Information on EC 3.4.11.B7 - arginyl aminopeptidase PH1704

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The expected taxonomic range for this enzyme is: Pyrococcus horikoshii

EC NUMBER
COMMENTARY hide
3.4.11.B7
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
arginyl aminopeptidase PH1704
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
the enzyme is an aminopeptidase with limited specificity, mainly releasing the N-terminal L-arginine and hardly cleaving other amino acids. L-Arg-7-amido-4-methylcoumarin is the best artificial substrate
show the reaction diagram
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ala-Ala-Phe-Arg-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
show the reaction diagram
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
L-Asp-7-amido-4-methylcoumarin + H2O
L-Asp + 7-amino-4-methylcoumarin
show the reaction diagram
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
L-Ser-7-amido-4-methylcoumarin + H2O
L-Ser + 7-amino-4-methylcoumarin
show the reaction diagram
L-Val-7-amido-4-methylcoumarin + H2O
L-Val + 7-amino-4-methylcoumarin
show the reaction diagram
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the specific activity for hydrolyzing L-Arg-7-amido-4-methylcoumarin is 90times to 300times higher than those hydrolyzing L-Asp-7-amido-4-methylcoumarin, L-Ala-7-amido-4-methylcoumarin, L-Val-7-amido-4-methylcoumarin, L-Phe-7-amido-4-methylcoumarin or L-Ser-7-amido-4-methylcoumarin. Arginine, phenylalanine, alanine, valine, aspartate, and serine substrates are hydrolyzed with decreasing efficiency, in that order
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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5 mM, 29% inhibition of protease activity
Co2+
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0.2 mM, 75% inhibition of protease activity
Cu2+
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0.2 mM, 57% inhibition of protease activity
Fe3+
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0.2 mM, 27% inhibition of protease activity
K+
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5 mM, 19% inhibition of protease activity
Mg2+
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5 mM, 10% inhibition of protease activity
Mn2+
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5 mM, 81% inhibition of protease activity
Na+
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5 mM, 28% inhibition of protease activity
Ni2+
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0.2 mM, 84% inhibition of protease activity
Zn2+
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0.2 mM, 63% inhibition of protease activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iodoacetamide
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strongly inhibits the peptidase activity, confirming that Cys100 is a nucleophilic residue
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
200000
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the most active form of the protein is a partially SDS-resistant, multimeric complex
240000
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non-denaturing PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
hexamer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure at 2 A resolution
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85
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mutant enzyme E12T is more stable than wild-type at 85°C
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E12T
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protease activity of E12T is 3.8 fold higher than that of wild-type enzyme. The mutant is more stable than wild-type at 85°C
Y120P
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kat and kat/Km of the mutant enzyme with L-Arg-7-amino-4-methylcoumarin are about 7 and 7.8times higher than that of the wild type enzyme, respectively
E12T
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protease activity of E12T is 3.8 fold higher than that of wild-type enzyme. The mutant is more stable than wild-type at 85°C
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Y120P
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kat and kat/Km of the mutant enzyme with L-Arg-7-amino-4-methylcoumarin are about 7 and 7.8times higher than that of the wild type enzyme, respectively
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