Information on EC 3.1.3.15 - histidinol-phosphatase

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

EC NUMBER
COMMENTARY hide
3.1.3.15
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RECOMMENDED NAME
GeneOntology No.
histidinol-phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
carbon disulfide + 2 H2O = CO2 + 2 hydrogen sulfide
show the reaction diagram
L-histidinol phosphate + H2O = L-histidinol + phosphate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-histidine biosynthesis
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histidine metabolism
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Histidine metabolism
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Metabolic pathways
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
L-histidinol-phosphate phosphohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9025-79-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
no activity in Acidithiobacillus albertensis strain DSM 14366
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-
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Manually annotated by BRENDA team
no activity in Acidithiobacillus ferrooxidans strain DSM 14882
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-
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Manually annotated by BRENDA team
no activity in Acidithiobacillus thiooxidans strains DSM504 and DSM14887
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-
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Manually annotated by BRENDA team
strain L120 containing pSS503 or pSH 368 compared with strain L120
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Manually annotated by BRENDA team
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
deletion of the histidinol-phosphate phosphatase gene hisN results in histidine auxotrophy
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
AMP + H2O
?
show the reaction diagram
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-
-
-
?
carbon disulfide + 2 H2O
CO2 + 2 hydrogen sulfide
show the reaction diagram
carbonyl sulfide + H2O
CO2 + H2S
show the reaction diagram
carbonyl sulfide + H2O
CO2 + hydrogen sulfide
show the reaction diagram
D-fructose 6-phosphate + H2O
?
show the reaction diagram
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-
-
?
L-histidinol phosphate + H2O
?
show the reaction diagram
L-histidinol phosphate + H2O
L-histidinol + phosphate
show the reaction diagram
L-phosphoserine + H2O
L-serine + phosphate
show the reaction diagram
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-
-
-
?
N-formyl-L-histidinol phosphate + H2O
N-formyl-L-histidinol + 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
carbon disulfide + 2 H2O
CO2 + 2 hydrogen sulfide
show the reaction diagram
carbonyl sulfide + H2O
CO2 + H2S
show the reaction diagram
L-histidinol phosphate + H2O
?
show the reaction diagram
L-histidinol phosphate + H2O
L-histidinol + phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
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strong activity in the presence of Cu2+
Iron
contains iron in the active site
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
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inhibits more rapidly at pH 7 than at pH 8.5
8-hydroxyquinoline
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arsenate
EDTA
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0.1 mM, no activity
ethylenimine
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iodoacetamide
iodoacetate
N-ethylmaleimide
p-chloromercuribenzoate
additional information
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inability of the small KCN and CF3SO2NH2 to inhibit CS2 hydrolase
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.59
AMP
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in the presence of 1 mM Co2+, at 80C and pH 6.5
0.046 - 0.193
carbon disulfide
0.014 - 0.074
carbonyl sulfide
2.37
D-fructose 6-phosphate
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in the presence of 1 mM Co2+, at 80C and pH 6.5
0.03 - 5.4
L-Histidinol phosphate
1.45
L-phosphoserine
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in the presence of 1 mM Co2+, at 80C and pH 6.5
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
29
AMP
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in the presence of 1 mM Co2+, at 80C and pH 6.5
48 - 952
carbon disulfide
1800
carbonyl sulfide
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pH and temperature not specified in the publication
11
D-fructose 6-phosphate
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in the presence of 1 mM Co2+, at 80C and pH 6.5
0.031 - 2140
L-Histidinol phosphate
14
L-phosphoserine
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in the presence of 1 mM Co2+, at 80C and pH 6.5
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.22 - 150
L-Histidinol phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0252
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strain L120
0.0498
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strain L120 (pSH368)
0.0503
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strain L120 (pSS503)
0.225
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strain 74A, grown in 0.5 mM tryptophan
0.241
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strain 74A, grown in 0.1 mM tryptophan
0.25
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strain 74A, grown in absence of tryptophan
0.273
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strain trp-1-13A, grown in 0.5 mM tryptophan
0.333
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strain trp-4-9A, grown in 0.5 mM tryptophan
0.541
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strain trp-1-13A, grown in 0.1 mM tryptophan
0.575
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strain trp-4-9A, grown in 0.1 mM tryptophan
2.586
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at pH 8.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at; assay at; assay at
50
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Lactococcus lactis subsp. lactis (strain IL1403)
Lactococcus lactis subsp. lactis (strain IL1403)
Lactococcus lactis subsp. lactis (strain IL1403)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19903
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2 * 19903, in the presence of Mg2+ and histidinol phosphate, ESI mass spectrometry
24000
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x * 24000, in the CS2 hydrolase two octameric rings form a hexadecamer by interlocking at right angles to each other, forming a catenane structure, MALDI-TOF MS
29500
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4 * 29500, dynamic light scattering
38000
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preparative PAGE
39000
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gel filtration
92000
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gel filtration
118000
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dynamic light scattering
119900
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calculated from sequence of cDNA
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 19903, in the presence of Mg2+ and histidinol phosphate, ESI mass spectrometry
hexadecamer
homotetramer
monomer
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1 * 39000, gel filtration
octamer
additional information
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the enzyme exists in solution as a mixture of unique hexadecameric catenane and octameric ring forms, multi-angle laser light scattering and native mass spectrometric analyses, overview. Four of the sixteen active sites of the catenane can be partially blocked due to the packed perpendicular arrangement of the two interlocked rings
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour diffusion method, crystal structures are determined from heterologously expressed selenomethionine-labelled protein at 2.6 A resolution and native purified protein at 2.4 A resolution
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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
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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
microbatch crystallization method
two crystal forms by the handing-drop vapour-diffusion technique
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vapour diffusion method with 0.68 M sodium malonate and 100 mM Tris-HCl (pH 8.5)
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 80
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stable up to 60C, complete loss of activity at 80C
54
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50% loss of phosphatase activity in 2 min
65
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15 min, stable
80
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complete loss after 10 min
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Ni2+), gel filtration
native enzyme by ammonium sulfate precipitation, followed by hydrophobic interaction chromatography, and anion exchange chromatography; native enzyme by ammonium sulfate precipitation, followed by hydrophobic interaction chromatography, and anion exchange chromatography
Ni-NTA affinity chromatography
Ni-NTA column chromatography
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nickel-nitrilotriacetic acid column chromatography
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TALON metal affinity column chromatography and Superdex 200 10/300 gel filtration
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the recombinant enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis; DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)pLysS cells
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expressed in Escherichia coli strain BL21(DE3)
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expressed in Streptomyces coelicolor M145
expression in Escherichia coli
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His-tagged version expressed in Escherichia coli Rosetta (DE3) pLysS
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F77A
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Km-value for carbon disulfide is 1.5fold fold lower than wild-type value, Vmax is 1.4fold higher than wild-type value
F96S
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Km-value for carbon disulfide is similar to wild-type value, Vmax is 2.4fold higher than wild-type value
G199stop
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Km-value for carbon disulfide is 1.5fold fold lower than wild-type value, Vmax is 1.2fold higher than wild-type value
F77A
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Km-value for carbon disulfide is 1.5fold fold lower than wild-type value, Vmax is 1.4fold higher than wild-type value
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F96S
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Km-value for carbon disulfide is similar to wild-type value, Vmax is 2.4fold higher than wild-type value
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G199stop
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Km-value for carbon disulfide is 1.5fold fold lower than wild-type value, Vmax is 1.2fold higher than wild-type value
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G195R
conserved Gly, required for histinol-phosphate phosphatase activity
D12A
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shows only traces of the wild type activity
E18A
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shows about 5% of the wild-type 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
E115Q
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the mutant shows reduced catalytic efficiency compared to the wild type enzyme
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R197M
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the mutant shows reduced catalytic efficiency compared to the wild type enzyme
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Y117F
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the mutant shows increased catalytic efficiency compared to the wild type enzyme
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Y157F
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the mutant shows reduced catalytic efficiency compared to the wild type enzyme
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from urea solution
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