| Pycnoporopepsin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
| |||||||||
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.
- ^ 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.
- Pycnoporopepsin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| Pycnoporopepsin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
| |||||||||
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.
- ^ 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.
- Pycnoporopepsin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)