3.4.21.81: Streptogrisin B
This is an abbreviated version!
For detailed information about Streptogrisin B, go to the full flat file.
Word Map on EC 3.4.21.81
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3.4.21.81
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vacuolar
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proteinases
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carboxypeptidase
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ovomucoid
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omtky3
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lignicolum
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scytalidium
- 3.4.21.81
- vacuolar
- proteinases
- carboxypeptidase
- ovomucoid
- omtky3
- lignicolum
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scytalidium
Reaction
Hydrolysis of proteins with trypsin-like specificity =
Synonyms
More, Pronase B, protease B, Proteinase B, Proteinase, Streptomyces griseus serine B, Serine proteinase B, SGPB, SprB, Streptogrisin B, Streptomyces griseus peptidase B, Streptomyces griseus protease B, Streptomyces griseus proteinase 1, Streptomyces griseus proteinase B
ECTree
3.4.21.81 Streptogrisin BAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.21.81 - Streptogrisin B
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3 acetyl-Pro-Ala-Phe-Phe-NH2 + H2O
acetyl-Pro-Ala-Phe-Phe + NH3 + acetyl-Pro-Ala + Phe-Phe-NH2 + acetyl-Pro-Ala-Phe + Phe-NH2
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hydrolyzed at the Ala-Phe, the Phe-Phe and the Phe-NH2 bond
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-
?
acetyl-Ala-Ala-Tyr-4-methylcoumarin 7-amide + H2O
acetyl-Ala-Ala-Tyr + 7-amino-4-methylcoumarin
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-
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?
Acetyl-Pro-Ala-Ala-Phe-NH2 + H2O
?
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split at the amide bond as well as at the Ala-Ala bond
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-
?
Acetyl-Pro-Ala-Gly-Phe-NH2 + H2O
?
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split at the amide bond as well as at the Ala-Gly bond
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-
?
Acetyl-Pro-Ala-Leu-Phe-NH2 + H2O
Acetyl-Pro-Ala-Leu-Phe-OH + NH3
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hydrolyzed at the amide bond only
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-
?
Acetyl-Pro-Ala-Pro-Phe-NH2 + H2O
Acetyl-Pro-Ala-Pro-Phe-OH + NH3
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hydrolyzed at the amide bond only
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-
?
OMSVP3 + H2O
?
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ovomucoid third domain from silver pheasant, potent inhibitor of chymotrypsin, subtilisin, and elastase
cleavage between residues Met18-Glu19
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?
OMSVP3 mutant P14C/N39C + H2O
?
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disulfide variant of the ovomucoid third domain from silver pheasant carrying an engineered Cys14-Cys39 bond near the reactive site
cleavage between residues Met18-Glu19. P14C/N39C can be selectively cleaved by Streptomyces griseus protease B at the reactive site of OMSVP3 to form a reactive site modified inhibitor. The conversion rate of P14C/N39C is much faster than that for wild type under any pH condition. The reactive site modified form of P14C/N39C is thermodynamically more stable than the intact one
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?
Sc-AAPF-SBn + FAASF-NH2
?
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ligation to nonapeptide by mutant S195A/T213L/F228H
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?
succinyl-Ala-Ala-Pro-4-methylcoumarin 7-amide + H2O
succinyl-Ala-Ala-Pro + 7-amino-4-methylcoumarin
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?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
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?
succinyl-Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Ala-Pro-Phe + 7-amino-4-methylcoumarin
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-
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?
succinyl-L-Ala-L-Ala-L-Pro-L-Asp-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Asp + 4-nitroaniline
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extremely poor substrate at pH 8 but becomes a moderately good substrate at pH 5.5
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-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Leu-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Leu + 4-nitroaniline
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optimum at pH 7.5-8.0
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-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Lys-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Lys + 4-nitroaniline
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optimum at pH 10.0
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?
additional information
?
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interacts favorably with peptides with hydrophobic non-aromatic, P2 amino acid residues, leucine being optimal
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?
additional information
?
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the catalytic preference of protease B for Phe, Tyr, Trp and leucyl-glycine peptide bonds under denaturing conditions enhances its utility in the site-specific proteolysis of insoluble or otherwise proteolysis-resistant polypeptide substrates
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?
additional information
?
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member of the chymotrypsin superfamily of serine proteases
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?
additional information
?
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member of the chymotrypsin superfamily of serine proteases
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?
additional information
?
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upon the formation of the tetrahedral intermediate, residues Glu192A to Gly193 of SGPB move towards the alpha-carboxylate O of residue P1 of the bound species, and adjustments in the side-chain conformational angles of His57 and Ser195 of SGPB favor the progression of the catalytic mechanism of SGPB
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?
