FUNCTION : THE PROTEASOME IS A MULTICATALYTIC PROTEINASE COMPLEX WHICH IS CHARACTERIZED BY ITS ABILITY TO CLEAVE PEPTIDES WITH ARG, PHE, TYR, LEU, AND GLU ADJACENT TO THE LEAVING GROUP AT NEUTRAL OR SLIGHTLY BASIC PH. THE PROTEASOME HAS AN ATP-DEPENDENT PROTEOLYTIC ACTIVITY. THE COMPONENT C3 MAY HAVE A POTENTIAL REGULATORY EFFECT ON ANOTHER COMPONENT(S) OF THE PROTEASOME COMPLEX THROUGH TYROSINE PHOSPHORYLATION. CATALYTIC ACTIVITY : Cleavage at peptide bonds with very broad specificity. PATHWAY : Involved in an ATP/ubiquitin-dependent non-lysosomal proteolytic pathway. SUBUNIT : THE PROTEASOME IS COMPOSED OF AT LEAST 15 NON IDENTICAL SUBUNITS WHICH FORM A HIGHLY ORDERED RING-SHAPED STRUCTURE. SUBCELLULAR LOCATION : Cytoplasmic and nuclear. SIMILARITY : BELONGS TO PEPTIDASE FAMILY T1A. |
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19-MAR-03
Last Update 20-Mar-03