Information on EC 3.9.1.3 - phosphohistidine phosphatase

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

EC NUMBER
COMMENTARY hide
3.9.1.3
-
RECOMMENDED NAME
GeneOntology No.
phosphohistidine phosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a [protein]-N-phospho-L-histidine + H2O = a [protein]-L-histidine + phosphate
show the reaction diagram
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-
-
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SYSTEMATIC NAME
IUBMB Comments
[protein]-N-phospho-L-histidine phosphohydrolase
This eukaryotic enzyme dephosphorylates phosphorylated histidine residues within proteins and peptides. The enzyme acts on phosphate groups attached to both the pros- and tele-nitrogen atoms, but the pros- position is somewhat preferred (by a factor of two at the most) [4]. The substrate specificity depends on the amino acid sequence or structural context of the phosphohistidine in a phosphoprotein. The enzyme is also active on free phosphoramidate [1,4] and peptide-bound phospholysine [5].
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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
a [CheA protein]-N-phospho-L-histidine + H2O
a [CheA protein]-L-histidine + phosphate
show the reaction diagram
a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
show the reaction diagram
AKR-N-phospho-HKV + H2O
AKRHKV + phosphate
show the reaction diagram
-
-
-
-
?
succinyl-L-Ala-N-phospho-L-His-L-Pro-L-Phe 4-nitroanilide + H2O
succinyl-L-Ala-L-His-L-Pro-L-Phe 4-nitroanilide + phosphate
show the reaction diagram
VIFIE-N-phospho-HAKRKG + H2O
VIFIEHAKRKG + phosphate
show the reaction diagram
-
-
-
-
?
[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
show the reaction diagram
[histidine kinase ArcB]-N-phospho-L-histidine + H2O
[histidine kinase ArcB]-L-histidine + phosphate
show the reaction diagram
-
-
-
-
?
[histone H4]-N-phospho-L-histidine + H2O
[histone H4]-L-histidine + phosphate
show the reaction diagram
[KCa3.1 channel protein]-N-phospho-L-histidine + H2O
[KCa3.1 channel protein]-L-histidine + phosphate
show the reaction diagram
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the enzyme directly binds and inhibits KCa3.1 by dephosphorylating histidine 358
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-
?
[protein]-N-phospho-L-histidine + H2O
[protein]-L-histidine + phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
a [CheA protein]-N-phospho-L-histidine + H2O
a [CheA protein]-L-histidine + phosphate
show the reaction diagram
a [protein]-N-phospho-L-histidine + H2O
a [protein]-L-histidine + phosphate
show the reaction diagram
[ATP-citrate lyase]-N-phospho-L-histidine + H2O
[ATP-citrate lyase]-L-histidine + phosphate
show the reaction diagram
[histidine kinase ArcB]-N-phospho-L-histidine + H2O
[histidine kinase ArcB]-L-histidine + phosphate
show the reaction diagram
-
-
-
-
?
[histone H4]-N-phospho-L-histidine + H2O
[histone H4]-L-histidine + phosphate
show the reaction diagram
[KCa3.1 channel protein]-N-phospho-L-histidine + H2O
[KCa3.1 channel protein]-L-histidine + phosphate
show the reaction diagram
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the enzyme directly binds and inhibits KCa3.1 by dephosphorylating histidine 358
-
-
?
[protein]-N-phospho-L-histidine + H2O
[protein]-L-histidine + phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
130% activity at 5 mM
Mn2+
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122% activity at 5 mM
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
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73% residual activity at 5 mM
Inhibitor-2
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N-ethylmaleimide
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74% residual activity at 1 mM
okadaic acid
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Calmodulin
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115% activity at 5 mM Ca2+ plus 0.01 mM calmodulin
iodoacetamide
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131% activity at 1 mM
additional information
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slightly increased activity in the presence of 5,5'-dithiobis-2-nitrobenzoic acid and GSH
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0028
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crude enzyme, at pH 7.5 and 30°C
0.06
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cell lysate, mutant enzyme R45A, pH and temperature not specified in the publication
0.2
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purified mutant enzyme R45A, pH and temperature not specified in the publication
0.3
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cell lysate, mutant enzyme R78A, pH and temperature not specified in the publication
0.4
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cell lysate, mutant enzyme H81A, pH and temperature not specified in the publication; cell lysate, wild type enzyme, pH and temperature not specified in the publication
0.9
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purified mutant enzyme R78A, pH and temperature not specified in the publication
1.4
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purified mutant enzyme H81A, pH and temperature not specified in the publication
1.8
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purified wild type enzyme, pH and temperature not specified in the publication
2.72
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after 971fold purification, at pH 7.5 and 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6 - 9
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16300
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1 * 16300, recombinant enzyme, SDS-PAGE
113000
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gel filtration
209000
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gel filtration
600000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
multimer
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x * 16000, MALDI-TOF mass spectrometry or SDS-PAGE, the enzyme forms multimers consisting of up to more than 35 protein molecules
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
free and tungstate-bound enzyme forms, vapor diffusion method
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hanging drop vapor diffusion method, with 20 mM CaCl2, 50 mM NaCl, 0.5 mM dithiothreitol and 6% (w/v) PEG 6 K using a reservoir containing 100 mM MES-K buffer (pH 6.6), 40 mM CaCl2, 50 mM NaCl and 12% (w/v) PEG 6 K at 10°C
free enzyme and in phosphate-bound state
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hanging drop vapor diffusion method, using 2.0 M ammonium sulfate and 0.1 M Bis-tris, pH 5.5
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Blue Sepharose column chromatography, and Superdex 75 gel filtration
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, Mono-Q column chromatography, and Sephacryl S-100 gel filtration
DE-52 cellulose column chromatography
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DEAE-cellulose column chromatography, Sephadex G-200 gel filtration, Mono-Q column chromatography, and Superose 12 gel filtration
HiTrap column chromatography and Superdex 75 gel filtration
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Mono Q column chromatography
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MonoQ column chromatography
Ni-NTA agarose column chromatography
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Ni-NTA agarose column chromatography, and gel filtration
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Ni-NTA column chromatography
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Ni2+-NTA agarose column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in CHO cells
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Top10 cells
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expressed in Sf9 insect cells
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expressed in SH-SY5Y cells and in primary cultures of cortical neurons from embryonic (E19) rats
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
long-term exposure (24 h) of INS 832/13 cells or rat islets to high glucose (30 mM) increases the expression of the enzyme. Such increases in enzyme expression are also seen in islets derived from the Zucker diabetic fatty rat compared with islets from the lean control animals
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C69A
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the mutation does not affect enzyme activity
C69A/C71A
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the mutations do not affect enzyme activity
C69A/C71A/C73A
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the mutations do not affect enzyme activity
C69A/C73A
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the mutation s do not affect enzyme activity
C71A
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the mutation does not affect enzyme activity
C71A/C73A
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the mutations do not affect enzyme activity
C73A
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the mutation does not affect enzyme activity
G75A
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inacvtive
G75A/G77A/S80A
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inactive
G77A
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inacvtive
H102A
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inactive
H81A
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the mutant shows wild type activity
R45A
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the specific activity of the mutant is decreased by one order of magnitude compared to the wild type enzyme
R78A
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the specific activity of the mutant is decreased by about 30% compared to the wild type enzyme
H53A
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inactive
additional information
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deletion of 9 N-terminal amino acids results in inactive enzyme, while 4 C-terminal residues can be deleted without losing enzyme activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine