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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

Engineering

Engineering on EC 3.4.21.B48 - kumamolysin

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D164N
-
site-directed mutagenesis, replacement of the catalytic residue of kumamolisin-As with that of subtilisin, disrupted interaction of Ser278 with residue 164, the mutant shows 1.3% of the wild-type turnover
E78A/D164N
-
site-directed mutagenesis, completely inactive mutant which stays unprocessed
E78H
-
0.01% activity compared to wild-type enzyme, the canonical catalytic triad is disrupted
E78H/D164N
-
site-directed mutagenesis, replacement of the catalytic residues of kumamolisin-As with those of subtilisin, disruption of the catalytic triad, the mutant shows 0.0001% of the wild-type turnover
E78Q/D164N
-
site-directed mutagenesis, completely inactive mutant which stays unprocessed
D164N
-
site-directed mutagenesis, replacement of the catalytic residue of kumamolisin-As with that of subtilisin, disrupted interaction of Ser278 with residue 164, the mutant shows 1.3% of the wild-type turnover
-
E78A/D164N
-
site-directed mutagenesis, completely inactive mutant which stays unprocessed
-
E78H/D164N
-
site-directed mutagenesis, replacement of the catalytic residues of kumamolisin-As with those of subtilisin, disruption of the catalytic triad, the mutant shows 0.0001% of the wild-type turnover
-
E78Q/D164N
-
site-directed mutagenesis, completely inactive mutant which stays unprocessed
-
E78H
-
0.01% activity compared to wild-type enzyme, the canonical catalytic triad is disrupted
-
E32A
Bacillus novosp.
-
the ratio of turnover number to Km-value for the substrate Lys-Pro-Ile-Ala-Phe-(4-nitro)Phe-Arg-Leu is reduced to 5.7% of the native enzyme
S278A
Bacillus novosp.
-
the ratio of turnover number to Km-value for the substrate Lys-Pro-Ile-Ala-Phe-(4-nitzo)Phe-Arg-Leu is reduced to 0.5% of the native enzyme
W129A
Bacillus novosp.
-
the ratio of turnover number to Km-value for the substrate Lys-Pro-Ile-Ala-Phe-(4-nitro)Phe-Arg-Leu is reduced to 3.8% of the native enzyme
E32A
-
the ratio of turnover number to Km-value for the substrate Lys-Pro-Ile-Ala-Phe-(4-nitro)Phe-Arg-Leu is reduced to 5.7% of the native enzyme
-
S278A
-
the ratio of turnover number to Km-value for the substrate Lys-Pro-Ile-Ala-Phe-(4-nitzo)Phe-Arg-Leu is reduced to 0.5% of the native enzyme
-
W129A
-
the ratio of turnover number to Km-value for the substrate Lys-Pro-Ile-Ala-Phe-(4-nitro)Phe-Arg-Leu is reduced to 3.8% of the native enzyme
-
S278A
D164
-
the mutant shows about 1.3% activity compared to the wild type enzyme
D164A
D316A
-
site-directed mutagenesis, autoactivation similar to the wild-type enzyme, 3% of wild-type enzyme activity
D82A
-
site-directed mutagenesis, no autoactivation of the proform, inactive mutant
E78A
-
site-directed mutagenesis, no autoactivation of the proform, inactive mutant
S278A
-
site-directed mutagenesis, no autoactivation of the proform, inactive mutant
D164A
-
site-directed mutagenesis, no autoactivation of the proform, inactive mutant
-
D316A
-
site-directed mutagenesis, autoactivation similar to the wild-type enzyme, 3% of wild-type enzyme activity
-
D82A
-
site-directed mutagenesis, no autoactivation of the proform, inactive mutant
-
E78A
-
site-directed mutagenesis, no autoactivation of the proform, inactive mutant
-
S278A
-
site-directed mutagenesis, no autoactivation of the proform, inactive mutant
-
additional information