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Information on EC 3.4.21.B48 - kumamolysin

for references in articles please use BRENDA:EC3.4.21.B48
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.B48 kumamolysin
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This record set is specific for:
UNIPROT: Q8RR56
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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-/-(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
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
kumamolysin, kumamolisin-as, kumamolisin, more
CAS REGISTRY NUMBER
COMMENTARY hide
145380-44-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q8RR56_9BACI
552
0
57743
TrEMBL
-