3.4.23.22: Endothiapepsin
This is an abbreviated version!
For detailed information about Endothiapepsin, go to the full flat file.
Word Map on EC 3.4.23.22
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3.4.23.22
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proteinases
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3.4.23.6
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renin
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rhizopuspepsin
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penicillopepsin
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scissile
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hydroxyethylene
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hit-to-lead
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isostere
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cryphonectria
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gem-diol
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medicine
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nutrition
- 3.4.23.22
- proteinases
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3.4.23.6
- renin
- rhizopuspepsin
- penicillopepsin
-
scissile
-
hydroxyethylene
-
hit-to-lead
-
isostere
- cryphonectria
-
gem-diol
- medicine
- nutrition
Reaction
hydrolysis of proteins with specificity similar to that of pepsin A; prefers hydrophobic residues at P1 and P1', but does not cleave Ala14-Leu in the B chain of insulin or Z-Glu-Tyr. Clots milk =
Synonyms
Aspartate protease, Aspartic proteinase, EC 3.4.23.10, EC 3.4.23.6, EC 3.4.4.17, Endothia acid proteinase, Endothia aspartic proteinase, Endothia parasitica acid proteinase, Endothia parasitica aspartic proteinase, Proteinase, Endothia aspartic
ECTree
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Reaction
Reaction on EC 3.4.23.22 - Endothiapepsin
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hydrolysis of proteins with specificity similar to that of pepsin A; prefers hydrophobic residues at P1 and P1', but does not cleave Ala14-Leu in the B chain of insulin or Z-Glu-Tyr. Clots milk
hydrolysis of proteins with specificity similar to that of pepsin A; prefers hydrophobic residues at P1 and P1', but does not cleave Ala14-Leu in the B chain of insulin or Z-Glu-Tyr. Clots milk
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hydrolysis of proteins with specificity similar to that of pepsin A; prefers hydrophobic residues at P1 and P1', but does not cleave Ala14-Leu in the B chain of insulin or Z-Glu-Tyr. Clots milk
the enzyme contains a catalytic Asp dyad
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hydrolysis of proteins with specificity similar to that of pepsin A; prefers hydrophobic residues at P1 and P1', but does not cleave Ala14-Leu in the B chain of insulin or Z-Glu-Tyr. Clots milk
catalytic mechanism, X-ray, neutron and NMR studies
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