3.4.21.B48: kumamolysin
This is an abbreviated version!
For detailed information about kumamolysin, go to the full flat file.
Word Map on EC 3.4.21.B48
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3.4.21.B48
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peptidase
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pepstatin-insensitive
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subtilisin
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hole
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oxyanion
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proteinases
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collagenase
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pepstatin
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merops
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diazoacetyl-dl-norleucine
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sedolisins
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celiac
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subtilisin-like
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acidophilic
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xanthomonas
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leu15-tyr16
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gluten
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alicyclobacillus
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biotechnology
- 3.4.21.B48
- peptidase
-
pepstatin-insensitive
- subtilisin
-
hole
-
oxyanion
- proteinases
- collagenase
- pepstatin
- merops
- diazoacetyl-dl-norleucine
- sedolisins
- celiac
-
subtilisin-like
-
acidophilic
- xanthomonas
-
leu15-tyr16
- gluten
-
alicyclobacillus
- biotechnology
Reaction
specifically hydrolyzes Leu15-Tyr16 peptide bond in oxidized insulin B chain, additional cleavage at Phe25-Tyr26 at a considerably lower rate. Good cleavage of the Phe-I-(p-nitrophenylalanine) bond in synthetic peptides. The enzyme preferentially hydrolyzes peptides having an Ala or Pro residue at P2 position and prefers such charged amino acid residues as Glu or Arg at the P2' position. No cleavage: Asp-Pro-Ala-Lys-Phe-(p-nitrophenylalanine)-Arg-Leu =
Synonyms
J-4 serine-carboxyl proteinase, KSCP, kumamolisin, kumamolisin serine-carboxyl proteinase, kumamolisin-ac, kumamolisin-AS, kumamolisin-like proteae, kumamolysin, More, SCPA
ECTree
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Cloned
Cloned on EC 3.4.21.B48 - kumamolysin
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expression of wild-type and mutant enzymes in Escherichia coli strain JM109
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overexpression of wild-type and mutant enzymes as soluble proteins in Escherichia coli
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