Aspergilloglutamic peptidase | |||||||||
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![]() Aspergilloglutamic peptidase dimer | |||||||||
Identifiers | |||||||||
EC no. | 3.4.23.19 | ||||||||
CAS no. | 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 a 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
This enzyme is isolated from Aspergillus niger var. macrosporus.
Aspergilloglutamic peptidase | |||||||||
---|---|---|---|---|---|---|---|---|---|
![]() Aspergilloglutamic peptidase dimer | |||||||||
Identifiers | |||||||||
EC no. | 3.4.23.19 | ||||||||
CAS no. | 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 | ||||||||
|
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 a 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
This enzyme is isolated from Aspergillus niger var. macrosporus.