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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

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

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.B48 kumamolysin

General Stability

General Stability on EC 3.4.21.B48 - kumamolysin

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is stable against perturbation by pressure and chemical denaturants
Bacillus novosp.
-