Literature summary for 3.4.23.19 extracted from

Sasaki, H.; Nakagawa, A.; Muramatsu, T.; Suganuma, M.; Sawano, Y.; Kojima, M.; Kubota, K.; Takahashi, K.; Tanokura, M.
The three-dimensional structure of aspergilloglutamic peptidase from Aspergillus niger (2004), Proc. Jpn. Acad. Ser. B, 80, 435-438.

No PubMed abstract available

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Crystallization (Commentary)

Crystallization (Comment)	Organism
purified enzyme, 100 mg/ml protein in 1.4 M ammonium sulfate, 5% v/v dimethyl sulfoxide, 50 mM glycine, pH 2.1, hanging drop vapour diffusion method, X-ray diffraction structure determination and analysis at 1.4 A resolution, modeling	Aspergillus niger var. macrosporus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
extracellular	the enzyme is secreted	Aspergillus niger var. macrosporus	-	-

Organism

Organism	UniProt	Comment	Textmining
Aspergillus niger var. macrosporus	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
preferential cleavage in B chain of insulin: Asn3-/-Gln, Gly13-/-Ala, Tyr26-/-Thr	catalytic residues are GluB110 and GluB24, catalytic mechanism	Aspergillus niger var. macrosporus	a

Subunits

Subunits	Comment	Organism
More	secondary and three-dimensional structure determination and analysis, two-fold symmetry, the enzyme consists of a C-terminal light and an N-terminal heavy chain	Aspergillus niger var. macrosporus

Synonyms

Synonyms	Comment	Organism
AGP	-	Aspergillus niger var. macrosporus
aspergilloglutamic peptidase	-	Aspergillus niger var. macrosporus

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Release 2023.1 (January 2023)