| EC |
3.4.21.94 |
| Accepted name: |
proprotein convertase 2 |
| Reaction: |
Release of protein hormones and neuropeptides from their precursors, generally by hydrolysis of -Lys-Arg┼ bonds |
| Other name(s): |
neuroendocrine convertase 2; PC2 |
| Comments: |
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) |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, CAS registry number: 388092-42-0 |
| References: |
| 1. |
Seidah, N.G., Gaspar, L., Mion, P., Marcinkiewicz, M., Mbikay, M. and Chrétien, 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 (1990) 415–424. [DOI] [PMID: 2169760] |
| 2. |
Smeekens, S.P. and Steiner, D.F. Identification of a human insulinoma cDNA encoding a novel mammalian protein structurally related to the yeast dibasic processing protease Kex2. J. Biol. Chem. 265 (1990) 2997–3000. [PMID: 2154467] |
| 3. |
Rouillé, Y., Westermark, G., Martin, S.K. and Steiner, D.F. Proglucagon is processed to glucagon by prohormone convertase PC2 in alphaTC1-6 cells. Proc. Natl. Acad. Sci. USA 91 (1994) 3242–3246. [DOI] [PMID: 8159732] |
| 4. |
Seidah, N.G. and Chrétien, M. Pro-protein convertases of the subtilisin/kexin family. Methods Enzymol. 244 (1994) 175–188. [DOI] [PMID: 7845206] |
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| [EC 3.4.21.94 created 1996] |
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