| Title: | Some characteristics of hormone (pheromone) processing enzymes in yeast |
| Author(s): | Wagner JC; Escher C; Wolf DH; |
| DOI: | 10.1016/0014-5793(87)81012-8 |
| ISSN/ISBN: | 0014-5793 (Print) 0014-5793 (Linking) |
| Abstract: | "The KEX2 gene-encoded, membrane-bound Ca2+-dependent thiol endoproteinase, proteinase yscF, responsible for processing of the precursor protein of the sex pheromone alpha-factor of the yeast Saccharomyces cerevisiae was solubilized from the membraneous fraction and partially purified. Gel filtration revealed an apparent Mr of the native protein of around 150,000. Ca2+ concentration for half-maximal activity was in the micromolar range and concentration of the substrate Cbz-Tyr-Lys-Arg-4-nitroanilide for half-maximal velocity was 0.05 mM. The enzyme able to cleave basic amino acids from the carboxy-terminus of peptides and probably involved in final maturation of the alpha-factor peptides generated by proteinase yscF is membrane-associated, active at neutral pH and responds strongly to the serine proteinase inhibitor phenyl-methylsulfonyl fluoride as well as to -SH group blocking agents" |
| Keywords: | "Chromatography, Gel Endopeptidases/isolation & purification/*metabolism Fungal Proteins/antagonists & inhibitors/isolation & purification/*metabolism Mating Factor Membrane Proteins/isolation & purification/*metabolism Peptides/*metabolism *Proprotein Con;" |
| Notes: | "MedlineWagner, J C Escher, C Wolf, D H eng Research Support, Non-U.S. Gov't England 1987/06/22 FEBS Lett. 1987 Jun 22; 218(1):31-4. doi: 10.1016/0014-5793(87)81012-8" |
