3.4.23.21: Rhizopuspepsin
This is an abbreviated version!
For detailed information about Rhizopuspepsin, go to the full flat file.
Word Map on EC 3.4.23.21
Reaction
hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1'. Clots milk and activates trypsinogen. Does not cleave Gln4-His, but does cleave His10-/-Leu and Val12-/-Glu in B chain of insulin =
Synonyms
Aspartate protease, aspartic peptidase, EC 3.4.23.6, EC 3.4.23.9, EC 3.4.4.17, EC 3.4.99.25, More, Neurase, Proteinase, Rhizopus acid, Rhizopus acid protease, Rhizopus acid proteinase, Rhizopus aspartic proteinase, rhizopuspepsinogen
ECTree
3.4.23.21 RhizopuspepsinAdvanced search results
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results (Crystallization
Crystallization on EC 3.4.23.21 - Rhizopuspepsin
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
three-dimensional structure of the complex of rhizopuspepsin with pepstatin at 2.5 A resolution
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crystal structure determined at pH 4.6, 7.0, and 8.0, using hanging-drop method, space group P2(1)2(1)2(1) unit-cell parameters a 0 60.48 A, b : 60.52 A, c : 106.87 A at pH 4.6, a : 60.19 A, b : 60.79 A, c : 106.99 A at pH 7.0, a : 60.37 A, b : 60.58 A, c : 107.36 A at pH 8.0, enzyme cannot be crystallized outside the pH range 4.6-8.0
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crystals with typical dimensions of 0.3 x 0.3 x 0.6 mm, orthorhombic crystals, space group P2(1)2(1)2(1), with dimensions a : 60.18A, b : 71.10A, and c : 81.21A
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