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]

Purification

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Purification on EC 3.4.21.B48 - kumamolysin

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

-

Bacillus novosp.

-

651844, 653914

recombinant wild-type and mutant enzymes from Escherichia coli by heat treatment and anion exchange chromatography at pH 7.0, to homogeneity, separation of the propeptide from the mature enzyme by hydroxyapatite chromatography

Alicyclobacillus sendaiensis

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664913