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EC Tree
The expected taxonomic range for this enzyme is: Vigna aconitifolia
Reaction Schemes
efficient hydrolysis of peptides with Arg in P1 position
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efficient hydrolysis of peptides with Arg in P1 position
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hydrolysis of peptide bond
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azocasein + H2O
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benzoyl-Phe-Val-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-Phe-Val-Arg + 7-amino-4-methylcoumarin
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4.4% of the activity with benzyloxycarbonyl-Phe-Arg-7-(4-methyl)coumarylamide
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benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
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10% of the activity with benzyloxycarbonyl-Phe-Arg-7-(4-methyl)coumarylamide
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benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
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Gelatin + H2O
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cystatin
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reversible inhibition
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iodoacetamide
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exceptionally low rat constant for inhibition
iodoacetate
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exceptionally low rat constant for inhibition
leupeptin
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reversible inhibition
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0.00003
cystatin
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26°C, pH 6.0
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0.0000075
leupeptin
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26°C, pH 6.0
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5.5
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reaction with azocasein
7.5
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activity with benzyloxycarbonyl-Phe-Arg-7-(4-methyl)coumarylamide
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3.5 - 7.5
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pH 3.5: about 40% of maximal activity, pH 7.5: about 65% of maximal activity, reaction with casein
4.5 - 8
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pH 4.5: about 35% of maximal activity, pH 8.0: about 60% of maximal activity, reaction with benzyloxycarbonyl-Phe-Arg-7-(4-methyl)coumarylamide
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brenda
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activity increases during germination
brenda
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27000
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x * 27000, SDS-PAGE
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additional information
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the enzyme is not a glycoprotein
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3 - 7
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stable at 26.5°C
30313
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26.5
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very stable during incubation in the range pH 3.0-7.0
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Kembhavi, A.A.; Buttle, D.J.; Knight, C.G.; Barrett, A.J.
The two cysteine endopeptidases of legume seeds: purification and characterization by use of specific fluorometric assays
Arch. Biochem. Biophys.
303
208-213
1993
Vigna aconitifolia
brenda
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