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 (Inhibitors
Inhibitors on EC 3.4.23.21 - Rhizopuspepsin
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
Ac-NA-Val-3-hydroxy 4-amino 6-methyl heptanoic acid-2-aminobutanoyl-NA-amide
-
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Co2+
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0.3% residual activity at 10 mM; about 36% residual activity at 10 mM
CTAB
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in the presence of CTAB, 20 and 10 % relative activities are maintained at concentrations of 0.1% (w/v) and 1% (w/v), respectively
dithiothreitol
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the peptidase shows residual activities of 50 and 40% following incubation with 100 or 150 mM dithiothreitol, respectively
guanidine
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the enzyme maintains approximately 70 and 60% of proteolytic activity at 100 and 150 mM guanidine, respectively
Peptide inhibitor
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sequence: D-His-Pro-Phe-His-Phe(Psi)[CH2-NH]Phe-Val-Tyr
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Piper hispidum essential oil
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less than 10% residual activity at 0.048 mg/ml
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Piper tmarginatum essential oil
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less than 50% residual activity at 0.048 mg/ml
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Piper tuberculatum essential oil
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less than 10% residual activity at 0.048 mg/ml
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SDS
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the peptidase maintains approximately 50 % of activity in the presence of 0.02 % (w/v) SDS andloses nearly all activity during incubation with 0.08 % (w/v) SDS
Triton X-100
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approximately 60% residual activity at 0.2 % (v/v) Triton X-100
1,2-epoxy-3-(4-nitrophenoxy)propane
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amino acid sequence around the 1,2-epoxy-3-(4-nitrophenoxy)propane-reactive residues
Diazoacetyl-DL-norleucine methyl ester
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Cu2+ essential for this reaction
Diazoacetyl-DL-norleucine methyl ester
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Cu2+ essential for this reaction; rate of reaction of this inhibitor with the enzyme is decreased in the presence of pepstatin; the rate of inactivation accelerates with increasing concentration of Cu2+
Diazoacetyl-DL-norleucine methyl ester
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Cu2+ essential for this reaction
additional information
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development of petidomimetic inhibitors
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