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]
^ abc"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.
Kexin (EC 3.4.21.61) is a prohormone-processing protease, specifically a yeast serine peptidase, found in the budding yeast (S. cerevisiae). It catalyzes...
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