The structure and function of Saccharomyces cerevisiae proteinase A.
作者： Charity L. Parr , Robert A. B. Keates , Brian C. Bryksa , Masahiro Ogawa , Rickey Y. Yada
DOI: 10.1002/YEA.1485
关键词:
摘要: Saccharomyces cerevisiae proteinase A (saccharopepsin; EC 3.4.23.25) is a member of the aspartic superfamily (InterPro IPR001969), which are proteolytic enzymes distributed among variety organisms. Targeted to vacuole as zymogen, its activation at acidic pH can occur by two different pathways, one-step process release mature A, involving intervention B, or step-wise pathway via autoactivation product known pseudo-proteinase A. Once active, S. essential activities other yeast vacuolar hydrolases, including B and carboxypeptidase Y. The enzyme bilobal, with each lobe providing one catalytically acid residues in active site. crystal structure free reveals that flap loop assumes an atypical position, pointing directly into S(1) pocket enzyme. With regard hydrolysis, has preference for hydrophobic Phe, Leu Glu P1 position Ile, Ala P1', inhibited IA(3), natural highly specific inhibitor produced cerevisiae. This review first comprehensive PrA.
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