Acrocylindropepsin | |||||||||
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Identifiers | |||||||||
EC no. | 3.4.23.28 | ||||||||
CAS no. | 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 | ||||||||
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Acrocylindropepsin (EC 3.4.23.28, Acrocylindrium proteinase, Acrocylindrium acid proteinase) is an enzyme. 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), Glu-Arg and Asn-Gln, although not Gln-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 WJ (September 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". Journal of Biochemistry. 80 (3): 497–506. PMID 10290.
External links
- Acrocylindropepsin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Proteases: aspartate proteases (EC 3.4.23) | |
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Cathepsin |
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