Aspergillopepsin II
| Aspergilloglutamic peptidase | |||||||||
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Aspergilloglutamic peptidase dimer | |||||||||
| Identifiers | |||||||||
| EC number | 3.4.23.19 | ||||||||
| CAS number | 9025-49-4 | ||||||||
| 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
- ↑ Chang, W.-J., Horiuchi, S., Takahashi, K., Yamasaki, M. and Yamada, Y. (1976). "The structure and function of acid proteases. VI. Effects of acid protease-specific inhibitors on the acid proteases from Aspergillus niger var. macrosporus". J. Biochem. (Tokyo) 80: 975–981. PMID 12156.
- ↑ Iio, K. and Yamasaki, M. (1976). "Specificity of acid proteinase A from Aspergillus niger var. macrosporus towards B-chain of performic acid oxidized bovine insulin". Biochim. Biophys. Acta 429: 912–924. doi:10.1016/0005-2744(76)90336-3. PMID 1268233.
- ↑ Takahashi K (2013). "Structure and function studies on enzymes with a catalytic carboxyl group(s): from ribonuclease T1 to carboxyl peptidases". Proc Jpn Acad Ser B Phys Biol Sci 89 (6): 201–25. doi:10.2183/pjab.89.201. PMC 3749792. PMID 23759941.
- ↑ Sasaki H1, Kubota K, Lee WC, Ohtsuka J, Kojima M, Iwata S, Nakagawa A, Takahashi K, Tanokura M. (2012). "The crystal structure of an intermediate dimer of aspergilloglutamic peptidase that mimics the enzyme-activation product complex produced upon autoproteolysis". Journal of Biochemistry 152 (1): 45–52. doi:10.1093/jb/mvs050. PMID 22569035.
External links
- Aspergillopepsin II at the US National Library of Medicine Medical Subject Headings (MeSH)
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