Kexin Explained
Kexin |
Organism: | Saccharomyces cerevisiae |
Taxid: | 559292 |
Symbol: | KEX2 |
Entrezgene: | 855483 |
Homologene: | 22495 |
Refseqmrna: | NM_001183076.1 |
Refseqprotein: | NP_014161.1 |
Uniprot: | D6W0V5 |
Ecnumber: | 3.4.21.61 |
Chromosome: | XIV |
Entrezchromosome: | NC_001146.8 |
Genloc Start: | 202060 |
Genloc End: | 205238 |
Kexin is a prohormone-processing protease, specifically a yeast serine peptidase, 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.
Nomenclature
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]
Notes and References
- Web site: Kexin . Oxford Reference . 2020-03-24.
- Book: Seidah NG, Chrétien M . Pro-protein convertases of subtilisin/kexin family . Methods in Enzymology . 244 . 175–88 . 1994 . 7845206 . 10.1016/0076-6879(94)44015-8 . Elsevier . 978-0-12-182145-6 .
- Rockwell NC, Krysan DJ, Komiyama T, Fuller RS . Precursor processing by kex2/furin proteases . Chemical Reviews . 102 . 12 . 4525–48 . December 2002 . 12475200 . 10.1021/cr010168i .
- Julius D, Brake A, Blair L, Kunisawa R, Thorner J . 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 . July 1984 . 6430565 . 10.1016/0092-8674(84)90442-2 . 37772545 .
- Achstetter T, Wolf DH . Hormone processing and membrane-bound proteinases in yeast . The EMBO Journal . 4 . 1 . 173–7 . January 1985 . 10.1002/j.1460-2075.1985.tb02333.x . 3894003 . 554167 .
- Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H . Yeast KEX2 genes encodes an endopeptidase homologous to subtilisin-like serine proteases . Biochemical and Biophysical Research Communications . 156 . 1 . 246–54 . October 1988 . 2845974 . 10.1016/s0006-291x(88)80832-5 .
- Fuller RS, Brake A, Thorner J . 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 . March 1989 . 2646633 . 286710 . 10.1073/pnas.86.5.1434 . 1989PNAS...86.1434F . free .
- Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H . Characterization of KEX2-encoded endopeptidase from yeast Saccharomyces cerevisiae . Biochemical and Biophysical Research Communications . 159 . 1 . 305–11 . February 1989 . 2647083 . 10.1016/0006-291x(89)92438-8 .