PR00932

AMINO1PTASE

PRINTS entry
Member databasePRINTS
PRINTS typefamily
Short nameAMINO1PTASE

Description
Imported from IPR001948

This group of metallopeptidases belong to the MEROPS peptidase family M18, (clan MH). The proteins have two catalytic zinc ions at the active site, bound by His/Asp, Asp, Glu, Asp/Glu and His. The catalysed reaction involves the release of an N-terminal aminoacid, usually neutral or hydrophobic, from a polypeptide
[1]
.

The type example is aminopeptidase I from Saccharomyces cerevisiae (Baker's yeast), the sequence of which has been deduced, and the mature protein shown to consist of 469 amino acids
[2]
. A 45-residue presequence contains both positively- and negatively-charged and hydrophobic residues, which could be arranged in an N-terminal amphiphilic α-helix
[2]
. The presequence differs from signal sequences that direct proteins across bacterial plasma membranes and endoplasmic reticulum or into mitochondria. It is unclear how this unique presequence targets aminopeptidase I to yeast vacuoles, and how this sorting utilises classical protein secretory pathways
[2]
.

References
Imported from IPR001948

1.Evolutionary families of metallopeptidases. Rawlings ND, Barrett AJ. Meth. Enzymol. 248, 183-228, (1995). View articlePMID: 7674922

2.Molecular cloning and sequencing of genomic DNA encoding aminopeptidase I from Saccharomyces cerevisiae. Chang YH, Smith JA. J. Biol. Chem. 264, 6979-83, (1989). View articlePMID: 2651436

Supplementary References

Integrated to
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.