The Enzyme Database

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Accepted name: kexin
Reaction: Cleavage of -Lys-Arg┼ and -Arg-Arg┼ bonds to process yeast α-factor pheromone and killer toxin precursors
Other name(s): yeast KEX2 protease; proteinase yscF (gene name); prohormone-processing endoprotease; paired-basic endopeptidase; yeast cysteine proteinase F (misleading); andrenorphin-Gly-generating enzyme; endoproteinase Kex2p; gene KEX2 dibasic proteinase; Kex 2p proteinase; Kex2 endopeptidase; Kex2 endoprotease; Kex2 endoproteinase; Kex2 protease; proteinase Kex2p; Kex2-like precursor protein processing endoprotease; prohormone-processing KEX2 proteinase; prohormone-processing proteinase; proprotein convertase; protease KEX2; Kex2 proteinase; Kex2-like endoproteinase
Comments: A Ca2+-activated peptidase of peptidase family S8, containing Cys near the active site His, and inhibited by p-mercuribenzoate. Similar enzymes occur in mammals.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 99676-46-7
1.  Julius, D., Brake, A., Blair, L., Kunisawa, R. and Thorner, J. Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-α-factor. Cell 37 (1984) 1075–1089. [DOI] [PMID: 6430565]
2.  Achstetter, T. and Wolf, D.H. Hormone processing and membrane-bound proteinases in yeast. EMBO J. 4 (1985) 173–177. [PMID: 3894003]
3.  Mizuno, K., Nakamura, T., Ohshima, T., Tanaka, S. and Matsuo, H. Yeast KEX2 gene encodes an endopeptidase homologous to subtilisin-like serine proteases. Biochem. Biophys. Res. Commun. 156 (1988) 246–254. [DOI] [PMID: 2845974]
4.  Fuller, R.S., Brake, A. and Thorner, J. Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease. Proc. Natl. Acad. Sci. USA 86 (1989) 1434–1438. [DOI] [PMID: 2646633]
5.  Mizuno, K., Nakamura, T., Ohshima, T., Tanaka, S. and Matsuo, H. Characterization of KEX2-encoded endopeptidase from yeast Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 159 (1989) 305–311. [DOI] [PMID: 2647083]
[EC created 1989 as EC, transferred 1992 to EC]

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