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Information on EC 3.1.3.1 - alkaline phosphatase and Organism(s) Bos taurus and UniProt Accession P09487

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.1 alkaline phosphatase
IUBMB Comments
Wide specificity. Also catalyses transphosphorylations. The human placental enzyme is a zinc protein. Some enzymes hydrolyse diphosphate (cf. EC 3.6.1.1 inorganic diphosphatase)
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This record set is specific for:
Bos taurus
UNIPROT: P09487
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Word Map
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
Synonyms
ap, alkaline phosphatase, bone alkaline phosphatase, placental alkaline phosphatase, alpase, apase, intestinal alkaline phosphatase, tnsalp, phosphomonoesterase, secreted alkaline phosphatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tissue-non-specific alkaline phosphatase
-
tissue-nonspecific alkaline phosphatase
-
alkaline phenyl phosphatase
-
-
-
-
alkaline phosphatase
alkaline phosphatase VI-1
-
-
alkaline phosphohydrolase
-
-
-
-
alkaline phosphomonoesterase
-
-
-
-
AP-TNAP
-
-
-
-
APase
APASED
-
-
-
-
BC6
-
-
-
-
BIALP
-
-
BIAP
-
-
calf intestinal alkaline phosphatase
-
-
CAP
-
-
CIAP
-
-
EAP
-
-
-
-
Germ-cell alkaline phosphatase
-
-
-
-
glycerophosphatase
-
-
-
-
H-AP
-
-
-
-
High molecular weight phosphatase
-
-
-
-
intestinal alkaline phosphatase
L-AP
-
-
-
-
Liver/bone/kidney isozyme
-
-
-
-
Low molecular weight phosphatase
-
-
-
-
M-ALP
-
-
-
-
Nagao isozyme
-
-
-
-
non-specific alkaline phosphatase
-
-
-
-
phosphatase, alkaline
-
-
-
-
phosphomonoesterase
-
-
-
-
PLAP-like
-
-
-
-
RAN1
-
-
-
-
Regan isozyme
-
-
-
-
TNAP
-
-
TNSALP
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
phosphate-monoester phosphohydrolase (alkaline optimum)
Wide specificity. Also catalyses transphosphorylations. The human placental enzyme is a zinc protein. Some enzymes hydrolyse diphosphate (cf. EC 3.6.1.1 inorganic diphosphatase)
CAS REGISTRY NUMBER
COMMENTARY hide
9001-78-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
ATP + H2O
?
show the reaction diagram
-
-
-
-
?
dentine phosphoprotein + H2O
?
show the reaction diagram
-
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
-
?
disodium 3-(4-meth- oxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]- decan]-4-yl)phenyl phosphate + H2O
?
show the reaction diagram
-
-
-
?
glycogen synthase + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
phospho-Ser histone + H2O
?
show the reaction diagram
-
-
-
-
?
phospho-Ser-casein + H2O
?
show the reaction diagram
-
-
-
-
?
phospho-Tyr angiotensin + H2O
angiotensin + phosphate
show the reaction diagram
-
-
-
-
?
phospho-Tyr-casein + H2O
?
show the reaction diagram
-
-
-
-
?
phospho-Tyr-histone + H2O
?
show the reaction diagram
-
-
-
-
?
phosphorylated acetyl-CoA carboxylase + H2O
acetyl-CoA carboxylase + phosphate
show the reaction diagram
-
-
-
-
?
phosvitin + H2O
?
show the reaction diagram
-
-
-
-
?
spermidine N'-acetyltransferase + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
TNAP is an essential component of serum calcification activity and that its role in the shotgun mechanism is to activate the serum nucleator of apatite crystal formation
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activates
sulfate
-
the rate of irreversible thermal inactivation is strongly reduced by addition of kosmotropic anions like sulfate (half-life increases from 8 to 580 min at 60 °C)
Zn2+
-
calf enzyme contains 0.2% Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(E)-N'-(1-(3-(4-fluorophenyl)-5-phenyl-4,5-dihydro-1H-pyrazol-1-yl)ethylidene)isonicotinohydrazide
-
(E)-N'-(4'-chlorobenzylidene)isonicotinohydrazide
-
(E)-N'-(4-hydroxy-3-methoxybenzylidene)isonicotinohydrazide
most potent inhibitor for tissue-non-specific alkaline phosphatase
1-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]-4-ethylpiperazine
-
1-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]-4-methylpiperazine
-
1-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]azepane
-
2-(4-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]piperazin-1-yl)ethanol
-
3-(2,4-dichloro-5-fluorophenyl)-N,N-bis(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichloro-5-fluorophenyl)-N,N-dimethyl-1H-pyrazole-5-carboxamide
-
3-(2,4-dichloro-5-fluorophenyl)-N-(1-methylethyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichloro-5-fluorophenyl)-N-(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichloro-5-fluorophenyl)-N-(3-hydroxypropyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichlorophenyl)-1H-pyrazole-5-carbohydrazide
-
3-(2,4-dichlorophenyl)-N,N-bis(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichlorophenyl)-N,N-diethyl-1H-pyrazole-5-carboxamide
-
3-(2,4-dichlorophenyl)-N,N-dimethyl-1H-pyrazole-5-carboxamide
-
3-(2,4-dichlorophenyl)-N-(1-methylethyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichlorophenyl)-N-(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichlorophenyl)-N-(2-methoxyethyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichlorophenyl)-N-(2-methylpropyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichlorophenyl)-N-(3-hydroxypropyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichlorophenyl)-N-(3-methylbutyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-dichlorophenyl)-N-(4-hydroxybutyl)-1H-pyrazole-5-carboxamide
-
3-(2,4-difluorophenyl)-N-(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
-
4-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]morpholine
-
L-phenylalanine
-
N'-[(Z)-(2-hydroxyphenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(Z)-(3-nitrophenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(Z)-(4-bromophenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(Z)-(4-fluorophenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(Z)-(4-methoxyphenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(Z)-(pyridin-3-yl)methylidene]pyridine-4-carbohydrazide
-
N'-[(Z)-(pyridin-4-yl)methylidene]pyridine-4-carbohydrazide
-
N-(2-hydroxyethyl)-3-(2,3,4-trichlorophenyl)-1H-pyrazole-5-carboxamide
-
N-(2-hydroxyethyl)-3-(2,4,5-trifluorophenyl)-1H-pyrazole-5-carboxamide
-
N-tert-butyl-3-(2,4-dichlorophenyl)-1H-pyrazole-5-carboxamide
-
(2Z)-2-(benzoylamino)-3-[2-[4-(trifluoromethyl)phenyl]-1-benzothiophen-3-yl]prop-2-enoate
-
with 0.1 mM 35% remaining activity
(4-methoxyphenyl)[2-(4-methoxyphenyl)-1-benzothiophen-3-yl]methanone
-
with 0.1 mM 70% remaining activity
(E)-N'-(1-(3-(4-fluorophenyl)-5-phenyl-4,5-dihydro-1H-pyrazol-1-yl)ethylidene)isonicotinohydrazide
-
(E)-N'-(4'-chlorobenzylidene)isonicotinohydrazide
most potent inhibitor for intestinal alkaline phosphatase
(E)-N'-(4-hydroxy-3-methoxybenzylidene)isonicotinohydrazide
-
1,10-phenanthroline
-
1 mM, irreversibly inactivates the enzyme
1-benzothiophen-3-yl(4-methoxyphenyl)methanone
-
with 0.1 mM 40% remaining activity
1-benzothiophen-3-yl(phenyl)methanone
-
with 0.1 mM 43% remaining activity
1-bromotetramisole
-
-
2,4-dichloro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
-
-
2-(2-chlorophenyl)-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 63% remaining activity
2-(2-methylphenyl)-1-benzothiophene-3-carbonitrile
-
with 0.1 mM 5% remaining activity
2-(3-chlorophenyl)-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 62% remaining activity
2-(3-methoxy-1-benzothiophen-2-yl)benzonitrile
-
with 0.1 mM 57% remaining activity
2-(4-chlorophenyl)-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 9% remaining activity
2-(4-chlorophenyl)-1-benzothiophene-3-carbonitrile
-
with 0.1 mM 69% remaining activity
2-(4-methoxyphenyl)-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 37% remaining activity
2-(naphthalen-2-yl)-1-benzothiophene-3-carbonitrile
-
with 0.1 mM 18% remaining activity
2-chloro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
-
-
2-iodo-1-benzothiophene
-
with 0.1 mM 41% remaining activity
2-phenyl-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 41% remaining activity
2-phenyl-1-benzothiophene-3-carbonitrile
-
with 0.1 mM 76% remaining activity
2-phenyl-3-oxime-benzo[b]thiophene
-
with 0.1 mM 1% remaining activity
2-[3-(2,2,2-trifluoroethyl)-1-benzothiophen-2-yl]benzonitrile
-
with 0.1 mM 70% remaining activity
2-[3-(4-fluorophenoxy)-1-benzothiophen-2-yl]benzonitrile
-
with 0.1 mM 66% remaining activity
2-[4-(1-benzothiophen-3-yl)piperazin-1-yl]phenol
-
with 0.1 mM 49% remaining activity
2-[4-(trifluoromethyl)phenyl]-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 30% remaining activity
3,5-dinitro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
-
-
3-(3-methoxy-1-benzothiophen-2-yl)quinoline
-
with 0.1 mM 64% remaining activity
3-methoxy-2-(2-methylphenyl)-1-benzothiophene
-
with 0.1 mM 73% remaining activity
3-methoxy-2-(4-methoxyphenyl)-1-benzothiophene
-
with 0.1 mM 78% remaining activity
4-(1-benzothiophen-3-yloxy)benzaldehyde
-
with 0.1 mM 9% remaining activity
4-chloro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
-
-
4-fluoro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
-
-
4-methoxy-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
-
-
arsenate
-
irreversible inhibitor
ascorbic acid
-
-
bis(1,1,1-trifluoroacetylacetonato)oxovanadium(IV)
-
-
bis(3-chloroacetylacetonato)oxovanadium(IV)
-
-
bis(3-chloroacetylacetonato)oxovanadium(IV)(4-Mepy)
-
-
bis(3-methylacetylacetonato)oxovanadium(IV)
-
-
bis(acetylacetonato)oxovanadium(IV)
-
-
bis(acetylacetonato)oxovanadium(IV)(4-Mepy)
-
-
bis(benzoylacetonato)oxovanadium(IV)
-
-
butanol
-
reversible noncompetitive
CO2
-
enzyme in buffer can be inactivated by COS treatment at atmospheric pressure, increasing inactivation, when temperature increases from 20°C to 50°C, 16% loss of activity after 30 min at 20°C, 81% loss of activity after 30 min at 50°C. Change in activity dependent on CO2 treatment is not observed in raw milk mainly due to strong buffering capacity of milk
ethanol
-
reversible noncompetitive
ethylene glycol
-
reversible noncompetitive
glutathione
-
strong
KCl
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
KH2PO4
-
-
KNO3
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
KPF6
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
L-phenylalanine
-
levamisole
methyl (2E)-2-(benzoylamino)-3-[2-(4-methoxyphenyl)-1-benzothiophen-3-yl]prop-2-enoate
-
with 0.1 mM 77% remaining activity
methyl N-benzoyl-3-[2-[4-(trifluoromethyl)phenyl]-1-benzothiophen-3-yl]alaninate
-
with 0.1 mM 63% remaining activity
N'-[(Z)-(2-hydroxyphenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(Z)-(3-nitrophenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(Z)-(4-bromophenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(Z)-(4-fluorophenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(Z)-(4-methoxyphenyl)methylidene]pyridine-4-carbohydrazide
-
N'-[(Z)-(pyridin-3-yl)methylidene]pyridine-4-carbohydrazide
-
N'-[(Z)-(pyridin-4-yl)methylidene]pyridine-4-carbohydrazide
-
N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)acetamide
-
-
N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)butyramide
-
-
N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)heptanamide
-
-
N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)octanamide
-
-
Na2SO4
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
Na3VO4
-
-
NaBF4
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
NaCl
-
reduces enzymatic activity and significantly decreased Vmax/Km ratio
NaNO3
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
phosphate
-
competitive inhibitor
Propanol
-
reversible noncompetitive
Sodium acetate
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
Sodium citrate
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
theophylline
VOSO4
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diethanolamine
-
highly activates BIALP. Km values increase with increasing concentrations of diethanolamine and N-methylethanolamine, but not triethanolamine
N-Methylethanolamine
-
highly activates BIALP. Km values increase with increasing concentrations of diethanolamine and N-methylethanolamine, but not triethanolamine
triethanolamine
-
highly activates BIALP. Km values increase with increasing concentrations of diethanolamine and N-methylethanolamine, but not triethanolamine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.037 - 0.1159
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
0.00000035 - 7.32
4-nitrophenyl phosphate
0.1
ATP
-
-
0.62
p-nitrophenyl phosphate
-
-
additional information
4-nitrophenyl phosphate
-
the Km values increase with increasing concentrations of diethanolamine and N-methylethanolamine, but not triethanolamine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.037 - 2250
4-nitrophenyl phosphate
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000261 - 0.0089
arsenate
0.00007
bis(1,1,1-trifluoroacetylacetonato)oxovanadium(IV)
-
pH 8, 37°C
0.00015
bis(3-chloroacetylacetonato)oxovanadium(IV)
-
pH 8, 37°C
0.00104
bis(3-chloroacetylacetonato)oxovanadium(IV)(4-Mepy)
-
pH 8, 37°C
0.00034
bis(3-methylacetylacetonato)oxovanadium(IV)
-
pH 8, 37°C
0.00043
bis(acetylacetonato)oxovanadium(IV)
-
pH 8, 37°C
0.00069
bis(acetylacetonato)oxovanadium(IV)(4-Mepy)
-
pH 8, 37°C
0.0004
bis(benzoylacetonato)oxovanadium(IV)
-
pH 8, 37°C
0.00049
Na3VO4
-
pH 8, 37°C
0.00241 - 0.00311
phosphate
0.05 - 0.096
theophylline
0.00055
VOSO4
-
pH 8, 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00106
(E)-N'-(1-(3-(4-fluorophenyl)-5-phenyl-4,5-dihydro-1H-pyrazol-1-yl)ethylidene)isonicotinohydrazide
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.00035
(E)-N'-(4-hydroxy-3-methoxybenzylidene)isonicotinohydrazide
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.000488
1-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]-4-ethylpiperazine
Bos taurus
-
0.000828
1-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]-4-methylpiperazine
Bos taurus
-
0.00145
1-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]azepane
Bos taurus
-
0.000375
2-(4-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]piperazin-1-yl)ethanol
Bos taurus
-
0.000127
3-(2,4-dichloro-5-fluorophenyl)-N,N-bis(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000324
3-(2,4-dichloro-5-fluorophenyl)-N,N-dimethyl-1H-pyrazole-5-carboxamide
Bos taurus
-
0.00485
3-(2,4-dichloro-5-fluorophenyl)-N-(1-methylethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.0001
3-(2,4-dichloro-5-fluorophenyl)-N-(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000056
3-(2,4-dichloro-5-fluorophenyl)-N-(3-hydroxypropyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000044
3-(2,4-dichlorophenyl)-1H-pyrazole-5-carbohydrazide
Bos taurus
-
0.000047
3-(2,4-dichlorophenyl)-N,N-bis(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000285
3-(2,4-dichlorophenyl)-N,N-diethyl-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000119
3-(2,4-dichlorophenyl)-N,N-dimethyl-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000051
3-(2,4-dichlorophenyl)-N-(1-methylethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000044
3-(2,4-dichlorophenyl)-N-(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000046
3-(2,4-dichlorophenyl)-N-(2-methoxyethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000082
3-(2,4-dichlorophenyl)-N-(2-methylpropyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000031
3-(2,4-dichlorophenyl)-N-(3-hydroxypropyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000459
3-(2,4-dichlorophenyl)-N-(3-methylbutyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000035
3-(2,4-dichlorophenyl)-N-(4-hydroxybutyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000035
3-(2,4-difluorophenyl)-N-(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000574
4-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]morpholine
Bos taurus
-
0.0192
levamisole
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.00182
N'-[(Z)-(3-nitrophenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.00413
N'-[(Z)-(4-bromophenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.00226
N'-[(Z)-(4-fluorophenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.00056
N'-[(Z)-(4-methoxyphenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.00243
N'-[(Z)-(pyridin-3-yl)methylidene]pyridine-4-carbohydrazide
Bos taurus
tissue-non-specific alkaline phosphatase, pH and temperature not specified in the publication
0.000005
N-(2-hydroxyethyl)-3-(2,3,4-trichlorophenyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000134
N-(2-hydroxyethyl)-3-(2,4,5-trifluorophenyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.000398
N-tert-butyl-3-(2,4-dichlorophenyl)-1H-pyrazole-5-carboxamide
Bos taurus
-
0.00398
(E)-N'-(1-(3-(4-fluorophenyl)-5-phenyl-4,5-dihydro-1H-pyrazol-1-yl)ethylidene)isonicotinohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00067
(E)-N'-(4'-chlorobenzylidene)isonicotinohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00192
(E)-N'-(4-hydroxy-3-methoxybenzylidene)isonicotinohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.000344
2,4-dichloro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
Bos taurus
-
at pH 9.5 and 37°C
0.003458
2-chloro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
Bos taurus
-
at pH 9.5 and 37°C
0.000896
3,5-dinitro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
Bos taurus
-
at pH 9.5 and 37°C
0.000251
4-chloro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
Bos taurus
-
at pH 9.5 and 37°C
0.001547
4-fluoro-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
Bos taurus
-
at pH 9.5 and 37°C
0.003291
4-methoxy-N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)benzamide
Bos taurus
-
at pH 9.5 and 37°C
0.004137
KH2PO4
Bos taurus
-
at pH 9.5 and 37°C
0.08
L-phenylalanine
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00144
N'-[(Z)-(2-hydroxyphenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00734
N'-[(Z)-(3-nitrophenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00972
N'-[(Z)-(4-bromophenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.0175
N'-[(Z)-(4-fluorophenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00174
N'-[(Z)-(4-methoxyphenyl)methylidene]pyridine-4-carbohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00146
N'-[(Z)-(pyridin-3-yl)methylidene]pyridine-4-carbohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.00246
N'-[(Z)-(pyridin-4-yl)methylidene]pyridine-4-carbohydrazide
Bos taurus
intestinal alkaline phosphatase, pH and temperature not specified in the publication
0.004256
N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)acetamide
Bos taurus
-
at pH 9.5 and 37°C
0.001636
N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)butyramide
Bos taurus
-
at pH 9.5 and 37°C
0.000492
N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)heptanamide
Bos taurus
-
at pH 9.5 and 37°C
0.001704
N-((4-(N-(pyrimidin-2-yl)sulfamoyl)phenyl)carbamothioyl)octanamide
Bos taurus
-
at pH 9.5 and 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.4
-
assay at
11
-
Tris-HCl buffer
8.5
-
five buffer systems are investigated at pH 8.5: tris, carbonate, hepes, borate, and glycine buffers, and the lowest catalytic activity of alkaline phosphatases at equal pH is observed in the borate buffer. The highest specific activity, is observed in the buffer solution of tris-(oxymethyl)-aminomethane-HCl
9.8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
assay at
25
assay at
37
-
assay at
45
-
at pH 11
56
-
native enzyme and enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
58
-
enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8
-
calculated from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
temperature-dependent localization of the glycosylphosphatidylinositol-anchored bovine intestinal alkaline phophatase into model raft made of palmitoyloleoylphosphatidylcholine/sphingomyelin/cholesterol supported membranes. Atomic force microscopy shows that the inserted BIAP is localized in the sphingomyelin/cholesterol enriched ordered domains at low temperature. Above 30°C, BIAP redistributes and is present in both the ‘fluid’ palmitoyloleoylphosphatidylcholine enriched and the ordered sphingomyelin/cholesterol domains
-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PPBT_BOVIN
524
0
57193
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
81000
-
x * 81000, SDS-PAGE
additional information
-
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
activity of the dimer is three or four times higher than that of the tetramer
tetramer
-
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
aqueous suspendible polymer nanostructures are prepared by simple microtome processing of electrospun nylon 6 nanofibers and are used to immobilize calf intestinal ALP by either covalent or noncovalent bioconjugation chemistries. Noncovalent immobilization of ALP to the mechanically cut nanofibers using a multi-stacked, layer-by-layer approach with the cationic polymer Sapphire II results in the highest enzyme loading. In terms of the overall catalytic performance of the various immobilized ALP systems, a single-stacked layer-by-layer assembly approach resulted in the highest level of enzymatic activity (30.1%) per unit mass of nanofiber support
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 70
-
the half-lives for the enzyme incubated in saltfree buffer at 50°C, 60°C, and 70°C is determined to be 5.3 h, 7.9 min, and 1.7 min. All the salts tested show the ability to stabilize the enzyme when incubated at 70°C
53
-
t1/2: 15 min, native enzyme
59
-
t1/2: 6 min, native enzyme
69
-
t1/2: 6 min, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
70
-
complete inactivation after 20 min in glycine buffer, complete inactivation after 40 min in pasteurized milk
73
-
t1/2: 4 min, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
80
-
complete inactivation after 4 min in glycine buffer, complete inactivation after 10 min in pasteurized milk
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity of alkaline phosphatase is not affected after 6 min of pressure treatments (206-620 MPa), regardless of the medium in which the enzyme is prepared. Increasing the processing time to 12 min significantly reduces the activity of alkaline phosphatase at 620 MPa. Circular dichroism data demonstrated a partial change in the secondary structure of ALP at 620 MPa leading to a random coil structure
-
carbohydrate additives such as sucrose may result in a remarkable higher reduction in the kinetics of deteriorative reactions and result in a better stability
-
improved activity and stability of alkaline phosphatases from psychrophilic and mesophilic organisms by chemically modifying aliphatic or amino groups using tetracarboxy-benzophenone derivatives
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
commercial product
-
liver/kidney/bone-isoenzyme
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
refolding behavior of guanidine hydrochloride-denatured alkaline phosphatase, despite the enhanced activity recovery yield (more than 50%), both the refolding and the reactivation rate constants decrease with increasing alpha-cyclodextrin concentrations. Detergents (used in the artificial chaperone method) increase the refolding rate significantly
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
enzyme is capable of precipitating Cu2+ from 50 ppm CuCl2 solution with 64.3% precipitation. Phosphate generated from enzyme-mediated hydrolysis of 4-nitrophenyl phosphate binds with the copper ions
biotechnology
food industry
-
quantification of alkaline phosphatase by using a monoclonal antibody-based immunoassay immunoassay is appropriate for determining mild time/temperature treatment of milk and for the control of milk pasteurization
medicine
-
TNAP is an essential component of serum calcification activity and that its role in the shotgun mechanism is to activate the serum nucleator of apatite crystal formation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Stinson, R.A.; Chan, J.R.A.
Alkaline phosphatase and its function as a protein phosphatase
Adv. Protein Phosphatases
4
127-151
1987
Bos taurus, Escherichia coli, Homo sapiens, Sus scrofa
-
Manually annotated by BRENDA team
Coleman, J.E.; Gettins, P.
Alkaline phosphatase, solution structure, and mechanism
Adv. Enzymol. Relat. Areas Mol. Biol.
55
381-452
1983
Bacillus subtilis, Bacillus licheniformis, Bos taurus, Escherichia coli, Homo sapiens, Micrococcus sodonensis, Rattus norvegicus
Manually annotated by BRENDA team
Fernley, H.N.
Mammalian alkaline phosphatases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
4
417-447
1971
Bos taurus, Equus caballus, Homo sapiens
-
Manually annotated by BRENDA team
Stadtman, T.C.
Alkaline phosphatases
The Enzymes, 2nd Ed. (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
5
55-71
1961
Bos taurus, Escherichia coli, Sus scrofa
-
Manually annotated by BRENDA team
Besman, M.; Coleman, J.E.
Isozymes of bovine intestinal alkaline phosphatase
J. Biol. Chem.
260
11190-11193
1985
Bos taurus
Manually annotated by BRENDA team
Hsu, H.H.T.; Munoz, P.A.; Barr, J.; Oppliger, I.; Morris, D.C.; Vaananen, H.K.; Tarkenton, N.; Anderson, H.C.
Purification and partial characterization of alkaline phosphatase of matrix vesicles from fetal bovine epiphyseal cartilage. Purification by monoclonal antibody affinity chromatography
J. Biol. Chem.
260
1826-1831
1985
Bos taurus
Manually annotated by BRENDA team
Goldstein, D.J.; Harris, H.
Human placental alkaline phosphatase differs from that of other species
Nature
280
602-605
1979
Bos taurus, Canis lupus familiaris, Cavia porcellus, Felis catus, Ovis aries, Homo sapiens, Macaca mulatta, Mesocricetus auratus, Mus musculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
McCarthy, A.D.; Cortizo, A.M.; Gimenez-Segura, G.; Bruzzone, L.; Etcheverry, S.B.
Non-enzymatic glycosylation of alkaline phosphatase alters its biological properties
Mol. Cell. Biochem.
181
63-69
1998
Bos taurus
Manually annotated by BRENDA team
Stagni, N.; Vittur, F.; de Bernard, B.
Solubility properties of alkaline phosphatase from matrix vesicles
Biochim. Biophys. Acta
761
246-251
1983
Bos taurus
Manually annotated by BRENDA team
Yazdanparast, R.; Khodagholi, F.
Kinetic aspects of alkaline phosphatase refolding in the presence of alpha-cyclodextrin
Arch. Biochem. Biophys.
446
11-19
2006
Bos taurus
Manually annotated by BRENDA team
Zhang, L.; Buchet, R.; Azzar, G.
Phosphate binding in the active site of alkaline phosphatase and the interactions of 2-nitrosoacetophenone with alkaline phosphatase-induced small structural changes
Biophys. J.
86
3873-3881
2004
Bos taurus
Manually annotated by BRENDA team
Terefe, N.S.; Arimi, J.M.; Van Loey, A.; Hendrickx, M.
Kinetics of the alkaline phosphatase catalyzed hydrolysis of disodium p-nitrophenyl phosphate: effects of carbohydrate additives, low temperature, and freezing
Biotechnol. Prog.
20
1467-1478
2004
Bos taurus
Manually annotated by BRENDA team
Siddiqui, K.S.; Poljak, A.; Cavicchioli, R.
Improved activity and stability of alkaline phosphatases from psychrophilic and mesophilic organisms by chemically modifying aliphatic or amino groups using tetracarboxy-benzophenone derivatives
Cell. Mol. Biol.
50
657-667
2004
Bos taurus, Pandalus borealis
Manually annotated by BRENDA team
Fadiloglu, S.; Erkmen, O.; Sekeroglu, G.
Thermal and carbon dioxide inactivation of alkaline phosphatase in buffer and milk
Food Technol. Biotechnol.
42
27-32
2004
Bos taurus
-
Manually annotated by BRENDA team
Sariri, R.; Ghanadzadesh, A.; Liali, E.; Sajedi, R.H.
The inhibitory effect of alcohols on alkaline phosphatase activity
Int. J. Chem. Sci.
3
16-22
2005
Bos taurus
-
Manually annotated by BRENDA team
Kouassi, G.K.; Anantheswaran, R.C.; Knabel, S.J.; Floros, J.D.
Effect of high-pressure processing on activity and structure of alkaline phosphatase and lactate dehydrogenase in buffer and milk
J. Agric. Food Chem.
55
9520-9529
2007
Bos taurus
Manually annotated by BRENDA team
Levieux, D.; Geneix, N.; Levieux, A.
Inactivation-denaturation kinetics of bovine milk alkaline phosphatase during mild heating as determined by using a monoclonal antibody-based immunoassay
J. Dairy Res.
74
296-301
2007
Bos taurus
Manually annotated by BRENDA team
Giocondi, M.C.; Besson, F.; Dosset, P.; Milhiet, P.E.; Le Grimellec, C.
Temperature-dependent localization of GPI-anchored intestinal alkaline phosphatase in model rafts
J. Mol. Recognit.
20
531-537
2007
Bos taurus
Manually annotated by BRENDA team
Sidique, S.; Ardecky, R.; Su, Y.; Narisawa, S.; Brown, B.; Millan, J.L.; Sergienko, E.; Cosford, N.D.
Design and synthesis of pyrazole derivatives as potent and selective inhibitors of tissue-nonspecific alkaline phosphatase (TNAP)
Bioorg. Med. Chem. Lett.
19
222-225
2009
Bos taurus (P09487)
Manually annotated by BRENDA team
Price, P.A.; Toroian, D.; Chan, W.S.
Tissue-nonspecific Alkaline Phosphatase Is Required for the Calcification of Collagen in Serum: A possible mechanism for biomineralization
J. Biol. Chem.
284
4594-4604
2009
Bos taurus
Manually annotated by BRENDA team
Schrenkhammer, P.; Rosnizeck, I.C.; Duerkop, A.; Wolfbeis, O.S.; Schaeferling, M.
Time-resolved fluorescence-based assay for the determination of alkaline phosphatase activity and application to the screening of its inhibitors
J. Biomol. Screen.
13
9-16
2008
Bos taurus (P19111)
Manually annotated by BRENDA team
Ziegler, A.J.; Florian, J.; Ballicora, M.A.; Herlinger, A.W.
Alkaline phosphatase inhibition by vanadyl-beta-diketone complexes: electron density effects
J. Enzyme Inhib. Med. Chem.
24
22-28
2009
Bos taurus
Manually annotated by BRENDA team
Mark, S.S.; Stolper, S.I.; Baratti, C.; Park, J.Y.; Taku, M.A.; Santiago-Aviles, J.J.; Kricka, L.J.
Bioconjugation of alkaline phosphatase to mechanically processed, aqueous suspendible electrospun polymer nanofibers for use in chemiluminescent detection assays
Macromol. Biosci.
8
484-498
2008
Bos taurus (P19111)
Manually annotated by BRENDA team
Atyaksheva, L.F.; Chukhrai, E.S.; Poltorak, O.M.
The catalytic properties of alkaline phosphatases under various conditions
Russ. J. Phys. Chem. A
82
1947-1951
2008
Bos taurus, Escherichia coli, Gallus gallus (Q92058)
-
Manually annotated by BRENDA team
Li, L.; Chang, L.; Pellet-Rostaing, S.; Liger, F.; Lemaire, M.; Buchet, R.; Wu, Y.
Synthesis and evaluation of benzo[b]thiophene derivatives as inhibitors of alkaline phosphatases
Bioorg. Med. Chem.
17
7290-7300
2009
Bos taurus, Sus scrofa
Manually annotated by BRENDA team
Iqbal, J.
An enzyme immobilized microassay in capillary electrophoresis for characterization and inhibition studies of alkaline phosphatases
Anal. Biochem.
414
226-231
2011
Bos taurus
Manually annotated by BRENDA team
Yang, Z.; Liu, X.; Chen, C.; Halling, P.
Hofmeister effects on activity and stability of alkaline phosphatase
Biochim. Biophys. Acta
1804
821-828
2010
Bos taurus
Manually annotated by BRENDA team
Sekiguchi, S.; Hashida, Y.; Yasukawa, K.; Inouye, K.
Effects of amines and aminoalcohols on bovine intestine alkaline phosphatase activity
Enzyme Microb. Technol.
49
171-176
2011
Bos taurus
Manually annotated by BRENDA team
Chaudhuri, G.; Chatterjee, S.; Venu-Babu, P.; Ramasamy, K.; Thilagaraj, W.R.
Kinetic behaviour of calf intestinal alkaline phosphatase with pNPP
Indian J. Biochem. Biophys.
50
64-71
2013
Bos taurus
Manually annotated by BRENDA team
Sajid-Ur-Rehman, X.; Saeed, A.; Saddique, G.; Ali Channar, P.; Ali Larik, F.; Abbas, Q.; Hassan, M.; Raza, H.; Fattah, T.A.; Seo, S.Y.
Synthesis of sulfadiazinyl acyl/aryl thiourea derivatives as calf intestinal alkaline phosphatase inhibitors, pharmacokinetic properties, lead optimization, Lineweaver-Burk plot evaluation and binding analysis
Bioorg. Med. Chem.
26
3707-3715
2018
Bos taurus
Manually annotated by BRENDA team
Channar, P.A.; Shah, S.J.; Hassan, S.; Nisa, Z.U.; Lecka, J.; Sevigny, J.; Bajorath, J.; Saeed, A.; Iqbal, J.
Isonicotinohydrazones as inhibitors of alkaline phosphatase and ecto-5-nucleotidase
Chem. Biol. Drug Des.
89
365-370
2017
Bos taurus (P09487), Bos taurus (P19111), Bos taurus
Manually annotated by BRENDA team
Zhang, Q.; Zhang, C.; Yang, M.; Yu, D.; Yu, C.
Pyrophosphate as substrate for alkaline phosphatase activity A convenient flow-injection chemiluminescence assay
Luminescence
32
1150-1156
2017
Bos taurus
Manually annotated by BRENDA team