Pycnoporopepsin
Appearance
Pycnoporopepsin | |||||||||
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Identifiers | |||||||||
EC no. | 3.4.23.30 | ||||||||
CAS no. | 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
[edit]- ^ Tomoda K, Shimazono H (1964). "Acid protease produced by Trametes sanguinea a wood-destroying fungus. Part I. Purification and crystallization of the enzyme". Agric. Biol. Chem. 28: 770–773. doi:10.1271/bbb1961.28.770.
- ^ Tsuru D, Hattori A, Tsuji H, Yamamoto T, Fukumoto J (1969). "Studies on mold proteases. Part II. Substrate specificity of acid protease of Rhizopus chinensis". Agric. Biol. Chem. 33: 1419–1426. doi:10.1080/00021369.1969.10859482.
- ^ Ichishima E, Kumagai H, Tomoda K (1980). "Substrate specificity of carboxyl proteinase from Pycnoporus coccineus, a wood-deteriorating fungus". Curr. Microbiol. 3: 333–337. doi:10.1007/bf02601897.
External links
[edit]- Pycnoporopepsin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)