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Enzyme Nomenclature
Information on EC 3.9.1.2 - protein arginine phosphatase
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
3.9.1.2
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RECOMMENDED NAME
GeneOntology No.
protein arginine phosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a [protein]-Nomega-phospho-L-arginine + H2O = a [protein]-L-arginine + phosphate
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-
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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.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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an enzyme deletion strain accumulates arginine phosphorylated proteins and allows for identification of 121 phosphorylation sites for 87 proteins. Protein arginine phosphorylation has a functional role and is involved in the regulation of many critical cellular processes, such as protein degradation, motility, competence, and stringent and stress responses
physiological function
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a mutant lacking the YwlE arginine phosphatase accumulates a strikingly large number of arginine phosphorylations i.e. 217 sites in 134 proteins, however only a minor fraction of these sites is increasingly modified during heat shock or oxidative stress. The main proteins accumulating comprise central factors of the stress response system including the CtsR and HrcA heat shock repressors, as well as major components of the protein quality control system such as the ClpCP protease and the GroEL chaperonine
physiological function
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a mutant lacking the YwlE arginine phosphatase accumulates a strikingly large number of arginine phosphorylations i.e. 217 sites in 134 proteins, however only a minor fraction of these sites is increasingly modified during heat shock or oxidative stress. The main proteins accumulating comprise central factors of the stress response system including the CtsR and HrcA heat shock repressors, as well as major components of the protein quality control system such as the ClpCP protease and the GroEL chaperonine
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
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-
-
?
KpRGGGGYIKIIKV + H2O
KRGGGGYIKIIKV + phosphate
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hydrolysis of the phosphoramidate bond of phospho-arginine residues in peptides
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-
?
[culpeine]-Nomega-phospho-L-arginine + H2O
[culpeine]-L-arginine + phosphate
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-
-
-
?
[histone VIII]-Nomega-phospho-L-arginine + H2O
[histone VIII]-L-arginine + phosphate
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-
-
-
?
[histone V]-Nomega-phospho-L-arginine + H2O
[histone V]-L-arginine + phosphate
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-
-
-
?
[salmine]-Nomega-phospho-L-arginine + H2O
[salmine]-L-arginine + phosphate
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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
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C9A
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
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
C9A
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substrate-trapping mutant, retains binding affinity toward arginine-phosphorylated proteins but cannot hydrolyze the captured substrates. Mutant C9A stably binds to arginine-phosphorylated proteins
C9A
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substrate-trapping mutant, retains binding affinity toward arginine-phosphorylated proteins but cannot hydrolyze the captured substrates. Mutant C9A stably binds to arginine-phosphorylated proteins
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
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development of a substrate-trapping mutant that retains binding affinity toward arginine-phosphorylated proteins but cannot hydrolyze the captured substrates. Mutant C9A stably binds to arginine-phosphorylated proteins. The substrate-trapping efficiency is improved by impeding the oligomerization of the phosphatase mutant. The engineered YwlE trap efficiently captures arginine-phosphorylated proteins from complex Bacillus subtilis ywlE- cell extracts, thus facilitating identification of phosphoarginine sites in the large pool of cellular protein modifications
analysis
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development of a substrate-trapping mutant that retains binding affinity toward arginine-phosphorylated proteins but cannot hydrolyze the captured substrates. Mutant C9A stably binds to arginine-phosphorylated proteins. The substrate-trapping efficiency is improved by impeding the oligomerization of the phosphatase mutant. The engineered YwlE trap efficiently captures arginine-phosphorylated proteins from complex Bacillus subtilis ywlE- cell extracts, thus facilitating identification of phosphoarginine sites in the large pool of cellular protein modifications
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LINKS TO OTHER DATABASES (specific for EC-Number 3.9.1.2)
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