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Some characteristics of hormone (pheromone) processing enzymes in yeast
Author(s) -
Wagner Jean-Claude,
Escher Claudia,
Wolf Dieter H.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81012-8
Subject(s) - phenylmethylsulfonyl fluoride , biochemistry , yeast , saccharomyces cerevisiae , enzyme , pmsf , chemistry , peptide , serine , size exclusion chromatography , membrane , biology
The KEX2 gene‐encoded, membrane‐bound Ca 2+ ‐dependent thiol endoproteinase, proteinase yscF, responsible for processing of the precursor protein of the sex pheromone α‐factor of the yeast Saccharomyces cerevisiae was solubilized from the membraneous fraction and partially purified. Gel filtration revealed an apparent M r of the native protein of around 150 000. Ca 2+ 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 is able to cleave basic amino acids from the carboxy‐terminus of peptides and probably involved in final maturation of the α‐factor peptides generated by proteinase yscF is membrane‐associated, active at neutral pH and responds strongly to the serine proteinase inhibitor phenylmethylsulfonyl fluoride as well as to ‐SH group blocking agents.