Biology:Pycnoporopepsin
From HandWiki
| Pycnoporopepsin | |||||||||
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| Identifiers | |||||||||
| EC number | 3.4.23.30 | ||||||||
| CAS number | 77967-78-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Pycnoporopepsin (EC 3.4.23.30, proteinase Ia, Pycnoporus coccineus aspartic proteinase, Trametes acid proteinase) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Similar to pepsin A, but narrower, cleaving only three bonds in the B chain of insulin: Ala14-Leu, Tyr16-Leu, and Phe24-Phe
This enzyme is isolated from the basidiomycete Pycnoporus sanguineus.
References
- ↑ "Acid protease produced by Trametes sanguinea a wood-destroying fungus. Part I. Purification and crystallization of the enzyme". Agric. Biol. Chem. 28: 770–773. 1964. doi:10.1271/bbb1961.28.770.
- ↑ "Studies on mold proteases. Part II. Substrate specificity of acid protease of Rhizopus chinensis". Agric. Biol. Chem. 33: 1419–1426. 1969. doi:10.1080/00021369.1969.10859482.
- ↑ "Substrate specificity of carboxyl proteinase from Pycnoporus coccineus, a wood-deteriorating fungus". Curr. Microbiol. 3: 333–337. 1980. doi:10.1007/bf02601897.
External links
- Pycnoporopepsin at the US National Library of Medicine Medical Subject Headings (MeSH)
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