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Information on EC 3.4.11.B7 - arginyl aminopeptidase PH1704 and Organism(s) Pyrococcus horikoshii and UniProt Accession O59413

for references in articles please use BRENDA:EC3.4.11.B7
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.B7 arginyl aminopeptidase PH1704
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Pyrococcus horikoshii
UNIPROT: O59413
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The taxonomic range for the selected organisms is: Pyrococcus horikoshii
The expected taxonomic range for this enzyme is: Pyrococcus horikoshii
Reaction Schemes
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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
Synonyms
ph1704, arginine-specific aminopeptidase, ph1704 protease, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
arginine-specific aminopeptidase
-
PH1704 protease
ambiguous, the recombinant protein is also identified as a cysteine endopeptidase
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
Glu12 is responsible for substrate binding
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
show the reaction diagram
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
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
the enzyme is also identified as an cysteine endopeptidase. Activity with the endopeptidase substrate Ala-Ala-Phe-Arg-7-amido-4-methylcoumarin is 10% compared to the activity with the aminopeptidase substrate L-Arg-7-amido-4-methylcoumarin. The enzyme exhibits primal aminopeptidase activity. 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
-
-
?
L-Asp-7-amido-4-methylcoumarin + H2O
L-Asp + 7-amino-4-methylcoumarin
show the reaction diagram
the specific activity for hydrolyzing L-Arg-7-amino-4-methylcoumarin is 90times to 300times higher than those hydrolyzing L-Asp-7-amino-4-methylcoumarin, L-Ala-7-amino-4-methylcoumarin, L-Val-7-amino-4-methylcoumarin, L-Phe-7-amino-4-methylcoumarin or L-Ser-7-amino-4-methylcoumarin. Arginine, phenylalanine, alanine, valine, aspartate, and serine substrates are hydrolyzed with decreasing efficiency, in that order
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
show the reaction diagram
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
-
-
?
L-Ser-7-amido-4-methylcoumarin + H2O
L-Ser + 7-amino-4-methylcoumarin
show the reaction diagram
the specific activity for hydrolyzing L-Arg-7-amino-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
-
-
?
L-Val-7-amido-4-methylcoumarin + H2O
L-Val + 7-amino-4-methylcoumarin
show the reaction diagram
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
5 mM, 29% inhibition of protease activity
Co2+
0.2 mM, 75% inhibition of protease activity
Cu2+
0.2 mM, 57% inhibition of protease activity
Fe3+
0.2 mM, 27% inhibition of protease activity
K+
5 mM, 19% inhibition of protease activity
Mg2+
5 mM, 10% inhibition of protease activity
Mn2+
5 mM, 81% inhibition of protease activity
Na+
5 mM, 28% inhibition of protease activity
Ni2+
0.2 mM, 84% inhibition of protease activity
Zn2+
0.2 mM, 63% inhibition of protease activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iodoacetamide
strongly inhibits the peptidase activity, confirming that Cys100 is a nucleophilic residue
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
200000
the most active form of the protein is a partially SDS-resistant, multimeric complex
240000
non-denaturing PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
in the crystal, the enzyme forms a hexameric ring structure, and the active sites are formed at the interfaces between three pairs of monomers
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure at 2 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E12T
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
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhan, D.; Han, W.; Feng, Y.
Experimental and computational studies indicate the mutation of Glu12 to increase the thermostability of oligomeric protease from Pyrococcus horikoshii
J. Mol. Model.
17
1241-1249
2011
Pyrococcus horikoshii (O59413), Pyrococcus horikoshii DSM 12428 (O59413)
Manually annotated by BRENDA team
Zhan, D.; Bai, A.; Yu, L.; Han, W.; Feng, Y.
Characterization of the PH1704 protease from Pyrococcus horikoshii OT3 and the critical functions of Tyr120
PLoS One
9
e103902
2014
Pyrococcus horikoshii (O59413), Pyrococcus horikoshii DSM 12428 (O59413)
Manually annotated by BRENDA team
Du, X.; Choi, I.G.; Kim, R.; Wang, W.; Jancarik, J.; Yokota, H.; Kim, S.H.
Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2 A resolution
Proc. Natl. Acad. Sci. USA
97
14079-14084
2000
Pyrococcus horikoshii (O59413), Pyrococcus horikoshii, Pyrococcus horikoshii DSM 12428 (O59413)
Manually annotated by BRENDA team