Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases
BRITE hierarchy

Release of protein hormones and neuropeptides from their precursors, generally by hydrolysis of -Lys-Arg! bonds

A Ca2+-dependent enzyme, maximally active at about pH 5.5. Specificity is broader than that of prohormone convertase 1. Substrates include pro-opiomelanocortin, proenkephalin, prodynorphin, proglucagon, proinsulin and proluteinizing-hormone-releasing-hormone. Does not hydrolyse prorenin or prosomatostatin, however. Unusually, processing of prodynorphin occurs at a bond in which P2 is Thr. Present in the regulated secretory pathway of neuroendocrine cells, commonly acting co-operatively with prohormone convertase 1. In peptidase family S8 (subtilisin family)

EC 3.4.21.94 created 1996

1  [PMID:2169760]

Seidah NG, Gaspar L, Mion P, Marcinkiewicz M, Mbikay M, Chretien M.

cDNA sequence of two distinct pituitary proteins homologous to Kex2 and furin gene products: tissue-specific mRNAs encoding candidates for pro-hormone processing proteinases.

DNA Cell Biol 9:415-24 (1990)
DOI:10.1089/dna.1990.9.415

[mmu:18549]

2  [PMID:2154467]

Smeekens SP, Steiner DF.

Identification of a human insulinoma cDNA encoding a novel mammalian protein structurally related to the yeast dibasic processing protease Kex2.

J Biol Chem 265:2997-3000 (1990)

[hsa:5126]

3  [PMID:8159732]

Rouille Y, Westermark G, Martin SK, Steiner DF.

Proglucagon is processed to glucagon by prohormone convertase PC2 in alpha TC1-6 cells.

Proc Natl Acad Sci U S A 91:3242-6 (1994)
DOI:10.1073/pnas.91.8.3242

4  [PMID:7845206]

Seidah NG, Chretien M.

Pro-protein convertases of subtilisin/kexin family.

Methods Enzymol 244:175-88 (1994)
DOI:10.1016/0076-6879(94)44015-8