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
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3.4.21.B48
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peptidase
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pepstatin-insensitive
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subtilisin
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hole
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oxyanion
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proteinases
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collagenase
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pepstatin
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merops
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diazoacetyl-dl-norleucine
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sedolisins
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celiac
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subtilisin-like
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acidophilic
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xanthomonas
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leu15-tyr16
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gluten
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alicyclobacillus
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biotechnology
- 3.4.21.B48
- peptidase
-
pepstatin-insensitive
- subtilisin
-
hole
-
oxyanion
- proteinases
- collagenase
- pepstatin
- merops
- diazoacetyl-dl-norleucine
- sedolisins
- celiac
-
subtilisin-like
-
acidophilic
- xanthomonas
-
leu15-tyr16
- gluten
-
alicyclobacillus
- biotechnology
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
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Posttranslational Modification
Posttranslational Modification on EC 3.4.21.B48 - kumamolysin
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no glycoprotein
proteolytic modification
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the enzyme needs to be cleaved in to the mature enzyme and the N-terminal prepropeptide, autocatalytic cleavage
proteolytic modification
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the enzyme needs to be cleaved in to the mature enzyme and the N-terminal prepropeptide, autocatalytic cleavage
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proteolytic modification
Bacillus novosp.
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pro-kumamolisinS278A: the prodomain exhibits a half-beta sandwich core docking to the catalytic domain similarly as the equivalent subtilisin prodomain complexes
proteolytic modification
Bacillus novosp.
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the enzyme is synthesiszed as a larger precursor consisting of two regions: amino-terminal prepro (199 amino acids) and mature proteins (384 amino acids)
proteolytic modification
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the enzyme is synthesiszed as a larger precursor consisting of two regions: amino-terminal prepro (199 amino acids) and mature proteins (384 amino acids)
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proteolytic modification
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pro-kumamolisinS278A: the prodomain exhibits a half-beta sandwich core docking to the catalytic domain similarly as the equivalent subtilisin prodomain complexes
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proteolytic modification
the enzyme performs autoactivation, autocatalytic process of pro-kumamolisin activation, the protonation of Asp164 triggers conformational changes and generates the functional active site for autocatalysis, mechanism of acylation for autocatalytic cleavage of prodomain, molecular dynamics and quantum mechanical/molecular mechanical free-energy simulations, overview
proteolytic modification
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the enzyme performs autoactivation, autocatalytic process of pro-kumamolisin activation, the protonation of Asp164 triggers conformational changes and generates the functional active site for autocatalysis, mechanism of acylation for autocatalytic cleavage of prodomain, molecular dynamics and quantum mechanical/molecular mechanical free-energy simulations, overview
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proteolytic modification
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the enzyme needs to cleaved in to the mature enzyme and the N-terminal prepropeptide, autocatalytic cleavage
proteolytic modification
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the enzyme needs to cleaved in to the mature enzyme and the N-terminal prepropeptide, autocatalytic cleavage
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