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http://www.biopax.org/relea... | |
http://www.biopax.org/relea... |
Vacuolar aminopeptidase 1
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http://www.biopax.org/relea... |
AMPL_YEAST
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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
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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.
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