Information on EC 3.4.21.80 - Streptogrisin A

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The expected taxonomic range for this enzyme is: Streptomyces griseus

EC NUMBER
COMMENTARY
3.4.21.80
-
RECOMMENDED NAME
GeneOntology No.
Streptogrisin A
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of proteins with specificity similar to chymotrypsin
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
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SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Protease A
-
-
-
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Proteinase A
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-
-
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Proteinase, Streptomyces griseus serine, A
-
-
-
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SGPA
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-
-
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Streptomyces griseus protease A
-
-
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Streptomyces griseus protease A
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Streptomyces griseus proteinase A
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-
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Streptomyces griseus serine proteinase 3
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-
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Streptomyces griseus serine proteinase A
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-
-
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CAS REGISTRY NUMBER
COMMENTARY
55326-50-6
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
-
hydrolyzed at the Ala-Phe, the Phe-Phe and the Phe-NH2 bonds
-
-
acetyl-Ala-Ala-Tyr-4-methylcoumarin 7-amide + H2O
acetyl-Ala-Ala-Tyr + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
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Acetyl-Pro-Ala-Ala-Phe-NH2 + H2O
?
show the reaction diagram
-
-
-
-
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Acetyl-Pro-Ala-Gly-Phe-NH2 + H2O
?
show the reaction diagram
-
split at amide bond as well as at the Ala-Gly bond
-
-
-
Acetyl-Pro-Ala-Leu-Phe-NH2 + H2O
Acetyl-Pro-Ala-Leu-Phe-OH + NH3
show the reaction diagram
-
hydrolyzed at the amide bond only
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-
Acetyl-Pro-Ala-Pro-Phe-Leu-NH2 + H2O
Acetyl-Pro-Ala-Pro-Phe + Leu-NH2
show the reaction diagram
-
-
-
-
Acetyl-Pro-Ala-Pro-Phe-NH2 + H2O
Acetyl-Pro-Ala-Pro-Phe-OH + NH3
show the reaction diagram
-
-
-
-
Acetyl-Pro-Ala-Pro-Phe-NH2 + H2O
Acetyl-Pro-Ala-Pro-Phe-OH + NH3
show the reaction diagram
-
hydrolyzed at the amide bond only
-
-
Acetyl-Pro-Ala-Pro-Phe-Tyr-NH2 + H2O
Acetyl-Pro-Ala-Pro-Phe + Tyr-NH2
show the reaction diagram
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-
-
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Acetyl-Pro-Ala-Pro-Trp-NH2 + H2O
Acetyl-Pro-Ala-Pro-Trp-OH + NH3
show the reaction diagram
-
-
-
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Peptide + H2O
Hydrolyzed peptide + H2O
show the reaction diagram
-
interacts favorably with peptides with hydrophobic non-aromatic, P2 amino acid residues, leucine being optimal
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succinyl-Ala-Ala-Pro-Phe 4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
show the reaction diagram
-
-
-
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Succinyl-Ala-Ala-Pro-Phe-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
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succinyl-Ala-Ala-Pro-X-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Ala-Pro-X-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Acetyl-Pro-Ala-Pro-Tyr-NH2 + H2O
Acetyl-Pro-Ala-Pro-Tyr-OH + NH3
show the reaction diagram
-
-
-
-
additional information
?
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model of serine protease catalytic tetrahedral intermediates
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-
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Benzyloxycarbonyl-Arg-Ile-phenylalanylaldehyde
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Benzyloxycarbonyl-Arg-Leu-phenylalanylaldehyde
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Bovine pancreatic trypsin inhibitor
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Kunitz
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protein inhibitor S13D14Y15-OMTKY3
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a OMTKY3 mutant variant, recombinantly produced in Escherichia coli strain RV308 and purified, slight inhibition, overview
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protein inhibitor S13D14Y15G18I19K21-OMTKY3
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a OMTKY3 mutant variant, recombinantly produced in Escherichia coli strain RV308 and purified, slight inhibition, overview. S13D14Y15G18I19K21 OMTKY3 inhibits Streptomyces griseus protease B, EC 3.4.21.81, 10times more strongly than Streptomyces griseus protease A
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Soybean trypsin inhibitor
-
-
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Streptomyces subtilisin inhibitor
-
-
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Turkey ovomucoid third domain
-
-
-
additional information
-
OMTKY3 inhibitor variant screening, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.45
Acetyl-Pro-Ala-Leu-Phe-NH2
-
-
0.02
Acetyl-Pro-Ala-Pro-Phe-Leu-NH2
-
-
0.54
Acetyl-Pro-Ala-Pro-Phe-NH2
-
-
0.15
Acetyl-Pro-Ala-Pro-Phe-Tyr-NH2
-
-
0.87
Acetyl-Pro-Ala-Pro-Trp-NH2
-
-
0.047
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
-
-
0.045
Succinyl-Ala-Ala-Pro-Phe-4-methylcoumarin 7-amide
-
-
1.4
Acetyl-Pro-Ala-Pro-Tyr-NH2
-
-
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04
Acetyl-Ala-Ala-Tyr-4-methylcoumarin 7-amide
Streptomyces griseus
-
-
5.1
Acetyl-Pro-Ala-Leu-Phe-NH2
Streptomyces griseus
-
-
20
Acetyl-Pro-Ala-Pro-Phe-Leu-NH2
Streptomyces griseus
-
-
5.8
Acetyl-Pro-Ala-Pro-Phe-NH2
Streptomyces griseus
-
-
56.8
Acetyl-Pro-Ala-Pro-Phe-Tyr-NH2
Streptomyces griseus
-
-
0.1
Acetyl-Pro-Ala-Pro-Trp-NH2
Streptomyces griseus
-
-
285
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
Streptomyces griseus
-
-
6.9
Succinyl-Ala-Ala-Pro-Phe-4-methylcoumarin 7-amide
Streptomyces griseus
-
-
10.1
Acetyl-Pro-Ala-Pro-Tyr-NH2
Streptomyces griseus
-
-
additional information
additional information
Streptomyces griseus
-
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8.3
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
requires further purification
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1.8 A resolution structure; in complex with acetyl-Pro-Ala-Pro-Phe-OH, acetyl-Pro-Ala-Pro-Tyr-OH and acetyl-Pro-Ala-Pro-phenylalanylaldehyde; in the native conformation
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1.8 A resolution structure; in the native conformation
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1.8 A resolution structure; of the complex between chymostatin and protease A
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active-site geometry; structure at 2.8 A resolution
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crystallographic re-investigation into structure of proteinase A reveals an acyl-enzyme intermediate
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of the complex between chymostatin and protease A
-
structure at 2.8 A resolution
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
further purification of a commercial preparation
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene structure
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