View source for Kexin

{{short description|Prohormone-processing protease}}
{{for|the Chinese gymnast|He Kexin}}
{{Infobox nonhuman protein
| Name = Kexin
| image =
| width =
| caption =
| Organism = Saccharomyces cerevisiae
| TaxID = 559292
| Symbol = KEX2
| AltSymbols =
| EntrezGene = 855483
| HomoloGene = 22495
| PDB =
| 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''' ({{EC number|3.4.21.61}}) is a [[prohormone]]-processing [[protease]], specifically a yeast serine peptidase,<ref name = "OR_Kexin" /> found in the budding [[yeast]] (''[[Saccharomyces cerevisiae|S. cerevisiae]]''). It [[catalysis|catalyzes]] the cleavage of -Lys-Arg- and -Arg-Arg- bonds to process [[yeast]] alpha-factor [[pheromone]] and [[killer yeast|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.<ref name = "OR_Kexin">{{cite web |url= https://www.oxfordreference.com/view/10.1093/oi/authority.20110803100035921 |title=Kexin |work =Oxford Reference |access-date=2020-03-24}}</ref><ref>{{cite book | vauthors = Seidah NG, Chrétien M | title = Pro-protein convertases of subtilisin/kexin family | series = Methods in Enzymology | volume = 244 | pages = 175–88 | date = 1994 | pmid = 7845206 | doi = 10.1016/0076-6879(94)44015-8 | publisher = Elsevier | isbn = 978-0-12-182145-6 }}</ref> 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.<ref name = "OR_Kexin" />
== 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.<ref name="pmid12475200">{{cite journal | vauthors = Rockwell NC, Krysan DJ, Komiyama T, Fuller RS | title = Precursor processing by kex2/furin proteases | journal = Chemical Reviews | volume = 102 | issue = 12 | pages = 4525–48 | date = December 2002 | pmid = 12475200 | doi = 10.1021/cr010168i }}</ref><ref>{{cite journal | vauthors = Julius D, Brake A, Blair L, Kunisawa R, Thorner J | title = Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-alpha-factor | journal = Cell | volume = 37 | issue = 3 | pages = 1075–89 | date = July 1984 | pmid = 6430565 | doi = 10.1016/0092-8674(84)90442-2 | s2cid = 37772545 }}</ref><ref>{{cite journal | vauthors = Achstetter T, Wolf DH | title = Hormone processing and membrane-bound proteinases in yeast | journal = The EMBO Journal | volume = 4 | issue = 1 | pages = 173–7 | date = January 1985 | doi = 10.1002/j.1460-2075.1985.tb02333.x | pmid = 3894003 | pmc = 554167 }}</ref><ref>{{cite journal | vauthors = Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H | title = Yeast KEX2 genes encodes an endopeptidase homologous to subtilisin-like serine proteases | journal = Biochemical and Biophysical Research Communications | volume = 156 | issue = 1 | pages = 246–54 | date = October 1988 | pmid = 2845974 | doi = 10.1016/s0006-291x(88)80832-5 }}</ref><ref>{{cite journal | vauthors = Fuller RS, Brake A, Thorner J | title = Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 86 | issue = 5 | pages = 1434–8 | date = March 1989 | pmid = 2646633 | pmc = 286710 | doi = 10.1073/pnas.86.5.1434 | bibcode = 1989PNAS...86.1434F | doi-access = free }}</ref><ref>{{cite journal | vauthors = Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H | title = Characterization of KEX2-encoded endopeptidase from yeast Saccharomyces cerevisiae | journal = Biochemical and Biophysical Research Communications | volume = 159 | issue = 1 | pages = 305–11 | date = February 1989 | pmid = 2647083 | doi = 10.1016/0006-291x(89)92438-8 }}</ref>
== References ==
{{Reflist|32em}}
== External links ==
* {{MeshName|Kexin}}
{{Serine endopeptidases}}
{{Enzymes}}
{{Portal bar|Biology|border=no}}
[[Category:EC 3.4.21]]
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