Acrocylindropepsin
| Acrocylindropepsin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.23.28 | ||||||||
| CAS number | 37288-84-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Acrocylindropepsin (EC 3.4.23.28, Acrocylindrium proteinase, Acrocylindrium acid proteinase) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Preference for hydrophobic residues at P1 and P1'. Action on the B chain of insulin is generally similar to that of pepsin A, but it also cleaves Leu6-Cys(SO3H), Glu21-Arg and Asn3-Gln, although not Gln4-His
This enzyme is present in fungus Acrocylindrium sp.
References
- ↑ Uchino, F.; Kurono, Y.; Doi, S. (1967). "Purification and some properties of crystalline acid protease from Acrocylindrium sp". Agric. Biol. Chem. 31: 428–434. doi:10.1271/bbb1961.31.428.
- ↑ Ichihara, S.; Uchino, F. (1975). "The specificity of acid proteinase from Acrocylindrium". Agric. Biol. Chem. 39: 423–428. doi:10.1271/bbb1961.39.423.
- ↑ Takahashi, K.; Chang, W.-J. (1976). "The structure and function of acid proteases. V. Comparative studies on the specific inhibition of acid proteases by diazoacetyl-DL-norleucine methyl ester, 1,2-epoxy-3-(p-nitrophenoxy)propane and pepstatin". J. Biochem. 80: 497–506. PMID 10290.
External links
- Acrocylindropepsin at the US National Library of Medicine Medical Subject Headings (MeSH)
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