase (M35.004) have been reviewed (Ichishima, 2004; Tatsumi, 2004; Takio, 2004). |
| Catalytic type | Metallo |
| Active site residues | H321 E322 H325 D336 |
| Active site | Family M35 members contain two zinc binding histidines and a catalytic glutamate in an HEXXH motif. There is a third zinc ligand, an Asp, found in a GTXDXXYG motif C-terminal to the His zinc ligands (see the Alignment). For this reason the peptidases in this family are sometimes termed 'aspzincins', although peptidases in which the third ligand of zinc is Asp also occur in families M6, M7 and M64. |
| Activities and specificities | Deuterolysin (M35.002) and penicillolysin (M35.001) have both been found to be especially active on basic protein substrates such as histones, protamine and salmine (Doi et al., 2003; Ichishima, 2004). A basic residue, Arg or Lys, is commonly prefered in the P1" subsite, and is required by the very selective peptidyl-Lys metalloendopeptidase (M35.004), which cleaves Xaa Lys bonds, in which Xaa can even be Pro. |
| Inhibitors | Chelating agents such as 1,10-phenanthroline inhibit. |
| Molecular structure | The tertiary structure of peptidyl-Lys metalloendopeptidase contains five alpha helices and four beta strands (Hori et al., 2001). It is reported that the conserved tyrosine, three residues C-terminal to the zinc-binding Asp, acts as a proton donor during catalysis (Hori et al., 2001). The structure of deuterolysin was determined by McAuley et al. (2001). There is no conserved methionine in the "Met-turn" in family M35 unlike other families of subclan MA(M) in clan MA. |
| Clan | MA |
| Subclan | MA(D) |
| Basis of clan assignment | Protein fold of the peptidase unit for members of this family resembles that of thermolysin, the type example for clan MA. |
