3.4.21.B48: kumamolysin

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For detailed information about kumamolysin, go to the full flat file.

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

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Results	in table
1	AA Sequence
1	Application
1	CAS Registry Number
4	Cloned(Commentary)
6	Crystallization (Commentary)
2	Disease/ Diagnostics
4	General Information
1	General Stability
9	Inhibitors
3	Ki Value [mM]
78	KM Value [mM]
2	Localization
14	Molecular Weight [Da]
70	Organism
4	pH Optimum
2	pH Range
2	pI Value
12	Posttranslational Modification
32	Protein Variants
3	Purification (Commentary)
6	Reaction
2	Reaction Type
26	Reference
4	Source Tissue
2	Specific Activity [micromol/min/mg]
94	Substrates and Products (Substrate)
15	Subunits
30	Synonyms
5	Temperature Optimum [°C]
2	Temperature Range [°C]
6	Temperature Stability [°C]
94	Turnover Number [1/s]

pH Range

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pH Range on EC 3.4.21.B48 - kumamolysin

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pH RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

1 - 4

Alicyclobacillus acidocaldarius

-

-

677899

2.5 - 4

Bacillus novosp.

-

pH 2.5: about 60% of maximal activity, pH 4.0: about 50% of maximal activity, hydrolysis of casein

651844