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 ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
-
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SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Protease A
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-
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Proteinase A
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-
-
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Proteinase, Streptomyces griseus serine, A
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-
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SGPA
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-
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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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Streptomyces griseus serine proteinase A
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-
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CAS REGISTRY NUMBER
COMMENTARY
55326-50-6
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
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
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hydrolyzed at the Ala-Phe, the Phe-Phe and the Phe-NH2 bonds
-
-
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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
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split at amide bond as well as at the Ala-Gly bond
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-
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Acetyl-Pro-Ala-Leu-Phe-NH2 + H2O
Acetyl-Pro-Ala-Leu-Phe-OH + NH3
show the reaction diagram
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hydrolyzed at the amide bond only
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-
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Acetyl-Pro-Ala-Pro-Phe-Leu-NH2 + H2O
Acetyl-Pro-Ala-Pro-Phe + Leu-NH2
show the reaction diagram
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-
-
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Acetyl-Pro-Ala-Pro-Phe-NH2 + H2O
Acetyl-Pro-Ala-Pro-Phe-OH + NH3
show the reaction diagram
-
-
-
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Acetyl-Pro-Ala-Pro-Phe-NH2 + H2O
Acetyl-Pro-Ala-Pro-Phe-OH + NH3
show the reaction diagram
-
hydrolyzed at the amide bond only
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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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-
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Peptide + H2O
Hydrolyzed peptide + H2O
show the reaction diagram
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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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-
-
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Succinyl-Ala-Ala-Pro-Phe-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
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-
-
-
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Acetyl-Pro-Ala-Pro-Tyr-NH2 + H2O
Acetyl-Pro-Ala-Pro-Tyr-OH + NH3
show the reaction diagram
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-
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additional information
?
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model of serine protease catalytic tetrahedral intermediates
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INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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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Soybean trypsin inhibitor
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Streptomyces subtilisin inhibitor
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-
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Turkey ovomucoid third domain
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-
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KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.45
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Acetyl-Pro-Ala-Leu-Phe-NH2
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-
0.02
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Acetyl-Pro-Ala-Pro-Phe-Leu-NH2
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-
0.54
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Acetyl-Pro-Ala-Pro-Phe-NH2
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-
0.15
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Acetyl-Pro-Ala-Pro-Phe-Tyr-NH2
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-
0.87
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Acetyl-Pro-Ala-Pro-Trp-NH2
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-
0.047
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succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
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-
0.045
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Succinyl-Ala-Ala-Pro-Phe-4-methylcoumarin 7-amide
-
-
1.4
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Acetyl-Pro-Ala-Pro-Tyr-NH2
-
-
additional information
-
additional information
-
-
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TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.04
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Acetyl-Ala-Ala-Tyr-4-methylcoumarin 7-amide
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-
5.1
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Acetyl-Pro-Ala-Leu-Phe-NH2
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-
20
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Acetyl-Pro-Ala-Pro-Phe-Leu-NH2
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5.8
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Acetyl-Pro-Ala-Pro-Phe-NH2
-
-
56.8
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Acetyl-Pro-Ala-Pro-Phe-Tyr-NH2
-
-
0.1
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Acetyl-Pro-Ala-Pro-Trp-NH2
-
-
285
-
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
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-
6.9
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Succinyl-Ala-Ala-Pro-Phe-4-methylcoumarin 7-amide
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10.1
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Acetyl-Pro-Ala-Pro-Tyr-NH2
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-
additional information
-
additional information
-
-
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TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
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assay at
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
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structure at 2.8 A resolution
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Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene structure
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