Kexin
| Kex2p | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | KEX2 | ||||||
| NCBI gene | 855483 | ||||||
| UniProt | D6W0V5 | ||||||
| Other data | |||||||
| EC number | 3.4.21.61 | ||||||
| |||||||
Kexin (EC 3.4.21.61) is a prohormone processing protease found in the budding yeast (S. cerevisiae). It catalyzes the cleavage of -Lys-Arg- and -Arg-Arg- bonds to process yeast alpha-factor pheromone and killer toxin precursors. The enzyme is encoded by the yeast gene KEX2, and usually referred to in the scientific community as Kex2p. It shares structural similarities with the bacterial protease subtilisin. The first mammalian homologue of this protein to be identified was furin.
The enzyme is also known as yeast KEX2 protease, proteinase yscF, prohormone-processing endoprotease, paired-basic endopeptidase, yeast cysteine proteinase F, paired-basic endopeptidase, 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, and Kex2-like endoproteinase.[1][2][3][4][5][6]
References
- ^ Rockwell NC, Krysan DJ, Komiyama T, Fuller RS (December 2002). "Precursor processing by kex2/furin proteases". Chem. Rev. 102 (12): 4525–48. doi:10.1021/cr010168i. PMID 12475200.
- ^ Julius D, Brake A, Blair L, Kunisawa R, Thorner J (1984). "Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-α-factor". Cell. 37: 1075–1089. doi:10.1016/0092-8674(84)90442-2. PMID 6430565.
- ^ Achstetter, T.; Wolf, D.H. (1985). "Hormone processing and membrane-bound proteinases in yeast". EMBO J. 4: 173–177. PMID 3894003.
- ^ Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H (1988). "Yeast KEX2 gene encodes an endopeptidase homologous to subtilisin-like serine proteases". Biochem. Biophys. Res. Commun. 156: 246–254. doi:10.1016/s0006-291x(88)80832-5. PMID 2845974.
- ^ Fuller RS, Brake A, Thorner J (1989). "Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease". Proc. Natl. Acad. Sci. USA. 86: 1434–1438. doi:10.1073/pnas.86.5.1434. PMID 2646633.
- ^ Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H (1989). "Characterization of KEX2-encoded endopeptidase from yeast Saccharomyces cerevisiae". Biochem. Biophys. Res. Commun. 159: 305–311. doi:10.1016/0006-291x(89)92438-8. PMID 2647083.
External links
- Kexin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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