Information on EC 3.9.1.2 - protein arginine phosphatase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.9.1.2
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RECOMMENDED NAME
GeneOntology No.
protein arginine phosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a [protein]-Nomega-phospho-L-arginine + H2O = a [protein]-L-arginine + phosphate
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
[protein]-Nomega-phospho-L-arginine phosphohydrolase
The enzyme, characterized from Gram-positive bacteria, hydrolyses the phosphoramidate (P-N) bond of Nomega-phospho-L-arginine residues in proteins and peptides that were phosphorylated by EC 2.7.14.1, protein-arginine-kinase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(N-omega-phospho Arg)n + H2O
(Arg)n + n phosphate
show the reaction diagram
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-
-
-
?
(Nomega-phospho-Arg-Gly-Glu)6 + H2O
(Arg-Gly-Glu)6 + 6 phosphate
show the reaction diagram
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-
-
-
?
(Nomega-phospho-Arg-Gly-Phe)6 + H2O
(Arg-Gly-Phe)6 + 6 phosphate
show the reaction diagram
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-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
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-
-
?
KpRGGGGYIKIIKV + H2O
KRGGGGYIKIIKV + phosphate
show the reaction diagram
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hydrolysis of the phosphoramidate bond of phospho-arginine residues in peptides
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-
?
phospho-L-arginine + H2O
L-arginine + phosphate
show the reaction diagram
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-
-
-
?
[culpeine]-Nomega-phospho-L-arginine + H2O
[culpeine]-L-arginine + phosphate
show the reaction diagram
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-
-
-
?
[histone VIII]-Nomega-phospho-L-arginine + H2O
[histone VIII]-L-arginine + phosphate
show the reaction diagram
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-
-
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?
[histone V]-Nomega-phospho-L-arginine + H2O
[histone V]-L-arginine + phosphate
show the reaction diagram
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-
-
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?
[salmine]-Nomega-phospho-L-arginine + H2O
[salmine]-L-arginine + phosphate
show the reaction diagram
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-
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?
additional information
?
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enzyme releases phosphate from Nomega-phosphoarginine residues of phosphopeptides
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-{(2S)-1-amino-5-[(2-imino-2,5-dihydro-1,3-selenazol-4-yl)amino]-1-oxopentan-2-yl}benzamide
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irreversible inhibition, kinact/KI is 310 per M and min, by inducing disulfide bond formation between the two active site cysteine residues
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.87
(N-omega-phospho Arg)n
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pH 7.5, 30C
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0.42
(Nomega-phospho-Arg-Gly-Glu)6
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pH 7.5, 30C
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1.74
(Nomega-phospho-Arg-Gly-Phe)6
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pH 7.5, 30C
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100 - 115
4-nitrophenyl phosphate
0.34
phospho-L-arginine
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pH 7.5, 30C
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0.87
[culpeine]-Nomega-phospho-L-arginine
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pH 7.5, 30C
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0.35
[histone VIII]-Nomega-phospho-L-arginine
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pH 7.5, 30C
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0.51
[histone V]-Nomega-phospho-L-arginine
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pH 7.5, 30C
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0.79
[salmine]-Nomega-phospho-L-arginine
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pH 7.5, 30C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19 - 1.12
4-nitrophenyl phosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00169 - 0.011
4-nitrophenyl phosphate
136
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with phosphate.The phosphate-binding site is formed by the side chain of Arg13, the backbone amides of the phosphate-loop and the positive end of the macrodipole of helix H1, which together generate a highly positively charged pocket at the bottom of the substrate-binding cleft. The substrate-mimicking Arg149 is sandwiched between Thr11, Asp118, and Phe120 with its guanidinium group hydrogen bonding to Asp118. Structure of mutant C7S in complex with phosphate shows the formation of a covalent phospho-Ser7 adduct indicating that the crystallized mutant mimics the phospho-enzyme intermediate of the dephosphorylation reaction
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C14S
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mutation of auxiliary cysteine residue present in the active site, significant resuction in kcat value
C7S
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structure in complex with phosphate shows the formation of a covalent phospho-Ser7 adduct indicating that the crystallized mutant mimics the phospho-enzyme intermediate of the dephosphorylation reaction
C9S
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mutation of active site cysteine, complete loss of activity
D118A
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complete loss of activity
F120A
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60fold reduction of specific activity
T11I
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18fold reduction of specific activity with phospho-arginine substrates, marked increasing in the activity toward phospho-tyrosine substrates
T11V
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18fold reduction of specific activity with phospho-arginine substrates, marked increasing in the activity toward phospho-tyrosine substrates
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis