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Information on EC 3.1.3.15 - histidinol-phosphatase
for references in articles please use BRENDA:EC3.1.3.15
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.3 Phosphoric-monoester hydrolases
3.1.3.15 histidinol-phosphatase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 3.1.3.15
-
photosensitizer
-
photodynamic
-
trinuclear
-
phosphoesterase
-
polxs
-
mthpc
- drug development
showSynonyms
mthpp, impl2, histidinol phosphatase, histidinol-phosphate phosphatase, holpase, histidinol phosphate phosphatase, sco5208, cg0910, ton_0887, cg0911, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cg0910
Cg0911
Cgl0800
D-erythro-imidazoleglycerol phosphate dehydratase-histidinol phosphate phosphatase
-
-
-
-
HisB-N
-
N-terminal domain of the bifunctional enzyme HisB with histidinol phosphate phosphatase activity
hisN
HisPPase
histidinol phosphatase
-
-
-
-
histidinol phosphate phosphatase
histidinol-P-phosphatase
-
-
-
-
histidinol-phosphate phosphatase
histidinolphosphatase
-
-
-
-
histinol-phosphate phosphatase
HOL-P phosphatase
Hol-Pase
HolPase
HP phosphatase
-
-
-
-
HPP
HPpase
-
-
-
-
imidazoleglycerol phosphate dehydratase-histidinol phosphate phosphatase
-
-
-
-
IMPase-like HolPase
inositol monophosphatase-like HolPase
L-histidinol phosphatase
-
-
-
-
L-histidinol phosphate phosphatase
L-histidinol-phosphate phosphatase
-
-
-
-
Mtb HolPase
PA0335
Rv3137
histidinol phosphate phosphatase
-
-
-
-
histinol-phosphate phosphatase
myoinositol monophosphatase-like2, IMPL2
HolPase
-
-
-
-
HolPase
-
member of the DDDD phosphohydrolase/phosphotransferase superfamily
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-histidinol phosphate + H2O = L-histidinol + phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
L-histidine biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
L-histidinol-phosphate phosphohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
9025-79-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-histidinol 1-phosphate + H2O
L-histidinol + phosphate
Substrates: 105% of the activity with D-myo-inositol1-phosphate
Products: -
Products: -
?
L-phosphoserine + H2O
L-serine + phosphate
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: low activity
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: low activity
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: low activity
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: low activity
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: low activity
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: low activity
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: the enzyme encoded by the Rv3137 gene, belonging to the inositol monophosphatase (IMPase) family, functions as the Mtb HolPase and specifically dephosphorylates histidinol phosphate
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: the enzyme encoded by the Rv3137 gene, belonging to the inositol monophosphatase (IMPase) family, functions as the Mtb HolPase and specifically dephosphorylates histidinol phosphate
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: the enzyme encoded by the Rv3137 gene, belonging to the inositol monophosphatase (IMPase) family, functions as the Mtb HolPase and specifically dephosphorylates histidinol phosphate
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
Substrates: the enzyme catalyses the eigthth step of histidine biosynthesis
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
Substrates: the enzyme catalyses the eigthth step of histidine biosynthesis
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
Substrates: -
Products: -
Products: -
?
N-formyl-L-histidinol phosphate + H2O
N-formyl-L-histidinol + phosphate
Substrates: the rate of hydrolysis of N-formyl-L-histidinol phosphate is less than 1% of the rate of hydrolysis of L-histidinol phosphate at pH 8.5
Products: -
Products: -
?
N-formyl-L-histidinol phosphate + H2O
N-formyl-L-histidinol + phosphate
Substrates: the rate of hydrolysis of N-formyl-L-histidinol phosphate is less than 1% of the rate of hydrolysis of L-histidinol phosphate at pH 8.5
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: 4-nitrophenyl phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: no substrate: 4-nitrophenyl phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: no substrate: 4-nitrophenyl phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: no substrate: 4-nitrophenyl phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: no substrate: 4-nitrophenyl phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: 4-nitrophenyl phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with inositol monophosphate by wild-type or mutant Mtb HolPases. Phosphate detection with malachite green
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with inositol monophosphate by wild-type or mutant Mtb HolPases. Phosphate detection with malachite green
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with inositol monophosphate by wild-type or mutant Mtb HolPases. Phosphate detection with malachite green
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with inositol monophosphate by wild-type or mutant Mtb HolPases. Phosphate detection with malachite green
Products: -
Products: -
?
additional information
?
-
-
Substrates: does not show any phosphatase activity with p-nitrophenyl phosphate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-histidinol phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
?
-
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Substrates: -
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
-
Substrates: the enzyme catalyses the eigthth step of histidine biosynthesis
Products: -
Products: -
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
Substrates: the enzyme catalyses the eigthth step of histidine biosynthesis
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Fe2+
Mg2+
Mn2+
Ni2+
Zn2+
additional information
Co2+
-
shifts optimal pH to 6.5, decreases Km at pH 6.5
Mg2+
assay in presence of 5 mM, Km value 0.65 mM, Hill coefficient 2.44
Mg2+
a divalent cation is required, saturation kinetics for Mtb HolPase with Mg2+ as a cofactor, the specificity constant (kcat/Km) with Zn2+ is 1.16fold higher compared to Mg2+, metal binding in the active site of Mtb HolPase, structure, overview
Mn2+
-
shifts optimal pH to 6.5, decreases Km at pH 6.5
Zn2+
-
the presence of a structural Zn2+ ion stabilizes the conformation of an extended loop
Zn2+
a divalent cation is required, saturation kinetics for Mtb HolPase with Zn2+ as a cofactor, the specificity constant (kcat/Km) with Zn2+ is 1.16fold higher compared to Mg2+, Michaelis-Menten kinetics, overview
Zn2+
-
shifts optimal pH to 6.5, decreases Km at pH 6.5
additional information
-
no activating effect by Zn2+, Cu2+, Ca2+, Mi2+, and Fe2+ at 5 mM
additional information
no activating effect by Zn2+, Cu2+, Ca2+, Mi2+, and Fe2+ at 5 mM
additional information
no activating effect by Zn2+, Cu2+, Ca2+, Mi2+, and Fe2+ at 5 mM
additional information
-
no activating effect on activity by Zn2+, Cu2+, Ca2+, Mi2+, and Fe2+ at 5 mM
additional information
no activating effect on activity by Zn2+, Cu2+, Ca2+, Mi2+, and Fe2+ at 5 mM
additional information
no activating effect on activity by Zn2+, Cu2+, Ca2+, Mi2+, and Fe2+ at 5 mM
additional information
the enzyme does not show any significant increases in catalytic activity when Zn2+, Mn2+, Co2+ or Ni2+ are added
additional information
-
the enzyme does not show any significant increases in catalytic activity when Zn2+, Mn2+, Co2+ or Ni2+ are added
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-[(1-(R))-1-(2,6-dichloro-4-fluorophenyl)ethoxy]-5-(1-piperidin-4-ylpyrazol-4-yl)pyridin-2-amine
NSC756645
4-chloro-1-N,3-N-bis[4-(4,5-dihydro-1H-imidazol-2-yl)phenyl]benzene-1,3-dicarboxamide
NSC67436
5,11-dimethyl-2-(2-piperidin-1-ylethyl)-6H-pyrido[4,3-b]carbazol-2-ium-9-ol
NSC311153, best tested inhibitor
5,5'-dithiobis(2-nitrobenzoic acid)
-
inhibits more rapidly at pH 7 than at pH 8.5
[(1S,4aR,10aR)-1,4a-dimethyl-7-propan-2-yl-2,3,4,9,10,10a-hexahydrophenanthren-1-yl]methanamine benzoic acid
NSC65238
EDTA
10 mM, complete loss of activity; 10 mM, complete loss of activity
p-chloromercuribenzoate
-
competitive
additional information
-
no inhibitory effect is observed by L-histidine at up to 60 mM L-histidine, by phosphate at up to 0.25 mM, or by L-histidinol at 20 mM; no inhibitory effect of L-histidine is observed with concentrations up to 60 mM L-histidine
-
additional information
no inhibitory effect is observed by L-histidine at up to 60 mM L-histidine, by phosphate at up to 0.25 mM, or by L-histidinol at 20 mM; no inhibitory effect of L-histidine is observed with concentrations up to 60 mM L-histidine
-
additional information
no inhibitory effect is observed by L-histidine at up to 60 mM L-histidine, by phosphate at up to 0.25 mM, or by L-histidinol at 20 mM; no inhibitory effect of L-histidine is observed with concentrations up to 60 mM L-histidine
-
additional information
identification of several small-molecule inhibitors of the enzyme by target-based screening against HolPase, high-throughput compound library screening
-
additional information
-
identification of several small-molecule inhibitors of the enzyme by target-based screening against HolPase, high-throughput compound library screening
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-histidinol
about 5% activation at 10 mM and above. Cg0911 is positively feedback regulated by L-histidinol
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma
A photosensitizer delivered by bispecific antibody redirected T lymphocytes enhances cytotoxicity against EpCAM-expressing carcinoma cells upon light irradiation.
Dermatitis, Phototoxic
Polymeric micelle nanoparticles for photodynamic treatment of head and neck cancer cells.
Head and Neck Neoplasms
Characterization and Optimization of mTHPP Nanoparticles for Photodynamic Therapy of Head and Neck Cancer.
Neoplasms
Malignant Drosophila tumors interrupt insulin signaling to induce cachexia-like wasting.
Neoplasms
Tumors overcome the action of the wasting factor ImpL2 by locally elevating Wnt/Wingless.
Tuberculosis
Identification and structural characterization of a histidinol phosphate phosphatase from Mycobacterium tuberculosis.
Tuberculosis
Mechanistic insights into the enzymatic activity and inhibition of the replicative polymerase exonuclease domain from Mycobacterium tuberculosis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.37
D-fructose 6-phosphate
-
in the presence of 1 mM Co2+, at 80°C and pH 6.5
1.45
L-phosphoserine
-
in the presence of 1 mM Co2+, at 80°C and pH 6.5
0.0236
L-histidinol phosphate
pH 7.4, 30°C, Hill coefficient 1.47
0.03
L-histidinol phosphate
-
in the presence of Mn2+, at 80°C and pH 6.5
0.03198
L-histidinol phosphate
pH 8.0, 37°C, recombinant enzyme
0.041
L-histidinol phosphate
-
in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Zn2+
0.05
L-histidinol phosphate
-
in the presence of Co2+, at 80°C and pH 6.5
0.052
L-histidinol phosphate
-
in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Mn2+
0.054
L-histidinol phosphate
-
in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Co2+
0.054
L-histidinol phosphate
-
in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Mg2+
0.09
L-histidinol phosphate
-
in the presence of Mg2+, at 80°C and pH 6.5
0.09
L-histidinol phosphate
-
in the presence of Ni2+, at 80°C and pH 6.5
0.14
L-histidinol phosphate
mutant enzyme D228N, at pH 9.0 and 22°C
0.638
L-histidinol phosphate
pH 7.4, 30°C, Hill coefficient 1.47
0.74
L-histidinol phosphate
mutant enzyme Y117F, at pH 9.0 and 22°C
1.3
L-histidinol phosphate
mutant enzyme H42N, at pH 9.0 and 22°C
1.5
L-histidinol phosphate
mutant enzyme R160M, at pH 9.0 and 22°C
1.7
L-histidinol phosphate
mutant enzyme E115Q, at pH 9.0 and 22°C
1.7
L-histidinol phosphate
mutant enzyme HY157F, at pH 9.0 and 22°C
1.9
L-histidinol phosphate
wild type enzyme, at pH 9.0 and 22°C
2.3
L-histidinol phosphate
mutant enzyme Y161F, at pH 9.0 and 22°C
2.5
L-histidinol phosphate
mutant enzyme Y161A, at pH 9.0 and 22°C
4.5
L-histidinol phosphate
mutant enzyme R197M, at pH 9.0 and 22°C
5.4
L-histidinol phosphate
mutant enzyme Y117A, at pH 9.0 and 22°C
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11
D-fructose 6-phosphate
-
in the presence of 1 mM Co2+, at 80°C and pH 6.5
14
L-phosphoserine
-
in the presence of 1 mM Co2+, at 80°C and pH 6.5
0.031
L-histidinol phosphate
mutant enzyme D228N, at pH 9.0 and 22°C
0.62
L-histidinol phosphate
mutant enzyme H42N, at pH 9.0 and 22°C
0.74
L-histidinol phosphate
mutant enzyme R160M, at pH 9.0 and 22°C
0.99
L-histidinol phosphate
pH 8.0, 37°C, recombinant enzyme
20 - 50
L-histidinol phosphate
-
in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Co2+
31
L-histidinol phosphate
mutant enzyme E115Q, at pH 9.0 and 22°C
38
L-histidinol phosphate
mutant enzyme R197M, at pH 9.0 and 22°C
48
L-histidinol phosphate
mutant enzyme Y161A, at pH 9.0 and 22°C
53
L-histidinol phosphate
mutant enzyme Y117A, at pH 9.0 and 22°C
61
L-histidinol phosphate
mutant enzyme HY157F, at pH 9.0 and 22°C
110
L-histidinol phosphate
mutant enzyme Y117F, at pH 9.0 and 22°C
174
L-histidinol phosphate
wild type enzyme, at pH 9.0 and 22°C
180
L-histidinol phosphate
mutant enzyme Y161F, at pH 9.0 and 22°C
260
L-histidinol phosphate
-
in the presence of 1 mM Co2+, at 80°C and pH 6.5
290
L-histidinol phosphate
-
in the presence of 1 mM Ni2+, at 80°C and pH 6.5
320
L-histidinol phosphate
-
in the presence of 1 mM Mn2+, at 80°C and pH 6.5
420
L-histidinol phosphate
-
in the presence of 1 mM Mg2+, at 80°C and pH 6.5
960
L-histidinol phosphate
-
in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Mn2+
1410
L-histidinol phosphate
-
in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Zn2+
2140
L-histidinol phosphate
-
in 25 mM Tris-HCl (pH 7.5), 70 nM enzyme, 0.025 mM Mg2+, and 0.2 mM histidinol phosphate, at 25°C, in the presence of 0.05 mM Mg2+
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002
L-histidinol phosphate
pH 7.4, 30°C, Hill coefficient 1.47
0.22
L-histidinol phosphate
mutant enzyme D228N, at pH 9.0 and 22°C
0.48
L-histidinol phosphate
mutant enzyme H42N, at pH 9.0 and 22°C
0.49
L-histidinol phosphate
mutant enzyme R160M, at pH 9.0 and 22°C
8.5
L-histidinol phosphate
mutant enzyme R197M, at pH 9.0 and 22°C
9.8
L-histidinol phosphate
mutant enzyme Y117A, at pH 9.0 and 22°C
18
L-histidinol phosphate
mutant enzyme E115Q, at pH 9.0 and 22°C
25
L-histidinol phosphate
mutant enzyme Y161A, at pH 9.0 and 22°C
30.96
L-histidinol phosphate
pH 8.0, 37°C, recombinant enzyme
36
L-histidinol phosphate
mutant enzyme HY157F, at pH 9.0 and 22°C
44.1
L-histidinol phosphate
pH 7.4, 30°C, Hill coefficient 1.47
79
L-histidinol phosphate
mutant enzyme Y161F, at pH 9.0 and 22°C
150
L-histidinol phosphate
mutant enzyme Y117F, at pH 9.0 and 22°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.09425
5,11-dimethyl-2-(2-piperidin-1-ylethyl)-6H-pyrido[4,3-b]carbazol-2-ium-9-ol
Mycobacterium tuberculosis
pH 8.0, 37°C, recombinant enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.5
-
in the absence of divalent metal ions
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9.5
recombinant enzyme, activity range, profile overview
7 - 10
recombinant enzyme, maximal Cg0911 activity is observed at around pH 8 and is only little reduced at pH 7.35, followed by a sharp loss in activity towards more acidic conditions. The drop in activity towards more alkaline conditions is less pronounced, the enzyme exhibits still 30% of its activity at around pH 10, profile overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
35 - 40
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
maximal Cg0911 activity at 30°C and less than 5% of this activity remains at 40°C, profile overview
20 - 50
maximal HisN activity at 35-40°C, no activity at 50°C, profile overview
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
strain L120 containing pSS503 or pSH 368 compared with strain L120
-
-
brenda
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
isoform Impl2, catalyzes both the reactions of EC 3.1.3.15 and 3.1.3.25
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
distribution of HisN orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
evolution
distribution of Cg0911 orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
evolution
enzyme Mtb HolPase belongs to the IMPase family, it is not an active inositol monophosphate phosphatase (IMPase) but a histidinol phosphate phosphatase (HolPase)
evolution
enzyme Hol-Pase belongs to the haloacid dehalogenase (HAD) family, which catalyzes phosphoryl group transfer of a variety of substrates. HAD family members include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, and P-type ATPase. They all use aspartate as an active-site residue for nucleophilic catalysis and contain four highly conserved motifs, namely, hhhDxDx(T/V) (L/V)h, hhhhhh (S/T), [KR], and (G/S) (D/S)x023-4 (D/E) hhhh (where h represents a hydrophobic residue and x any amino acid)
evolution
-
enzyme Mtb HolPase belongs to the IMPase family, it is not an active inositol monophosphate phosphatase (IMPase) but a histidinol phosphate phosphatase (HolPase)
-
evolution
-
distribution of HisN orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
-
evolution
-
distribution of Cg0911 orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
-
evolution
-
distribution of HisN orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
-
evolution
-
distribution of Cg0911 orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
-
evolution
-
enzyme Hol-Pase belongs to the haloacid dehalogenase (HAD) family, which catalyzes phosphoryl group transfer of a variety of substrates. HAD family members include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, and P-type ATPase. They all use aspartate as an active-site residue for nucleophilic catalysis and contain four highly conserved motifs, namely, hhhDxDx(T/V) (L/V)h, hhhhhh (S/T), [KR], and (G/S) (D/S)x023-4 (D/E) hhhh (where h represents a hydrophobic residue and x any amino acid)
-
evolution
-
enzyme Mtb HolPase belongs to the IMPase family, it is not an active inositol monophosphate phosphatase (IMPase) but a histidinol phosphate phosphatase (HolPase)
-
evolution
-
enzyme Hol-Pase belongs to the haloacid dehalogenase (HAD) family, which catalyzes phosphoryl group transfer of a variety of substrates. HAD family members include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, and P-type ATPase. They all use aspartate as an active-site residue for nucleophilic catalysis and contain four highly conserved motifs, namely, hhhDxDx(T/V) (L/V)h, hhhhhh (S/T), [KR], and (G/S) (D/S)x023-4 (D/E) hhhh (where h represents a hydrophobic residue and x any amino acid)
-
evolution
-
enzyme Hol-Pase belongs to the haloacid dehalogenase (HAD) family, which catalyzes phosphoryl group transfer of a variety of substrates. HAD family members include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, and P-type ATPase. They all use aspartate as an active-site residue for nucleophilic catalysis and contain four highly conserved motifs, namely, hhhDxDx(T/V) (L/V)h, hhhhhh (S/T), [KR], and (G/S) (D/S)x023-4 (D/E) hhhh (where h represents a hydrophobic residue and x any amino acid)
-
evolution
-
enzyme Hol-Pase belongs to the haloacid dehalogenase (HAD) family, which catalyzes phosphoryl group transfer of a variety of substrates. HAD family members include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, and P-type ATPase. They all use aspartate as an active-site residue for nucleophilic catalysis and contain four highly conserved motifs, namely, hhhDxDx(T/V) (L/V)h, hhhhhh (S/T), [KR], and (G/S) (D/S)x023-4 (D/E) hhhh (where h represents a hydrophobic residue and x any amino acid)
-
evolution
-
enzyme Hol-Pase belongs to the haloacid dehalogenase (HAD) family, which catalyzes phosphoryl group transfer of a variety of substrates. HAD family members include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, and P-type ATPase. They all use aspartate as an active-site residue for nucleophilic catalysis and contain four highly conserved motifs, namely, hhhDxDx(T/V) (L/V)h, hhhhhh (S/T), [KR], and (G/S) (D/S)x023-4 (D/E) hhhh (where h represents a hydrophobic residue and x any amino acid)
-
evolution
-
enzyme Hol-Pase belongs to the haloacid dehalogenase (HAD) family, which catalyzes phosphoryl group transfer of a variety of substrates. HAD family members include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, and P-type ATPase. They all use aspartate as an active-site residue for nucleophilic catalysis and contain four highly conserved motifs, namely, hhhDxDx(T/V) (L/V)h, hhhhhh (S/T), [KR], and (G/S) (D/S)x023-4 (D/E) hhhh (where h represents a hydrophobic residue and x any amino acid)
-
evolution
-
enzyme Hol-Pase belongs to the haloacid dehalogenase (HAD) family, which catalyzes phosphoryl group transfer of a variety of substrates. HAD family members include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, and P-type ATPase. They all use aspartate as an active-site residue for nucleophilic catalysis and contain four highly conserved motifs, namely, hhhDxDx(T/V) (L/V)h, hhhhhh (S/T), [KR], and (G/S) (D/S)x023-4 (D/E) hhhh (where h represents a hydrophobic residue and x any amino acid)
-
evolution
-
distribution of HisN orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
-
evolution
-
distribution of Cg0911 orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
-
evolution
-
distribution of HisN orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
-
evolution
-
distribution of Cg0911 orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
-
evolution
-
distribution of HisN orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
-
evolution
-
distribution of Cg0911 orthologues within bacteria, sequences and structure motifs comparisons, phylogenetic analysis, overview
-
malfunction
deletion of the histidinol-phosphate phosphatase gene hisN results in histidine auxotrophy
malfunction
deletion of hisN in Corynebacterium glutamicum results in pronounced L-histidine bradytrophy instead of complete auxotrophy. Growth of the DELTAhisN mutant is visible after several days of incubation on minimal medium plates without L-histidine. Addition of L-histidine abolishes the observed growth defect completely. Complementation of the DELTAhisN growth defect is observed with gene cg0911
malfunction
a transposon mutant of Pseudomonas aeruginosa displays a growth defect on glucose-containing minimal solid medium. The growth defect is due to incomplete histidine auxotrophy caused by inactivation of gene PA0335 which encodes enzyme histidinol phosphate phosphatase (Hol-Pase). Genes involved in the histidine biosynthesis in PAO1. In addition to PA0335, the roles of 12 other predicted genes involved in histidine biosynthesis in Pseudomonas aeruginosa are examined. Among them, hisC2 (PA3165), hisH2 (PA3152), and hisF2 (PA3151) are found to be dispensable for histidine synthesis, whereas hisG (PA4449), hisE (PA5067), hisF1 (PA5140), hisB (PA5143), hisI (PA5066), hisC1 (PA4447), and hisA (PA5141) are essential because deletion of each results in complete histidine auxotrophy; similar to the case for PA0335, hisH1 (PA5142) or hisD (PA4448) deletion causes incomplete histidine auxotrophy
malfunction
-
deletion of hisN in Corynebacterium glutamicum results in pronounced L-histidine bradytrophy instead of complete auxotrophy. Growth of the DELTAhisN mutant is visible after several days of incubation on minimal medium plates without L-histidine. Addition of L-histidine abolishes the observed growth defect completely. Complementation of the DELTAhisN growth defect is observed with gene cg0911
-
malfunction
-
deletion of hisN in Corynebacterium glutamicum results in pronounced L-histidine bradytrophy instead of complete auxotrophy. Growth of the DELTAhisN mutant is visible after several days of incubation on minimal medium plates without L-histidine. Addition of L-histidine abolishes the observed growth defect completely. Complementation of the DELTAhisN growth defect is observed with gene cg0911
-
malfunction
-
a transposon mutant of Pseudomonas aeruginosa displays a growth defect on glucose-containing minimal solid medium. The growth defect is due to incomplete histidine auxotrophy caused by inactivation of gene PA0335 which encodes enzyme histidinol phosphate phosphatase (Hol-Pase). Genes involved in the histidine biosynthesis in PAO1. In addition to PA0335, the roles of 12 other predicted genes involved in histidine biosynthesis in Pseudomonas aeruginosa are examined. Among them, hisC2 (PA3165), hisH2 (PA3152), and hisF2 (PA3151) are found to be dispensable for histidine synthesis, whereas hisG (PA4449), hisE (PA5067), hisF1 (PA5140), hisB (PA5143), hisI (PA5066), hisC1 (PA4447), and hisA (PA5141) are essential because deletion of each results in complete histidine auxotrophy; similar to the case for PA0335, hisH1 (PA5142) or hisD (PA4448) deletion causes incomplete histidine auxotrophy
-
malfunction
-
a transposon mutant of Pseudomonas aeruginosa displays a growth defect on glucose-containing minimal solid medium. The growth defect is due to incomplete histidine auxotrophy caused by inactivation of gene PA0335 which encodes enzyme histidinol phosphate phosphatase (Hol-Pase). Genes involved in the histidine biosynthesis in PAO1. In addition to PA0335, the roles of 12 other predicted genes involved in histidine biosynthesis in Pseudomonas aeruginosa are examined. Among them, hisC2 (PA3165), hisH2 (PA3152), and hisF2 (PA3151) are found to be dispensable for histidine synthesis, whereas hisG (PA4449), hisE (PA5067), hisF1 (PA5140), hisB (PA5143), hisI (PA5066), hisC1 (PA4447), and hisA (PA5141) are essential because deletion of each results in complete histidine auxotrophy; similar to the case for PA0335, hisH1 (PA5142) or hisD (PA4448) deletion causes incomplete histidine auxotrophy
-
malfunction
-
a transposon mutant of Pseudomonas aeruginosa displays a growth defect on glucose-containing minimal solid medium. The growth defect is due to incomplete histidine auxotrophy caused by inactivation of gene PA0335 which encodes enzyme histidinol phosphate phosphatase (Hol-Pase). Genes involved in the histidine biosynthesis in PAO1. In addition to PA0335, the roles of 12 other predicted genes involved in histidine biosynthesis in Pseudomonas aeruginosa are examined. Among them, hisC2 (PA3165), hisH2 (PA3152), and hisF2 (PA3151) are found to be dispensable for histidine synthesis, whereas hisG (PA4449), hisE (PA5067), hisF1 (PA5140), hisB (PA5143), hisI (PA5066), hisC1 (PA4447), and hisA (PA5141) are essential because deletion of each results in complete histidine auxotrophy; similar to the case for PA0335, hisH1 (PA5142) or hisD (PA4448) deletion causes incomplete histidine auxotrophy
-
malfunction
-
a transposon mutant of Pseudomonas aeruginosa displays a growth defect on glucose-containing minimal solid medium. The growth defect is due to incomplete histidine auxotrophy caused by inactivation of gene PA0335 which encodes enzyme histidinol phosphate phosphatase (Hol-Pase). Genes involved in the histidine biosynthesis in PAO1. In addition to PA0335, the roles of 12 other predicted genes involved in histidine biosynthesis in Pseudomonas aeruginosa are examined. Among them, hisC2 (PA3165), hisH2 (PA3152), and hisF2 (PA3151) are found to be dispensable for histidine synthesis, whereas hisG (PA4449), hisE (PA5067), hisF1 (PA5140), hisB (PA5143), hisI (PA5066), hisC1 (PA4447), and hisA (PA5141) are essential because deletion of each results in complete histidine auxotrophy; similar to the case for PA0335, hisH1 (PA5142) or hisD (PA4448) deletion causes incomplete histidine auxotrophy
-
malfunction
-
a transposon mutant of Pseudomonas aeruginosa displays a growth defect on glucose-containing minimal solid medium. The growth defect is due to incomplete histidine auxotrophy caused by inactivation of gene PA0335 which encodes enzyme histidinol phosphate phosphatase (Hol-Pase). Genes involved in the histidine biosynthesis in PAO1. In addition to PA0335, the roles of 12 other predicted genes involved in histidine biosynthesis in Pseudomonas aeruginosa are examined. Among them, hisC2 (PA3165), hisH2 (PA3152), and hisF2 (PA3151) are found to be dispensable for histidine synthesis, whereas hisG (PA4449), hisE (PA5067), hisF1 (PA5140), hisB (PA5143), hisI (PA5066), hisC1 (PA4447), and hisA (PA5141) are essential because deletion of each results in complete histidine auxotrophy; similar to the case for PA0335, hisH1 (PA5142) or hisD (PA4448) deletion causes incomplete histidine auxotrophy
-
malfunction
-
a transposon mutant of Pseudomonas aeruginosa displays a growth defect on glucose-containing minimal solid medium. The growth defect is due to incomplete histidine auxotrophy caused by inactivation of gene PA0335 which encodes enzyme histidinol phosphate phosphatase (Hol-Pase). Genes involved in the histidine biosynthesis in PAO1. In addition to PA0335, the roles of 12 other predicted genes involved in histidine biosynthesis in Pseudomonas aeruginosa are examined. Among them, hisC2 (PA3165), hisH2 (PA3152), and hisF2 (PA3151) are found to be dispensable for histidine synthesis, whereas hisG (PA4449), hisE (PA5067), hisF1 (PA5140), hisB (PA5143), hisI (PA5066), hisC1 (PA4447), and hisA (PA5141) are essential because deletion of each results in complete histidine auxotrophy; similar to the case for PA0335, hisH1 (PA5142) or hisD (PA4448) deletion causes incomplete histidine auxotrophy
-
malfunction
-
a transposon mutant of Pseudomonas aeruginosa displays a growth defect on glucose-containing minimal solid medium. The growth defect is due to incomplete histidine auxotrophy caused by inactivation of gene PA0335 which encodes enzyme histidinol phosphate phosphatase (Hol-Pase). Genes involved in the histidine biosynthesis in PAO1. In addition to PA0335, the roles of 12 other predicted genes involved in histidine biosynthesis in Pseudomonas aeruginosa are examined. Among them, hisC2 (PA3165), hisH2 (PA3152), and hisF2 (PA3151) are found to be dispensable for histidine synthesis, whereas hisG (PA4449), hisE (PA5067), hisF1 (PA5140), hisB (PA5143), hisI (PA5066), hisC1 (PA4447), and hisA (PA5141) are essential because deletion of each results in complete histidine auxotrophy; similar to the case for PA0335, hisH1 (PA5142) or hisD (PA4448) deletion causes incomplete histidine auxotrophy
-
malfunction
-
deletion of hisN in Corynebacterium glutamicum results in pronounced L-histidine bradytrophy instead of complete auxotrophy. Growth of the DELTAhisN mutant is visible after several days of incubation on minimal medium plates without L-histidine. Addition of L-histidine abolishes the observed growth defect completely. Complementation of the DELTAhisN growth defect is observed with gene cg0911
-
malfunction
-
deletion of hisN in Corynebacterium glutamicum results in pronounced L-histidine bradytrophy instead of complete auxotrophy. Growth of the DELTAhisN mutant is visible after several days of incubation on minimal medium plates without L-histidine. Addition of L-histidine abolishes the observed growth defect completely. Complementation of the DELTAhisN growth defect is observed with gene cg0911
-
malfunction
-
deletion of hisN in Corynebacterium glutamicum results in pronounced L-histidine bradytrophy instead of complete auxotrophy. Growth of the DELTAhisN mutant is visible after several days of incubation on minimal medium plates without L-histidine. Addition of L-histidine abolishes the observed growth defect completely. Complementation of the DELTAhisN growth defect is observed with gene cg0911
-
metabolism
enzyme histidinol phosphate phosphatase (Hol-Pase) is responsible for the penultimate step of histidine biosynthesis. Genes involved in the histidine biosynthesis in PAO1 and related enzyme functions, overview
metabolism
enzyme IMP is involved in the network of the inositol phosphate (IP) and phosphoinositide (PI) signaling pathway, together with the stress responding processes, such as the abscisic acid pathway, Ca2+ release, and ROS generation, inositol phosphatases in the plant inositol (Ins) signaling pathways under stress, overview. Isozyme IMPL2 is involved in seed development and the histidine biosynthesis. Inositol phosphatases and their inositol-related substrates analyzed in Arabidopsis thaliana, overview
metabolism
-
enzyme histidinol phosphate phosphatase (Hol-Pase) is responsible for the penultimate step of histidine biosynthesis. Genes involved in the histidine biosynthesis in PAO1 and related enzyme functions, overview
-
metabolism
-
enzyme histidinol phosphate phosphatase (Hol-Pase) is responsible for the penultimate step of histidine biosynthesis. Genes involved in the histidine biosynthesis in PAO1 and related enzyme functions, overview
-
metabolism
-
enzyme histidinol phosphate phosphatase (Hol-Pase) is responsible for the penultimate step of histidine biosynthesis. Genes involved in the histidine biosynthesis in PAO1 and related enzyme functions, overview
-
metabolism
-
enzyme histidinol phosphate phosphatase (Hol-Pase) is responsible for the penultimate step of histidine biosynthesis. Genes involved in the histidine biosynthesis in PAO1 and related enzyme functions, overview
-
metabolism
-
enzyme histidinol phosphate phosphatase (Hol-Pase) is responsible for the penultimate step of histidine biosynthesis. Genes involved in the histidine biosynthesis in PAO1 and related enzyme functions, overview
-
metabolism
-
enzyme histidinol phosphate phosphatase (Hol-Pase) is responsible for the penultimate step of histidine biosynthesis. Genes involved in the histidine biosynthesis in PAO1 and related enzyme functions, overview
-
metabolism
-
enzyme histidinol phosphate phosphatase (Hol-Pase) is responsible for the penultimate step of histidine biosynthesis. Genes involved in the histidine biosynthesis in PAO1 and related enzyme functions, overview
-
physiological function
gene cg0911 encodes an enzyme with HolPase activity, the hisN paralogue gene cg0911 can complement the growth defect of mutant DELTAhisN. Enzyme Cg0911 is positively feedback regulated by L-histidinol
physiological function
the enzyme encoded by the Rv3137 gene, belonging to the inositol monophosphatase (IMPase) family, functions as the Mtb HolPase and specifically dephosphorylates histidinol phosphate
physiological function
IMPase-like HPPs play a role only in His biosynthesis
physiological function
the PA0335-encoded protein is a Hol-Pase with alkaline phosphatase activity
physiological function
myo-inositol-3-phosphate (Ins3P) is dephosphorylated by inositol monophosphatase (IMP) to form inositol. IMP is also responsible for the dephosphorylation of myo-inositol-4-phosphate (Ins4P). As an important component in biosynthesis and degradation of myo-inositol and its derivatives, inositol phosphatases could hydrolyze the phosphate of the inositol ring, thus affecting inositol signaling. Inositol signaling is believed to play a crucial role in various aspects of plant growth and adaptation. Isozyme IMPL2 is involved in seed development and the histidine biosynthesis, IMPL2 is a histidinol-phosphate phosphatase affecting histone biosynthesis pathways
physiological function
-
the enzyme encoded by the Rv3137 gene, belonging to the inositol monophosphatase (IMPase) family, functions as the Mtb HolPase and specifically dephosphorylates histidinol phosphate
-
physiological function
-
gene cg0911 encodes an enzyme with HolPase activity, the hisN paralogue gene cg0911 can complement the growth defect of mutant DELTAhisN. Enzyme Cg0911 is positively feedback regulated by L-histidinol
-
physiological function
-
gene cg0911 encodes an enzyme with HolPase activity, the hisN paralogue gene cg0911 can complement the growth defect of mutant DELTAhisN. Enzyme Cg0911 is positively feedback regulated by L-histidinol
-
physiological function
-
the PA0335-encoded protein is a Hol-Pase with alkaline phosphatase activity
-
physiological function
-
the enzyme encoded by the Rv3137 gene, belonging to the inositol monophosphatase (IMPase) family, functions as the Mtb HolPase and specifically dephosphorylates histidinol phosphate
-
physiological function
-
the PA0335-encoded protein is a Hol-Pase with alkaline phosphatase activity
-
physiological function
-
the PA0335-encoded protein is a Hol-Pase with alkaline phosphatase activity
-
physiological function
-
the PA0335-encoded protein is a Hol-Pase with alkaline phosphatase activity
-
physiological function
-
the PA0335-encoded protein is a Hol-Pase with alkaline phosphatase activity
-
physiological function
-
the PA0335-encoded protein is a Hol-Pase with alkaline phosphatase activity
-
physiological function
-
the PA0335-encoded protein is a Hol-Pase with alkaline phosphatase activity
-
physiological function
-
gene cg0911 encodes an enzyme with HolPase activity, the hisN paralogue gene cg0911 can complement the growth defect of mutant DELTAhisN. Enzyme Cg0911 is positively feedback regulated by L-histidinol
-
physiological function
-
gene cg0911 encodes an enzyme with HolPase activity, the hisN paralogue gene cg0911 can complement the growth defect of mutant DELTAhisN. Enzyme Cg0911 is positively feedback regulated by L-histidinol
-
physiological function
-
gene cg0911 encodes an enzyme with HolPase activity, the hisN paralogue gene cg0911 can complement the growth defect of mutant DELTAhisN. Enzyme Cg0911 is positively feedback regulated by L-histidinol
-
additional information
-
importance of a highly conserved aspartate residue accompanied by several aromatic amino acid residues present in motif 5 for HolPase activity
additional information
importance of a highly conserved aspartate residue accompanied by several aromatic amino acid residues present in motif 5 for HolPase activity
additional information
importance of a highly conserved aspartate residue accompanied by several aromatic amino acid residues present in motif 5 for HolPase activity
additional information
the cocrystal structure of Mtb HolPase with HOLP reveals a unique mode of substrate binding, a multizinc active-site pocket, and a product-exit channel. Dephosphorylation mechanism of Mtb Hol-Pase, overview
additional information
-
the cocrystal structure of Mtb HolPase with HOLP reveals a unique mode of substrate binding, a multizinc active-site pocket, and a product-exit channel. Dephosphorylation mechanism of Mtb Hol-Pase, overview
additional information
the histidinol phosphate dephosphorylation reaction occurs at the interface between N- and C-terminal domains, structure-function relationship, active site structure with bound substrate, overview
additional information
-
the histidinol phosphate dephosphorylation reaction occurs at the interface between N- and C-terminal domains, structure-function relationship, active site structure with bound substrate, overview
additional information
detailed enzyme structure analysis of structure PDB ID 5EQA at 1.32 A resolution, mass spectrometric analysis, overview. Residues Lys158/subunit A and Cys245/subunit B are involved in formation of Cys-Lys bridges in enzyme HPP
additional information
-
the cocrystal structure of Mtb HolPase with HOLP reveals a unique mode of substrate binding, a multizinc active-site pocket, and a product-exit channel. Dephosphorylation mechanism of Mtb Hol-Pase, overview
-
additional information
-
importance of a highly conserved aspartate residue accompanied by several aromatic amino acid residues present in motif 5 for HolPase activity
-
additional information
-
importance of a highly conserved aspartate residue accompanied by several aromatic amino acid residues present in motif 5 for HolPase activity
-
additional information
-
the cocrystal structure of Mtb HolPase with HOLP reveals a unique mode of substrate binding, a multizinc active-site pocket, and a product-exit channel. Dephosphorylation mechanism of Mtb Hol-Pase, overview
-
additional information
-
importance of a highly conserved aspartate residue accompanied by several aromatic amino acid residues present in motif 5 for HolPase activity
-
additional information
-
importance of a highly conserved aspartate residue accompanied by several aromatic amino acid residues present in motif 5 for HolPase activity
-
additional information
-
importance of a highly conserved aspartate residue accompanied by several aromatic amino acid residues present in motif 5 for HolPase activity
-
Show AA Sequence and Transmembrane Helices (19716 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
19903
-
2 * 19903, in the presence of Mg2+ and histidinol phosphate, ESI mass spectrometry
29976
46000
52000
-
disc gel electrophoresis
46000
-
Mn2+ precipitiation, antibody affinity chromatography, selective proteolysis
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homotetramer
additional information
?
-
x * 16000-18000, SDS-PAGE
dimer
-
2 * 19903, in the presence of Mg2+ and histidinol phosphate, ESI mass spectrometry
dimer
2 * 30378, recombinant enzyme, mass spectrometry, the monomer is with the N-terminal SNA linker that resides after cleavage with tobacco etch virus protease, plus the difference from the two added methylene groups (24 Da) with SNAMSS adduct (577.6 Da) that most probably is an artifact resulting from the MS experiment
homotetramer
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
4 * 29500, dynamic light scattering
-
homotetramer
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
4 * 29976, calculated from sequence of cDNA
-
additional information
covalent dimerization of MtHPP, a monomer of MtHPP has an alphabetaalphabetaalpha-sandwich-like arrangement. The N-terminal domain, which forms an alpha + beta structure, covers residues from the N-terminus to Glu201. Two long alpha-helices (alpha1 and alpha2) are separated by a mobile loop. The eight-stranded beta-sheet of the N-terminal domain contains a alpha-loop motif (residues 131-149), where the beta1 strand is flanked by strands beta2 and beta3. Moreover, a loop between strands beta3 and beta4 encompasses the helix beta3. Strands beta3-beta8 have antiparallel organization. The linker between the N- and C-terminal domains consists of residues between Val202 and Asp209. An extensive interface between the N- and C-terminal domains results in the rigidity of the entire structure, meaning that there is no hinge between the two domains, and they cannot move independently. The C-terminal domain, residues Leu210-Trp326, constitutes an alpha/beta/alpha fold, in which the mixed parallel/antiparallel beta-sheet is sandwiched between helices alpha6, eta7 (310 helix), and alpha8 from one side (close to the beta-sheet of the N-terminal domain) and eta4, alpha5, and alpha9 from the other. MtHPP dimeric assembly is stabilized by intermolecular Lys-CH2-Cys covalent bonds
additional information
-
covalent dimerization of MtHPP, a monomer of MtHPP has an alphabetaalphabetaalpha-sandwich-like arrangement. The N-terminal domain, which forms an alpha + beta structure, covers residues from the N-terminus to Glu201. Two long alpha-helices (alpha1 and alpha2) are separated by a mobile loop. The eight-stranded beta-sheet of the N-terminal domain contains a alpha-loop motif (residues 131-149), where the beta1 strand is flanked by strands beta2 and beta3. Moreover, a loop between strands beta3 and beta4 encompasses the helix beta3. Strands beta3-beta8 have antiparallel organization. The linker between the N- and C-terminal domains consists of residues between Val202 and Asp209. An extensive interface between the N- and C-terminal domains results in the rigidity of the entire structure, meaning that there is no hinge between the two domains, and they cannot move independently. The C-terminal domain, residues Leu210-Trp326, constitutes an alpha/beta/alpha fold, in which the mixed parallel/antiparallel beta-sheet is sandwiched between helices alpha6, eta7 (310 helix), and alpha8 from one side (close to the beta-sheet of the N-terminal domain) and eta4, alpha5, and alpha9 from the other. MtHPP dimeric assembly is stabilized by intermolecular Lys-CH2-Cys covalent bonds
additional information
the dimer is stabilized largely by hydrogen bonds, salt bridges, and van der Waals interactions. Asp189, Val149, Arg183, Asp202, Ala119, Arg171, Asn90, Arg93, Ile31, Arg122, and Ala186 of one monomer form hydrogen-bonding interactions with Arg185, Ile31, Asn90, Arg93, Arg122, Asp179, Tyr187, Gly199, Ser148, Gln121, and Ala186, respectively, of the other monomer and vice versa. There are two catalytic sites in the dimer, but only one product-exit channel shared by the two monomers at the dimer interface
additional information
-
the dimer is stabilized largely by hydrogen bonds, salt bridges, and van der Waals interactions. Asp189, Val149, Arg183, Asp202, Ala119, Arg171, Asn90, Arg93, Ile31, Arg122, and Ala186 of one monomer form hydrogen-bonding interactions with Arg185, Ile31, Asn90, Arg93, Arg122, Asp179, Tyr187, Gly199, Ser148, Gln121, and Ala186, respectively, of the other monomer and vice versa. There are two catalytic sites in the dimer, but only one product-exit channel shared by the two monomers at the dimer interface
additional information
-
the dimer is stabilized largely by hydrogen bonds, salt bridges, and van der Waals interactions. Asp189, Val149, Arg183, Asp202, Ala119, Arg171, Asn90, Arg93, Ile31, Arg122, and Ala186 of one monomer form hydrogen-bonding interactions with Arg185, Ile31, Asn90, Arg93, Arg122, Asp179, Tyr187, Gly199, Ser148, Gln121, and Ala186, respectively, of the other monomer and vice versa. There are two catalytic sites in the dimer, but only one product-exit channel shared by the two monomers at the dimer interface
-
additional information
-
the dimer is stabilized largely by hydrogen bonds, salt bridges, and van der Waals interactions. Asp189, Val149, Arg183, Asp202, Ala119, Arg171, Asn90, Arg93, Ile31, Arg122, and Ala186 of one monomer form hydrogen-bonding interactions with Arg185, Ile31, Asn90, Arg93, Arg122, Asp179, Tyr187, Gly199, Ser148, Gln121, and Ala186, respectively, of the other monomer and vice versa. There are two catalytic sites in the dimer, but only one product-exit channel shared by the two monomers at the dimer interface
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
25% (w/v) polyethylene glycol 3350, 0.2M MgCl2 and 0.1 M Tris-HCl (pH 8.5) by the sitting drop vapor diffusion, or 30% (w/v) polyethylene glycol monomethyl ether, 0.05 M CaCl2, and 0.1 M Bis-Tris (pH 6.5) by the micro-batch method
-
sitting drop vapor diffusion method, using 25% (w/v) PEG 4000, 0.1 M sodium acetate (pH 4.6), and 0.2 M ammonium sulfate
purified enzyme in complex with products histidiol or phosphate, or substrate histidinol phosphate with Mg2+, or Lys-CH2-Cys, sitting drop vapor diffusion, mixing of 19 mg/ml protein solution with crystallization solution containing 15% PEG 3350, and 0.2 M diammonium hydrogen phosphate, pH 8.0, or 30% PEG 3350, 0.1 M Bis-Tris, pH 6.5, 0.2 M ammonium acetate, and 10 mM magnesium acetate, over the reservoir supplemented with 100 mM formaldehyde to complete cross-linking between Lys158 and Cys245 and vitrified in Paraton-N, X-ray diffraction structure determination and analysis at 1.19-1.36 A resolution
purified recombinant enzyme, histidinol-phosphate phosphatase (mthpp) with intermolecular cross-link between Lys158 and Cys245, X-ray diffraction structure analysis of structure PDB ID 5EQA at 1.32 A resolution, mass spectrometric analysis
purified recombinant wild-type enzyme free or in complex with substrate histidinol phosphate, hanging drop vapor diffusion method, mixing of 0.0015 ml of protein solution containing 0.1 mM Zn2+ and 7.5 mM substrate for the complexed crystals, with 0.015 ml of reservoir solution containing 1 M ammonium sulfate, and 750 nl additive which is praseodymium (III) acetate hydrate, 35-40 days, 23°C, X-ray diffraction structure determination and analysis at 1.95 A and 2.90 A, respectively
vapour diffusion method with 0.68 M sodium malonate and 100 mM Tris-HCl (pH 8.5)
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G195R
conserved Gly, required for histinol-phosphate phosphatase activity
D228N
the mutant shows reduced catalytic efficiency and kcat is reduced by approximately 6000fold compared to the wild type enzyme
E115Q
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
H42N
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R197M
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Y117A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Y117F
the mutant shows increased catalytic efficiency compared to the wild type enzyme
Y157F
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Y161A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Y161F
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
D228N
-
the mutant shows reduced catalytic efficiency and kcat is reduced by approximately 6000fold compared to the wild type enzyme
-
H42N
-
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
-
additional information
additional information
-
generation of a DELTAhisN single mutant, a DELTAhisN DELTAcg0911 double mutant, and a quintuple mutant, lacking hisN and all its paralogues, phenotypes, overview. No further reduction of growth of the DELTAhisN DELTAcg0911 double or the DELTAhisN DELTAcg0911 DELTAimpA DELTAsuhB DELTAcysQ quintuple mutant as compared to the DELTAhisN single mutant. Supplementation with L-histidine results in the same growth of all mutants. Expression of impA, suhB or cysQ does not improve the growth of the DELTAhisN strain on minimal medium. Beside the complementation by hisN itself, a complementation of the DELTAhisN growth defect is only observed with cg0911. Although the complementation assay clearly demonstrates HolPase activity of the cg0911 gene product in vivo if expressed on a multiple copy plasmid, this activity does not account for L-histidine biosynthesis in a measurable degree if present in single copy under control of the native promotor
additional information
generation of a DELTAhisN single mutant, a DELTAhisN DELTAcg0911 double mutant, and a quintuple mutant, lacking hisN and all its paralogues, phenotypes, overview. No further reduction of growth of the DELTAhisN DELTAcg0911 double or the DELTAhisN DELTAcg0911 DELTAimpA DELTAsuhB DELTAcysQ quintuple mutant as compared to the DELTAhisN single mutant. Supplementation with L-histidine results in the same growth of all mutants. Expression of impA, suhB or cysQ does not improve the growth of the DELTAhisN strain on minimal medium. Beside the complementation by hisN itself, a complementation of the DELTAhisN growth defect is only observed with cg0911. Although the complementation assay clearly demonstrates HolPase activity of the cg0911 gene product in vivo if expressed on a multiple copy plasmid, this activity does not account for L-histidine biosynthesis in a measurable degree if present in single copy under control of the native promotor
additional information
generation of a DELTAhisN single mutant, a DELTAhisN DELTAcg0911 double mutant, and a quintuple mutant, lacking hisN and all its paralogues, phenotypes, overview. No further reduction of growth of the DELTAhisN DELTAcg0911 double or the DELTAhisN DELTAcg0911 DELTAimpA DELTAsuhB DELTAcysQ quintuple mutant as compared to the DELTAhisN single mutant. Supplementation with L-histidine results in the same growth of all mutants. Expression of impA, suhB or cysQ does not improve the growth of the DELTAhisN strain on minimal medium. Beside the complementation by hisN itself, a complementation of the DELTAhisN growth defect is only observed with cg0911. Although the complementation assay clearly demonstrates HolPase activity of the cg0911 gene product in vivo if expressed on a multiple copy plasmid, this activity does not account for L-histidine biosynthesis in a measurable degree if present in single copy under control of the native promotor
additional information
-
generation of a DELTAhisN single mutant, a DELTAhisN DELTAcg0911 double mutant, and a quintuple mutant, lacking hisN and all its paralogues, phenotypes, overview. No further reduction of growth of the DELTAhisN DELTAcg0911 double or the DELTAhisN DELTAcg0911 DELTAimpA DELTAsuhB DELTAcysQ quintuple mutant as compared to the DELTAhisN single mutant. Supplementation with L-histidine results in the same growth of all mutants. Expression of impA, suhB or cysQ does not improve the growth of the DELTAhisN strain on minimal medium. Beside the complementation by hisN itself, a complementation of the DELTAhisN growth defect is only observed with cg0911. Although the complementation assay clearly demonstrates HolPase activity of the cg0911 gene product in vivo if expressed on a multiple copy plasmid, this activity does not account for L-histidine biosynthesis in a measurable degree if present in single copy under control of the native promotor
-
additional information
-
generation of a DELTAhisN single mutant, a DELTAhisN DELTAcg0911 double mutant, and a quintuple mutant, lacking hisN and all its paralogues, phenotypes, overview. No further reduction of growth of the DELTAhisN DELTAcg0911 double or the DELTAhisN DELTAcg0911 DELTAimpA DELTAsuhB DELTAcysQ quintuple mutant as compared to the DELTAhisN single mutant. Supplementation with L-histidine results in the same growth of all mutants. Expression of impA, suhB or cysQ does not improve the growth of the DELTAhisN strain on minimal medium. Beside the complementation by hisN itself, a complementation of the DELTAhisN growth defect is only observed with cg0911. Although the complementation assay clearly demonstrates HolPase activity of the cg0911 gene product in vivo if expressed on a multiple copy plasmid, this activity does not account for L-histidine biosynthesis in a measurable degree if present in single copy under control of the native promotor
-
additional information
-
generation of a DELTAhisN single mutant, a DELTAhisN DELTAcg0911 double mutant, and a quintuple mutant, lacking hisN and all its paralogues, phenotypes, overview. No further reduction of growth of the DELTAhisN DELTAcg0911 double or the DELTAhisN DELTAcg0911 DELTAimpA DELTAsuhB DELTAcysQ quintuple mutant as compared to the DELTAhisN single mutant. Supplementation with L-histidine results in the same growth of all mutants. Expression of impA, suhB or cysQ does not improve the growth of the DELTAhisN strain on minimal medium. Beside the complementation by hisN itself, a complementation of the DELTAhisN growth defect is only observed with cg0911. Although the complementation assay clearly demonstrates HolPase activity of the cg0911 gene product in vivo if expressed on a multiple copy plasmid, this activity does not account for L-histidine biosynthesis in a measurable degree if present in single copy under control of the native promotor
-
additional information
-
generation of a DELTAhisN single mutant, a DELTAhisN DELTAcg0911 double mutant, and a quintuple mutant, lacking hisN and all its paralogues, phenotypes, overview. No further reduction of growth of the DELTAhisN DELTAcg0911 double or the DELTAhisN DELTAcg0911 DELTAimpA DELTAsuhB DELTAcysQ quintuple mutant as compared to the DELTAhisN single mutant. Supplementation with L-histidine results in the same growth of all mutants. Expression of impA, suhB or cysQ does not improve the growth of the DELTAhisN strain on minimal medium. Beside the complementation by hisN itself, a complementation of the DELTAhisN growth defect is only observed with cg0911. Although the complementation assay clearly demonstrates HolPase activity of the cg0911 gene product in vivo if expressed on a multiple copy plasmid, this activity does not account for L-histidine biosynthesis in a measurable degree if present in single copy under control of the native promotor
-
additional information
-
generation of a DELTAhisN single mutant, a DELTAhisN DELTAcg0911 double mutant, and a quintuple mutant, lacking hisN and all its paralogues, phenotypes, overview. No further reduction of growth of the DELTAhisN DELTAcg0911 double or the DELTAhisN DELTAcg0911 DELTAimpA DELTAsuhB DELTAcysQ quintuple mutant as compared to the DELTAhisN single mutant. Supplementation with L-histidine results in the same growth of all mutants. Expression of impA, suhB or cysQ does not improve the growth of the DELTAhisN strain on minimal medium. Beside the complementation by hisN itself, a complementation of the DELTAhisN growth defect is only observed with cg0911. Although the complementation assay clearly demonstrates HolPase activity of the cg0911 gene product in vivo if expressed on a multiple copy plasmid, this activity does not account for L-histidine biosynthesis in a measurable degree if present in single copy under control of the native promotor
-
additional information
inactivation of gene PA0335 causes incomplete auxotrophy of Pseudomonas aeruginosa strain PAO1, phenotype, overview. HisN from Corynebacterium glutamicum is cloned into mutant PAO1(DELTA0335) to produce the complementation strain PAO1(DELTA0335)C1. Consequently, PAO1(DELTA0335)C1 displays the same growth as the wild-type strain PAO1 and PAO1(DELTA0335)C on glucose-containing MM agar, whereas PA(DELTA0335) could not grow under the same conditions. Enzyme Hol-Pase from Corynebacterium glutamicum can completely complement the inactivation of gene PA0335 from Pseusomonas aeruginosa strain PAO1
additional information
-
inactivation of gene PA0335 causes incomplete auxotrophy of Pseudomonas aeruginosa strain PAO1, phenotype, overview. HisN from Corynebacterium glutamicum is cloned into mutant PAO1(DELTA0335) to produce the complementation strain PAO1(DELTA0335)C1. Consequently, PAO1(DELTA0335)C1 displays the same growth as the wild-type strain PAO1 and PAO1(DELTA0335)C on glucose-containing MM agar, whereas PA(DELTA0335) could not grow under the same conditions. Enzyme Hol-Pase from Corynebacterium glutamicum can completely complement the inactivation of gene PA0335 from Pseusomonas aeruginosa strain PAO1
-
additional information
-
inactivation of gene PA0335 causes incomplete auxotrophy of Pseudomonas aeruginosa strain PAO1, phenotype, overview. HisN from Corynebacterium glutamicum is cloned into mutant PAO1(DELTA0335) to produce the complementation strain PAO1(DELTA0335)C1. Consequently, PAO1(DELTA0335)C1 displays the same growth as the wild-type strain PAO1 and PAO1(DELTA0335)C on glucose-containing MM agar, whereas PA(DELTA0335) could not grow under the same conditions. Enzyme Hol-Pase from Corynebacterium glutamicum can completely complement the inactivation of gene PA0335 from Pseusomonas aeruginosa strain PAO1
-
additional information
-
inactivation of gene PA0335 causes incomplete auxotrophy of Pseudomonas aeruginosa strain PAO1, phenotype, overview. HisN from Corynebacterium glutamicum is cloned into mutant PAO1(DELTA0335) to produce the complementation strain PAO1(DELTA0335)C1. Consequently, PAO1(DELTA0335)C1 displays the same growth as the wild-type strain PAO1 and PAO1(DELTA0335)C on glucose-containing MM agar, whereas PA(DELTA0335) could not grow under the same conditions. Enzyme Hol-Pase from Corynebacterium glutamicum can completely complement the inactivation of gene PA0335 from Pseusomonas aeruginosa strain PAO1
-
additional information
-
inactivation of gene PA0335 causes incomplete auxotrophy of Pseudomonas aeruginosa strain PAO1, phenotype, overview. HisN from Corynebacterium glutamicum is cloned into mutant PAO1(DELTA0335) to produce the complementation strain PAO1(DELTA0335)C1. Consequently, PAO1(DELTA0335)C1 displays the same growth as the wild-type strain PAO1 and PAO1(DELTA0335)C on glucose-containing MM agar, whereas PA(DELTA0335) could not grow under the same conditions. Enzyme Hol-Pase from Corynebacterium glutamicum can completely complement the inactivation of gene PA0335 from Pseusomonas aeruginosa strain PAO1
-
additional information
-
inactivation of gene PA0335 causes incomplete auxotrophy of Pseudomonas aeruginosa strain PAO1, phenotype, overview. HisN from Corynebacterium glutamicum is cloned into mutant PAO1(DELTA0335) to produce the complementation strain PAO1(DELTA0335)C1. Consequently, PAO1(DELTA0335)C1 displays the same growth as the wild-type strain PAO1 and PAO1(DELTA0335)C on glucose-containing MM agar, whereas PA(DELTA0335) could not grow under the same conditions. Enzyme Hol-Pase from Corynebacterium glutamicum can completely complement the inactivation of gene PA0335 from Pseusomonas aeruginosa strain PAO1
-
additional information
-
inactivation of gene PA0335 causes incomplete auxotrophy of Pseudomonas aeruginosa strain PAO1, phenotype, overview. HisN from Corynebacterium glutamicum is cloned into mutant PAO1(DELTA0335) to produce the complementation strain PAO1(DELTA0335)C1. Consequently, PAO1(DELTA0335)C1 displays the same growth as the wild-type strain PAO1 and PAO1(DELTA0335)C on glucose-containing MM agar, whereas PA(DELTA0335) could not grow under the same conditions. Enzyme Hol-Pase from Corynebacterium glutamicum can completely complement the inactivation of gene PA0335 from Pseusomonas aeruginosa strain PAO1
-
additional information
-
inactivation of gene PA0335 causes incomplete auxotrophy of Pseudomonas aeruginosa strain PAO1, phenotype, overview. HisN from Corynebacterium glutamicum is cloned into mutant PAO1(DELTA0335) to produce the complementation strain PAO1(DELTA0335)C1. Consequently, PAO1(DELTA0335)C1 displays the same growth as the wild-type strain PAO1 and PAO1(DELTA0335)C on glucose-containing MM agar, whereas PA(DELTA0335) could not grow under the same conditions. Enzyme Hol-Pase from Corynebacterium glutamicum can completely complement the inactivation of gene PA0335 from Pseusomonas aeruginosa strain PAO1
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
54
-
50% loss of phosphatase activity in 2 min
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Ni2+), gel filtration
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography and gel filtration
TALON metal affinity column chromatography and Superdex 200 10/300 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene hisN or Rv3137, DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli and Mycobacterium smegmatis strain mc24517
gene PA0335, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, recombinant expression in Escherichia coli strain BL21(DE3)
His-tagged version expressed in Escherichia coli Rosetta (DE3) pLysS
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
drug development
the absence of a histidine biosynthesis pathway in humans, coupled with histidine essentiality for survival of the important human pathogen Mycobacterium tuberculosis (Mtb), underscores the importance of the bacterial enzymes of this pathway as major antituberculosis drug targets
drug development
-
the absence of a histidine biosynthesis pathway in humans, coupled with histidine essentiality for survival of the important human pathogen Mycobacterium tuberculosis (Mtb), underscores the importance of the bacterial enzymes of this pathway as major antituberculosis drug targets
-
drug development
-
the absence of a histidine biosynthesis pathway in humans, coupled with histidine essentiality for survival of the important human pathogen Mycobacterium tuberculosis (Mtb), underscores the importance of the bacterial enzymes of this pathway as major antituberculosis drug targets
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Staples, M.A.; Houston, L.L.
Purification of the bifunctional enzyme imidazoleglycerolphosphate dehydratase-histidinol phosphatase of Salmonella typhimurium
Biochim. Biophys. Acta
613
210-219
1980
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Brady, D.R.; Houston, L.L.
Some properties of the catalytic sites of imidazoleglycerol phosphate dehydratase-histidinol phosphate phosphatase, a bifunctional enzyme from Salmonella typhimurium
J. Biol. Chem.
248
2588-2592
1973
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Staples, M.A.; Houston, L.L.
Proteolytic degradation of imidazoleglycerolphosphate dehydratase-histidinol phosphatase from Salmonella typhimurium and the isolation of a resistant bifunctional core enzyme
J. Biol. Chem.
254
1395-1401
1979
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Sugiura, M.; Suzuki, S.; Kisumi M.
Improvement of histidine-producing strains of Serratia marcescens by cloning of a mutant allele of the histidine operon on a mini-F plasmid vector
Agric. Biol. Chem.
2
371-377
1987
Serratia marcescens
-
brenda
Carsiotis, M.; Jones R.F.
Cross-pathway regulation: tryptophan-mediated control of histidine and arginine biosynthetic enzymes in Neurospora crassa
J. Bacteriol.
119
889-892
1974
Neurospora crassa
brenda
Grisolia, V.; Carlomagno, M.S.; Bruni, C.B.
Cloning and expression of the distal portion of the histidine operon of Escherichia coli K-12
J. Bacteriol.
151
692-700
1982
Escherichia coli
brenda
Houston, L.L.; Graham, M.E.
Divalent metal Ion effects on a mutant histidinol phophate phosphatase from Samonella typhimurium
Arch. Biochem. Biophys.
162
513-522
1974
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium TA387
brenda
Araki, K.; Nakayama K.
A Biochemical characterization of histidine auxotrophs
Agric. Biol. Chem.
38
2219-2225
1974
Corynebacterium glutamicum
-
brenda
Houston, L.L.; Millay, Jr., H.
Effect of sulfhydryl reagents on the activity of histidinolphosphatase from Salmonella typhimurium and bakerss yeast
Biochim. Biophys. Acta
370
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Salmonella enterica subsp. enterica serovar Typhimurium, Saccharomyces cerevisiae
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Salmonella enterica subsp. enterica serovar Typhimurium, Saccharomyces cerevisiae
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Acta Crystallogr. Sect. D
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Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
brenda
Marineo, S.; Cusimano, M.G.; Limauro, D.; Coticchio, G.; Puglia, A.M.
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Streptomyces coelicolor
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Lee, H.S.; Cho, Y.; Lee, J.H.; Kang, S.G.
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Jung, H.I.; Lee, H.S.; An, Y.J.; Cho, Y.; Lee, J.H.; Kang, S.G.; Cha, S.S.
Crystallization and preliminary X-ray crystallographic analysis of a novel histidinol-phosphate phosphatase from Thermococcus onnurineus NA1
Acta Crystallogr. Sect. F
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Thermococcus onnurineus NA1 (B1PRL6), Thermococcus onnurineus NA1
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Petersen, L.N.; Marineo, S.; Mandala, S.; Davids, F.; Sewell, B.T.; Ingle, R.A.
The missing link in plant histidine biosynthesis: arabidopsis myoinositol monophosphatase-like2 encodes a functional histidinol-phosphate phosphatase
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Arabidopsis thaliana (Q6NPM8)
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Ghodge, S.V.; Fedorov, A.A.; Fedorov, E.V.; Hillerich, B.; Seidel, R.; Almo, S.C.; Raushel, F.M.
Structural and mechanistic characterization of L-histidinol phosphate phosphatase from the polymerase and histidinol phosphatase family of proteins
Biochemistry
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Lactococcus lactis subsp. lactis (Q02150), Lactococcus lactis subsp. lactis, Lactococcus lactis subsp. lactis IL1403 (Q02150)
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Kulis-Horn, R.K.; Persicke, M.; Kalinowski, J.
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Kulis-Horn, R.; Rueckert, C.; Kalinowski, J.; Persicke, M.
Sequence-based identification of inositol monophosphatase-like histidinol-phosphate phosphatases (HisN) in Corynebacterium glutamicum, Actinobacteria, and beyond
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Corynebacterium glutamicum, Corynebacterium glutamicum (Q8NS80), Corynebacterium glutamicum (Q8NS79), Corynebacterium glutamicum ATCC 13032 (Q8NS80), Corynebacterium glutamicum ATCC 13032 (Q8NS79), Corynebacterium glutamicum DSM 20300 (Q8NS80), Corynebacterium glutamicum DSM 20300 (Q8NS79), Corynebacterium glutamicum DSM 20300, Corynebacterium glutamicum JCM 1318 (Q8NS80), Corynebacterium glutamicum JCM 1318 (Q8NS79), Corynebacterium glutamicum LMG 3730 (Q8NS80), Corynebacterium glutamicum LMG 3730 (Q8NS79), Corynebacterium glutamicum NCIMB 10025 (Q8NS80), Corynebacterium glutamicum NCIMB 10025 (Q8NS79)
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Nourbakhsh, A.; Collakova, E.; Gillaspy, G.
Characterization of the inositol monophosphatase gene family in Arabidopsis
Front. Plant Sci.
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Arabidopsis thaliana (Q6NPM8)
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Ruszkowski, M.; Dauter, Z.
Structural studies of Medicago truncatula histidinol phosphate phosphatase from inositol monophosphatase superfamily reveal details of penultimate step of histidine biosynthesis in plants
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Medicago truncatula (G7J7Q5), Medicago truncatula
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Jha, B.; Kumar, D.; Sharma, A.; Dwivedy, A.; Singh, R.; Biswal, B.K.
Identification and structural characterization of a histidinol phosphate phosphatase from Mycobacterium tuberculosis
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Mycobacterium tuberculosis (P95189), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P95189), Mycobacterium tuberculosis ATCC 25618 (P95189)
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Wang, Y.; Wang, L.; Zhang, J.; Duan, X.; Feng, Y.; Wang, S.; Shen, L.
PA0335, a gene encoding histidinol phosphate phosphatase, mediates histidine auxotrophy in Pseudomonas aeruginosa
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Pseudomonas aeruginosa (Q9I6F6), Pseudomonas aeruginosa ATCC 15692 (Q9I6F6), Pseudomonas aeruginosa DSM 22644 (Q9I6F6), Pseudomonas aeruginosa CIP 104116 (Q9I6F6), Pseudomonas aeruginosa JCM 14847 (Q9I6F6), Pseudomonas aeruginosa LMG 12228 (Q9I6F6), Pseudomonas aeruginosa 1C (Q9I6F6), Pseudomonas aeruginosa PRS 101 (Q9I6F6)
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Jia, Q.; Kong, D.; Li, Q.; Sun, S.; Song, J.; Zhu, Y.; Liang, K.; Ke, Q.; Lin, W.; Huang, J.
The function of inositol phosphatases in plant tolerance to abiotic stress
Int. J. Mol. Sci.
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3999
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Arabidopsis thaliana (Q6NPM8)
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Wang, J.
Crystallographic identification of spontaneous oxidation intermediates and products of protein sulfhydryl groups
Protein Sci.
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472-477
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Medicago truncatula (A0A072V306)
brenda
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