Aspergillopepsin II
| Aspergilloglutamic peptidase | |||||||||
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| 240px
Aspergilloglutamic peptidase dimer
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| Identifiers | |||||||||
| EC number | 3.4.23.19 | ||||||||
| CAS number | Template:CAS | ||||||||
| 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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Aspergilloglutamic peptidase, also called aspergillopepsin II (EC 3.4.23.19, proctase A, Aspergillus niger acid proteinase A, Aspergillus niger var. macrosporus aspartic proteinase) is a proteolytic enzyme.[1][2] The enzyme was previously thought be an aspartic protease, but it was later shown to be an glutamic protease with a catalytic Glu residue at the active site, and was therefore renamed aspergilloglutamic peptidase.[3]
Determination of its molecular structure showed it to be a unique two-chain enzyme with a light chain and a heavy chain bound non-covalently with each other. The C-terminal region of the light chain of one molecule binds to the active site cleft of another molecule in the manner of a substrate.[4]
This enzyme catalyses the following chemical reaction
- Preferential cleavage in B chain of insulin: Asn3-Gln, Gly13-Ala, Tyr26-Thr
This enzyme is isolated from Aspergillus niger var. macrosporus.
References
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<references />, or <references group="..." />External links
- Aspergillopepsin II at the US National Library of Medicine Medical Subject Headings (MeSH)
