Kexin
| Kexin | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Organism | |||||||
| Symbol | KEX2 | ||||||
| Entrez | 855483 | ||||||
| HomoloGene | 22495 | ||||||
| RefSeq (mRNA) | NM_001183076.1 | ||||||
| RefSeq (Prot) | NP_014161.1 | ||||||
| UniProt | D6W0V5 | ||||||
| Other data | |||||||
| EC number | 3.4.21.61 | ||||||
| Chromosome | XIV: 0.2 - 0.21 Mb | ||||||
| |||||||
Kexin (EC 3.4.21.61) is a prohormone-processing protease, specifically a yeast serine peptidase,[1] 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 human homolog is PCSK4. It is a family of subtilisin-like peptidases. Even though there are a few prokaryote kexin-like peptidases, all kexins are eukaryotes.[1][2] 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. In the mammal, kexin-like peptidases function in creating and regulating many differing proproteins.[1]
Nomenclature
[edit]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.[3][4][5][6][7][8]
References
[edit]- ^ a b c "Kexin". Oxford Reference. Retrieved 2020-03-24.
- ^ Seidah NG, Chrétien M (1994). Pro-protein convertases of subtilisin/kexin family. Methods in Enzymology. Vol. 244. Elsevier. pp. 175–88. doi:10.1016/0076-6879(94)44015-8. ISBN 978-0-12-182145-6. PMID 7845206.
- ^ Rockwell NC, Krysan DJ, Komiyama T, Fuller RS (December 2002). "Precursor processing by kex2/furin proteases". Chemical Reviews. 102 (12): 4525–48. doi:10.1021/cr010168i. PMID 12475200.
- ^ Julius D, Brake A, Blair L, Kunisawa R, Thorner J (July 1984). "Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-alpha-factor". Cell. 37 (3): 1075–89. doi:10.1016/0092-8674(84)90442-2. PMID 6430565. S2CID 37772545.
- ^ Achstetter T, Wolf DH (January 1985). "Hormone processing and membrane-bound proteinases in yeast". The EMBO Journal. 4 (1): 173–7. doi:10.1002/j.1460-2075.1985.tb02333.x. PMC 554167. PMID 3894003.
- ^ Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H (October 1988). "Yeast KEX2 genes encodes an endopeptidase homologous to subtilisin-like serine proteases". Biochemical and Biophysical Research Communications. 156 (1): 246–54. doi:10.1016/s0006-291x(88)80832-5. PMID 2845974.
- ^ Fuller RS, Brake A, Thorner J (March 1989). "Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease". Proceedings of the National Academy of Sciences of the United States of America. 86 (5): 1434–8. Bibcode:1989PNAS...86.1434F. doi:10.1073/pnas.86.5.1434. PMC 286710. PMID 2646633.
- ^ Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H (February 1989). "Characterization of KEX2-encoded endopeptidase from yeast Saccharomyces cerevisiae". Biochemical and Biophysical Research Communications. 159 (1): 305–11. doi:10.1016/0006-291x(89)92438-8. PMID 2647083.
External links
[edit]- Kexin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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