Statements in which the resource exists as a subject.
PredicateObject
rdf:type
http://www.biopax.org/relea...
http://www.biopax.org/relea...
Vacuolar aminopeptidase 1
http://www.biopax.org/relea...
AMPL_YEAST
http://www.biopax.org/relea...
http://www.biopax.org/relea...
3.4.11.22, Aminopeptidase III, Aminopeptidase yscI, LAPIV, Leucine aminopeptidase IV, Polypeptidase, Vacuolar aminopeptidase I
http://www.biopax.org/relea...
FUNCTION: This vacuolar enzyme catalyzes the removal of amino acids from the N-terminus of peptides and proteins. CATALYTIC ACTIVITY: Release of an N-terminal amino acid, preferably a neutral or hydrophobic one, from a polypeptide. Aminoacyl-arylamides are poor substrates. COFACTOR: Binds 1 zinc ion per subunit. ENZYME REGULATION: Inactivated by metal-chelating agents and specifically activated by Zn(2+) and Cl(-). SUBUNIT: Homododecamer. SUBCELLULAR LOCATION: Vacuole. PTM: After a zymogenic synthesis this vacuolar peptidase might be processed by proteinase yscA (PEP4). MISCELLANEOUS: Present with 5730 molecules/cell in log phase SD medium. SIMILARITY: Belongs to the peptidase M18 family. GENE SYNONYMS: APE1 API YSC1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
skos:exactMatch
skos:closeMatch