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Information on EC 3.1.3.1 - alkaline phosphatase and Organism(s) Homo sapiens and UniProt Accession P05186

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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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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P05186
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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 phosphohydrolase
-
-
-
-
alkaline phosphomonoesterase
-
-
-
-
ALPP
-
-
AP-TNAP
-
-
-
-
APase
-
-
-
-
APASED
-
-
-
-
BALP
-
-
BC6
-
-
-
-
bone alkaline phosphatase
-
-
bone specific alkaline phosphatase
-
-
EAP
-
-
-
-
germ cell alkaline phosphatase
-
-
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
-
-
-
-
PALP
-
-
phosphatase, alkaline
-
-
-
-
phosphomonoesterase
-
-
-
-
placental alkaline phosphatase
-
-
PLAP-like
-
-
-
-
RAN1
-
-
-
-
Regan isozyme
-
-
-
-
salivary alkaline phosphatase
-
-
SEAP
-
-
secreted alkaline phosphatase
-
-
strensiq
-
recombinant enzyme, previously known as asfotase-alfa
tissue non-specific alkaline phosphatase
tissue nonspecific alkaline phosphatase
-
-
tissue-nonspecific alkaline phosphatase
-
-
TNSALP
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
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-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
alpha-naphthyl phosphate + H2O
alpha-naphthol + phosphate
show the reaction diagram
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
2-chloro-5-(4-methoxyspiro (1,2-dioxetane-3,2'-(5'-chloro)tricyclo[3.3.1.13,7]decan)-4-yl)phenyl phosphate + H2O
2-chloro-5-(4-methoxyspiro (1,2-dioxetane-3,2'-(5'-chloro)tricyclo[3.3.1.13,7]decan)-4-yl)phenol + phosphate
show the reaction diagram
-
CDP-star
-
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
show the reaction diagram
-
-
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
3-phosphoglycerate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
5'-dTMP + H2O
?
show the reaction diagram
-
-
-
-
?
5'-UMP + H2O
uridine + phosphate
show the reaction diagram
-
-
-
-
?
ADP + H2O
?
show the reaction diagram
-
-
-
-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
?
show the reaction diagram
-
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
glucose 1-phosphate + H2O
glucose + phosphate
show the reaction diagram
-
-
-
-
?
glycogen synthase + H2O
?
show the reaction diagram
-
-
-
-
?
histone + H2O
?
show the reaction diagram
-
32P-labelled
-
-
?
indoxyl phosphate + nitroblue tetrazolium chloride
nitrioblue diformazan + phosphate
show the reaction diagram
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
p-toluidinium 5-bromo-4-chloro-3-indolyl phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
show the reaction diagram
-
-
-
-
?
phospho-DL-Thr + H2O
phosphate + Thr
show the reaction diagram
-
-
-
-
?
phospho-DL-Tyr + H2O
phosphate + Tyr
show the reaction diagram
-
-
-
-
?
phospho-Ser histone + H2O
?
show the reaction diagram
-
-
-
-
?
phospho-Ser-casein + H2O
?
show the reaction diagram
-
-
-
-
?
phosphoethanolamine + H2O
phosphate + ethanolamine
show the reaction diagram
-
-
-
-
?
phosphorylase kinase + H2O
?
show the reaction diagram
-
-
-
-
?
phosphorylated acetyl-CoA carboxylase + H2O
acetyl-CoA carboxylase + phosphate
show the reaction diagram
-
-
-
-
?
phosphoserine + H2O
phosphate + Ser
show the reaction diagram
-
-
-
-
?
phosvitin + H2O
?
show the reaction diagram
-
-
-
-
?
protamine + H2O
?
show the reaction diagram
-
-
-
-
?
pyridoxal 5'-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
show the reaction diagram
-
-
-
?
thiamin diphosphate + H2O
thiamin phosphate + phosphate
show the reaction diagram
-
-
-
-
?
triphosphate + H2O
diphosphate + phosphate
show the reaction diagram
-
-
-
-
?
UDP + H2O
?
show the reaction diagram
-
-
-
-
?
UMP + H2O
uridine + phosphate
show the reaction diagram
-
-
-
-
?
UTP + 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
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
stimulates glycogen synthase phosphatase activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,4-dimethoxy-2-methylbenzene
-
-
1-(3,4-dihydroxyphenyl)-2-(1H-imidazol-1-yl)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-(2-ethyl-1H-imidazol-1-yl)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-(2-methyl-1H-benzimidazol-1-yl)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-(2-methyl-1H-imidazol-1-yl)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-(2-phenyl-1H-imidazol-1-yl)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-(4-methyl-1H-imidazol-1-yl)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-(4-methyl-1H-pyrazol-1-yl)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-(4H-1,2,4-triazol-4-yl)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-(5,6-dimethyl-1H-benzimidazol-1-yl)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-(propan-2-ylamino)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-[(4,6-dimethylpyrimidin-2-yl)sulfanyl]ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-[(4-methyl-5-phenyl-4H-1,2,4-triazol-3-yl)sulfanyl]ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-[[1-(4-methoxyphenyl)-1H-tetrazol-5-yl]sulfanyl]ethanone
-
-
1-bromotetramisole
-
-
1-chloro-4-ethoxy-2-methylbenzene
-
-
1-chloro-4-methoxy-2-methylbenzene
-
-
1-fluoro-4-methoxybenzene
-
-
2,5-dimethoxy-N-(pyridin-3-yl)benzenesulfonamide
-
-
2,5-dimethoxy-N-(quinolin-3-yl)benzenesulfonamide
-
-
2-(1-methylhydrazenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(1H-benzimidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
-
-
2-(1H-benzimidazol-2-ylamino)-1-(3,4-dihydroxyphenyl)ethanone
-
-
2-(2-ethoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(2-fluorophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(2-methoxyphenyl)-7- trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3,4-di-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3,5-di-methoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3,5-di-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3-cyanophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3-fluoromethylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3-fluorophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3-methoxyphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3-nitrophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(3-phenylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-aminophenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-bromo-1H-imidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
-
-
2-(4-bromo-2-methyl-1H-imidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
-
-
2-(4-ethoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-ethoxyphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-ethylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-i-propylphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-methoxylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-(4-trifluoromethoxylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-allylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-chloro-1,4-dimethoxybenzene
-
-
2-di-n-butylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-ethoxy-5-methyl-N-(pyridin-3-yl)benzenesulfonamide
-
-
2-methoxy-4-nitro-N-(pyridin-3-yl)benzenesulfonamide
-
-
2-methoxy-4-nitro-N-(quinolin-3-yl)benzenesulfonamide
-
-
2-methoxy-5-methyl-N-(pyridin-3-yl)benzenesulfonamide
-
-
2-methoxy-5-methyl-N-(quinolin-3-yl)benzenesulfonamide
-
-
2-n-butylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-n-pentylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-n-propylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-phenyl-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-[2-(dimethylamino)ethyl]amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
-
2-[[2-(3,4-dihydroxyphenyl)-2-oxoethyl]sulfanyl]-4-(methoxymethyl)-6-methylpyridine-3-carbonitrile
-
-
3-[2-(3,4-dihydroxyphenyl)-2-oxoethyl]-6,7-dimethoxy-2-benzofuran-1(3H)-one
-
-
4-bromo-2,5-dimethoxy-N-(pyridin-3-yl)benzenesulfonamide
-
-
4-methoxy-1,2-dimethylbenzene
-
-
4-[[(4,6-dimethylpyrimidin-2-yl)amino]methyl]benzene-1,2-diol
-
-
5-bromo-2-methoxy-N-(quinolin-3-yl)benzenesulfonamide
-
-
5-chloro-2-ethoxy-N-(pyridin-3-yl)benzenesulfonamide
-
-
arsenate
-
-
Be2+
-
-
Ca2+
-
10 mM, glycogen synthase phosphatase activity
Cys
-
uncompetitive inhibition of phosphatase activity, mixed-competitive inhibition of inorganic pyrophosphatase activity. Inorganic pyrophosphatase activity is inhibited more than phosphatase activity. Ca2+ and Mg2+ ion concentrations may regulate this inhibition
diethyl-p-nitrophenyl phosphate
-
-
F-
-
50 mM KF, 13% inhibition of p-nitrophenyl phosphate hydrolysis, 50% inhibition of dephosphorylation of P-labelled histones
heparin
-
histone phosphatase activity
histidine
-
-
L-amino acids
specific uncompetitive inhibition, molecular mechanism involves Arg166 and Glu429
L-homoarginine
L-leucine
-
allozyme D is highly sensitive and shows uncompetitive inhibition, allozymes S and F are less sensitive, allozymes SD and FD, mixed type, respond in an intermediate fashion to inhibition
L-Phe-Gly-Gly
L-phenylalanine
inhibitor of intestinal alkaline phosphatase
Leu
-
L-Leu, uncompetitive, D-Leu with greatly decreased efficiencies
leucinamide
-
-
leucinol
-
-
levamisole
Mg2+
-
-
NaCN
-
-
NADH
-
-
NEM
-
very slowly
p-hydroxymercuribenzoate
-
reactivation by DTT and 2-mercaptoethanol
Phenanthroline
-
-
phenyl phosphonate
-
competitive
phenylalanine
-
-
phenylphosphonate
-
10 mM, 47% inhibition of p-nitrophenyl phosphate hydrolysis, 80% inhibition of dephosphorylation of P-labelled histones
phosphate
-
-
polylysine
-
histone phosphatase activity
protamine
-
histone phosphatase activity
Trimetaphosphate
-
-
vanadate
-
-
Zn2+
-
above 0.02 mM
additional information
-
no inhibition at 10 mM by L-phenylalanine at 10 mM for all three isozymes
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
albumin
-
3fold stimulation of hydrophilic enzyme, slight stimulation of amphiphilic enzyme
-
phosphatidylcholine
-
1fold stimulation of hydrophilic enzyme form
phosphatidylethanolamine
-
1fold stimulation of hydrophilic enzyme form
phosphatidylinositol
-
1.5fold stimulation of hydrophilic enzyme form
phosphatidylserine
-
1fold stimulation of amphiphilic enzyme form, 3fold stimulation of hydrophilic enzyme form
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.5
2'-AMP
-
-
0.01 - 0.177
2-chloro-5-(4-methoxyspiro (1,2-dioxetane-3,2'-(5'-chloro)tricyclo[3.3.1.13,7]decan)-4-yl)phenyl phosphate
0.026 - 0.078
2-naphthyl phosphate
2.3
3'-AMP
-
-
0.0156 - 49.7
4-nitrophenyl phosphate
3
5'-AMP
-
-
4.5
5'-dTMP
-
-
4.4
ADP
-
-
5.7
ATP
-
-
1.4 - 3
beta-Glycerophosphate
0.12 - 4
diphosphate
4.8
glucose 1-phosphate
-
-
0.02 - 5.02
p-nitrophenyl phosphate
0.39 - 0.9
phospho-DL-Thr
0.4 - 0.72
phospho-DL-Tyr
0.38 - 0.68
phospho-L-Ser
2.9
Phosphoethanolamine
-
-
0.12
pyridoxal 5'-phosphate
-
allozyme D, pH 7.5, 37°C, in presence of Mg2+ and Zn2+
0.2 - 0.37
pyridoxal phosphate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
34 - 971
4-nitrophenyl phosphate
244
diphosphate
-
allozyme D, pH 7.5, 37°C, in presence of Mg2+ and Zn2+
92
pyridoxal 5'-phosphate
-
allozyme D, pH 7.5, 37°C, in presence of Mg2+ and Zn2+
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00149
1,4-dimethoxy-2-methylbenzene
Homo sapiens
-
-
0.0012 - 0.0302
1-(3,4-dihydroxyphenyl)-2-(1H-imidazol-1-yl)ethanone
0.0042
1-(3,4-dihydroxyphenyl)-2-(2-ethyl-1H-imidazol-1-yl)ethanone
Homo sapiens
-
-
0.0012 - 0.0263
1-(3,4-dihydroxyphenyl)-2-(2-methyl-1H-benzimidazol-1-yl)ethanone
0.0033 - 0.0783
1-(3,4-dihydroxyphenyl)-2-(2-methyl-1H-imidazol-1-yl)ethanone
0.0172
1-(3,4-dihydroxyphenyl)-2-(2-phenyl-1H-imidazol-1-yl)ethanone
Homo sapiens
-
-
0.0058 - 0.0411
1-(3,4-dihydroxyphenyl)-2-(4-methyl-1H-imidazol-1-yl)ethanone
0.0027 - 0.0533
1-(3,4-dihydroxyphenyl)-2-(4-methyl-1H-pyrazol-1-yl)ethanone
0.0134
1-(3,4-dihydroxyphenyl)-2-(4H-1,2,4-triazol-4-yl)ethanone
Homo sapiens
-
-
0.0058
1-(3,4-dihydroxyphenyl)-2-(5,6-dimethyl-1H-benzimidazol-1-yl)ethanone
Homo sapiens
-
-
0.0393
1-(3,4-dihydroxyphenyl)-2-(propan-2-ylamino)ethanone
Homo sapiens
-
-
0.0006 - 0.0495
1-(3,4-dihydroxyphenyl)-2-[(4,6-dimethylpyrimidin-2-yl)sulfanyl]ethanone
0.0067
1-(3,4-dihydroxyphenyl)-2-[(4-methyl-5-phenyl-4H-1,2,4-triazol-3-yl)sulfanyl]ethanone
Homo sapiens
-
-
0.002 - 0.008
1-(3,4-dihydroxyphenyl)-2-[[1-(4-methoxyphenyl)-1H-tetrazol-5-yl]sulfanyl]ethanone
0.00069
1-chloro-4-ethoxy-2-methylbenzene
Homo sapiens
-
-
0.00051
1-chloro-4-methoxy-2-methylbenzene
Homo sapiens
-
-
0.00129
1-fluoro-4-methoxybenzene
Homo sapiens
-
-
0.00106
2,5-dimethoxy-N-(pyridin-3-yl)benzenesulfonamide
Homo sapiens
-
-
0.00019
2,5-dimethoxy-N-(quinolin-3-yl)benzenesulfonamide
Homo sapiens
-
-
0.00202 - 0.00222
2-(1-methylhydrazenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.0008 - 0.018
2-(1H-benzimidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
0.0062 - 0.0938
2-(1H-benzimidazol-2-ylamino)-1-(3,4-dihydroxyphenyl)ethanone
0.00452 - 0.1
2-(2-ethoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.1
2-(2-fluorophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00348 - 0.1
2-(2-methoxyphenyl)-7- trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00054 - 0.00175
2-(3,4-di-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00076 - 0.00115
2-(3,5-di-methoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00046 - 0.00052
2-(3,5-di-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00056 - 0.00112
2-(3-cyanophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00052 - 0.00068
2-(3-fluoromethylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00074 - 0.00139
2-(3-fluorophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00038 - 0.00044
2-(3-methoxyphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00048 - 0.00062
2-(3-nitrophenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00112 - 0.00167
2-(3-phenylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00033 - 0.00071
2-(4-aminophenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.0158 - 0.0475
2-(4-bromo-1H-imidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
0.0049 - 0.0087
2-(4-bromo-2-methyl-1H-imidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
0.00079 - 0.00093
2-(4-ethoxyphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00158 - 0.00202
2-(4-ethoxyphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00455 - 0.1
2-(4-ethylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00198 - 0.0315
2-(4-i-propylphenyl)amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00028 - 0.00048
2-(4-methoxylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00036 - 0.00106
2-(4-methylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00024 - 0.1
2-(4-trifluoromethoxylphenyl)-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00029 - 0.00089
2-allylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00113
2-chloro-1,4-dimethoxybenzene
Homo sapiens
-
-
0.00153 - 0.00463
2-di-n-butylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00113
2-ethoxy-5-methyl-N-(pyridin-3-yl)benzenesulfonamide
Homo sapiens
-
-
0.00316
2-methoxy-4-nitro-N-(pyridin-3-yl)benzenesulfonamide
Homo sapiens
-
-
0.00074
2-methoxy-4-nitro-N-(quinolin-3-yl)benzenesulfonamide
Homo sapiens
-
-
0.00185
2-methoxy-5-methyl-N-(pyridin-3-yl)benzenesulfonamide
Homo sapiens
-
-
0.00065
2-methoxy-5-methyl-N-(quinolin-3-yl)benzenesulfonamide
Homo sapiens
-
-
0.00071 - 0.00088
2-n-butylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00061 - 0.00076
2-n-pentylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00031 - 0.00144
2-n-propylamino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00021 - 0.00043
2-phenyl-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.00045 - 0.00375
2-[2-(dimethylamino)ethyl]amino-7-trifluoromethyl-5H-1,3,4-thiadiazolo[3,2-a]pyrimidin-5-one
0.0022 - 0.0048
2-[[2-(3,4-dihydroxyphenyl)-2-oxoethyl]sulfanyl]-4-(methoxymethyl)-6-methylpyridine-3-carbonitrile
0.003 - 0.0292
3-[2-(3,4-dihydroxyphenyl)-2-oxoethyl]-6,7-dimethoxy-2-benzofuran-1(3H)-one
0.00155
4-bromo-2,5-dimethoxy-N-(pyridin-3-yl)benzenesulfonamide
Homo sapiens
-
-
0.00168
4-methoxy-1,2-dimethylbenzene
Homo sapiens
-
-
0.0512
4-[[(4,6-dimethylpyrimidin-2-yl)amino]methyl]benzene-1,2-diol
Homo sapiens
-
-
0.00012
5-bromo-2-methoxy-N-(quinolin-3-yl)benzenesulfonamide
Homo sapiens
-
-
0.00054
5-chloro-2-ethoxy-N-(pyridin-3-yl)benzenesulfonamide
Homo sapiens
-
-
0.0802
L-phenylalanine
Homo sapiens
intestinal alkaline phosphatase, at 37°C, pH not specified in the publication
0.0192
levamisole
Homo sapiens
tissue non-specific alkaline phosphatase, at 37°C, pH not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
629
-
purified recombinant enzyme expressed in Sf-9 cells
738
-
purified native placental enzyme
850
-
purified recombinant enzyme expressed in Tn-5B1-4 cells
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9 - 9.5
-
hydrolysis of organic diphosphates
9.2
-
hydrolysis of 2 mM p-nitrophenyl phosphate, borate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
pH 6.0: about 30% of maximal activity, pH 9.0: about 15% of maximal activity
9.5 - 11.5
-
pH 9.5: about 40% of maximal activity, pH 11.5: about 45% of maximal activity, hydrolysis of beta-glycerophosphate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
dental pulp stromal cell
Manually annotated by BRENDA team
-
using a monoclonal antibody against bone specific alkaline phosphatase (BAP), its expression is detected in approximately 50% of circulating B cells but not T cells. Following stimulations with Pokeweed Mitogen (PWM) and Staphylococcus aureus Cowan I (SAC), BAP expression on human B cells is increased
Manually annotated by BRENDA team
-
78 160 cells from brain produce the intestinal isoenzyme
Manually annotated by BRENDA team
-
neuronal and endothelial cells exclusively express the bone TNAP transcript
Manually annotated by BRENDA team
-
HeLa S3 cells from cervix produce the term-placental isoenzyme
Manually annotated by BRENDA team
-
HT-29 cells from colon produce the intestinal isoenzyme
Manually annotated by BRENDA team
-
neutrophilic from peripheral blood
Manually annotated by BRENDA team
-
LoVo cells from colon produce the term-placental and the intestinal isoenzyme
Manually annotated by BRENDA team
-
non-carcinoma tissue. Liver type alkaline phosphatesse AP is detected in the heavy and light surfactant aggregates from both non-carcinoma and squamous carcinoma tissues, but not in heavy surfactant aggregates from adenocarcinoma tissues. A larger amount of bone type alkaline phosphatase is found in light surfactant aggregate fractions from squamous cell carcinomas than those from adenocarcinoma tissues or noncarcinoma tissues from patients with either type of cancer
Manually annotated by BRENDA team
-
neuronal and endothelial cells exclusively express the bone TNAP transcript
Manually annotated by BRENDA team
-
activity increases during adipogenesis
Manually annotated by BRENDA team
-
non-carcinoma tissue. Liver type alkaline phosphatesse AP is detected in the heavy and light surfactant aggregates from both non-carcinoma and squamous carcinoma tissues, but not in heavy surfactant aggregates from adenocarcinoma tissues. A larger amount of bone type alkaline phosphatase is found in light surfactant aggregate fractions from squamous cell carcinomas than those from adenocarcinoma tissues or noncarcinoma tissues from patients with either type of cancer
Manually annotated by BRENDA team
-
SW-620 cells from colon produce the term-placental and the liver/bone/kidney isoenzyme
Manually annotated by BRENDA team
-
T24 cells from bladder produce the term-placental isoenzyme
Manually annotated by BRENDA team
-
enzyme activity of alkaline phosphatase is not observed in chondrocytes of the subperichondral and central cartilage layer of thyroid cartilage prior to cartilage mineralization. In the thyroid cartilage of a male foetus from 23rd gestational week, as well as from a 9-year-old girl and an 11-year-old boy, the enzymohistochemical reaction is negative. Beginning approximately at the middle of the second decade, the reaction product of the enzyme alkaline phosphatase is detected in distinct chondrocytes in the neighbourhood of mineralized cartilage areas or within the mineralized cartilage. In a comparison of aged-matched thyroid cartilages, male thyroid cartilage often contains more chondrocytes with a positive enzymohistochemical reaction for alkaline phosphatase than samples from females
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
the enzyme from liver is associated with the particulate fractions such as nuclei, mitochondria and lysosomes
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
enzyme deficiency diminishes chondrocyte vascular endothelial cell growth factor expression
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PPBT_HUMAN
524
0
57305
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
126000
-
isozyme B/I, native PAGE
136000
-
isozyme B1, native PAGE
141000
-
isozyme B2, native PAGE
146000
gel filtreation
158000
-
gel filtration
200000
-
gel filtration
211000
-
hydrophilic liver enzyme, density gradient gel electrophoresis
214000
-
hydrophilic enzyme form, gradient gel electrophoresis
220000
-
hydrophilic enzyme from osteosarcoma cells, density gradient gel electrophoresis
227000
-
hydrophilic enzyme from lymphoma cells L248, density gradient gel electrophoresis
255000
-
hydrophilic enzyme form, gel filtration
340000
-
gel filtration
433000
-
amphiphilic liver enzyme, density gradient gel electrophoresis
483000
-
amphiphilic enzyme from osteosarcoma cells, density gradient gel electrophoresis
494000
-
amphiphilic enzyme from lymphoma cells L248, density gradient gel electrophoresis
62000
-
x * 62000 or x * 65000, the purified recombinant enzyme appears in two subunit sizes, 62000 Da and 65000 Da, due to heterogenous N-glycosylation, SDS-PAGE
64000
65000
66000
-
immunoblotting, immature form bearing high mannose-type N-linked oligosaccharides
66200
-
native placental enzyme, gel filtration
72000
-
x * 72000, milk isoenzyme, SDS-PAGE
75000
-
2 * 75000, SDS-PAGE
80000
-
immunoblotting, mature form bearing complex-type oligosaccharides
81000
-
x * 81000, liver isoenzyme, SDS-PAGE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 80000, SDS-PAGE
dimer
homodimer
-
sucrose density gradient centrifugation, wild-type and V406A form a homodimer
monomer
-
1 * 64000, recombinant enzyme, SDS-PAGE, 1 * 66200, native enzyme, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
mature form of 80 ka bears complex-type oligosaccharides. The 80 kDa form is sensitive to neuraminidase, but is resistant to treatment with Endo H
glycoprotein
side-chain modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
10-16 mg/ml purified enzyme in 10 mM Tris, pH 7.0, 2 mM MgCl2, 0.02% NaN3, sitting drop vapour diffusion method, free or in complex with substrate 4-nitrophenyl phosphate, reservoir solution: 12-14% PEG 4000, 20% PEG 3350, 2 mM zinc acetate, 100 mM sodium cacodylate, pH 6.5, the buffer can also be acetate, citrate or imidazole malate, X-ray diffraction structure determination and analysis at 1.9 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C201Y
mutation identified in patient diagnosed with perinatal hypophosphatasia. Mutants exhibit a diminished alkaline phosphatase activity in the cells, where a 66 kDa immature form is predominant with a marginal amount of a 80 kDa mature form. The 66 kDa form exists as a monomer in contrast to a dimer form of wild-type. Only a small fraction of the mutant protein reaches cell surface as the 80 kDa mature form, most of the 66 kDa form is found to be endo-beta-N-acetylglucosaminidase H sensitive and rapidly degraded in proteasome following polyubiquitination
C489S
mutation identified in patient diagnosed with perinatal hypophosphatasia. Mutants exhibit a diminished alkaline phosphatase activity in the cells, where a 66 kDa immature form is predominant with a marginal amount of a 80 kDa mature form
G420A
naturally occuring mutant, reported in perinatal and childhood hypophosphatasia. Mutant lacks its alkaline phosphatase activity
G420S
naturally occuring mutant, reported in perinatal and childhood hypophosphatasia. Mutant lacks its alkaline phosphatase activity, although mutant protein is anchored to the cell surface lipid bilayers by glycosylphosphatidylinositol as an 80 kDa mature form bearing complex-type oligosaccharides similar to wild-type. Mutant G420S largely fails to assemble into the homodimer in contrast to wild-type
N417D
mutation abolishes the dimerization without perturbing its cell surface localization
N417E
mutation abolishes the dimerization without perturbing its cell surface localization
N417S
mutation associated with severe hypophosphatasia, mutants lack enzymic activity. Mutant undergoes N-linked oligosaccharide processing and appears on the cell surface similar to wild-type. Mutant fails to assemble into a dimer structure, which is needed for the catalytic function
P108L
inactive, the mutation is associated with dominant odontohypophosphatasia
A115V
-
activity in U2OS cells after 48h after transfection: 0.1%
A116T
-
mutant responsible for hypophosphatasia shows negligible alkaline phosphatase activity and a weak dominant negative effect when co-expressed with the wild-type enzyme, mutant exists as a monomer and heterogeneously associated aggregates covalently linked via disulfide bonds in contrast to wild-type enzyme which exists as a homodimer
A16V
-
in combination with P275T the mutation causes infantile hypophosphatasia, 7.2% of wild-type activity
M278T
-
lethal mutation, 8.5% of wild-type activity
P275T
-
in combination with A16V mutation causes infantile hypophosphatasia, 4% of wild-type activity
R119H
-
in combination with Y280D the mutation causes childhood hypophosphatasia, 33.4% of wild-type activity
R166A
-
mutation changes the inhibition mechanism of the mutant enzyme to a more complex mixed-type inhibition with decreased affinities for L-Leu and L-Phe
R206W
-
lethal mutation, 2.8% of wild-type activity
R255H
-
mutation (homozygote) causes infantile hypophosphatasia, 6.8% of wild-type activity
R54A
-
activity in U2OS cells after 48h after transfection: 0.1%
T394
-
lethal mutation, 0.3% of wild-type activity
V406A
-
mutant protein shows a markedly reduced alkaline phosphatase activity. Mutant is conveyed to the Golgi apparatus and incorporated into a cold detergent insoluble fraction (raft) at a rate similar to that of the wild-type. Mutant shows increased susceptibility to digestion by trypsin or proteinase K. When purified as a glycosylphosphatidylinositol-anchorless soluble form, mutant protein exhibits a remarkably lower Kcat /Km value compared with that of the wild-type TNSALP
V406F
-
replacement with phenylalanine results in a low enzyme activity, even though TNSALP (V406F) is processed to the 80 kDa mature form similarly to TNSALP (V406A) and appears on the cell surface like the wild-type protein
V406I
-
similar to wild-type, leucine and isoleucine can be successfully substituted for the valine residue
V406L
-
similar to wild-type, leucine and isoleucine can be successfully substituted for the valine residue
Y280D
-
in combination with R119H the mutation causes childhood hypophosphatasia, 1.3% of wild-type activity
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.1
-
0°C, 65% inactivation of the intestinal enzyme, liver enzyme is inactivated at a rate too rapid to be measured, the longer the period in acid the smaller is the percentage of reactivation attainable after returning to pH 7.2
94581
3.5
-
about 50% loss of activity of the liver enzyme after 25 min, about 85% loss of activity of the bone enzyme after 5 min
94582
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54
-
20 min, about 45% loss of activity of the liver enzyme, about 60% loss of activity of the bone enzyme
61
-
allozyme D, half-life 10 min, in presence of Zn2+ and Mg2+, pH 9.8
72
-
allozyme S and F, half-life 10 min, in presence of Zn2+ and Mg2+, pH 9.8
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
24 h incubation is necessary for reaching an unfolding equilibrium, dimeric enzyme does not show any sign of dissociation up to a urea concentration of 4 M
8 M urea, at 37°C, half-life of placental enzyme: 3 h. 3 M urea, half-life of the bone enzyme: 7 min
-
at urea concentrations below a critical value, the enzymes are only slightly and reversibly inhibited, but above this value inactivation is progressive with time and generally irreversible. The critical concentration of urea is considerably greater for intestinal phosphatase than for the kidney and liver enzyme
-
urea, 3 M, 5 h, about 50% loss of activity of the liver enzyme, about 60% loss of activity of the bone enzyme. 5 M, 30 min, about 70% loss of activity of the liver enzyme, about 90% loss of activity of the bone enzyme. 6 M, 10 min, about 70% loss of activity of the liver enzyme, about 90% loss of activity of the bone enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 18% loss of activity after 2 years
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from placenta
partial purification of isozymes
-
purified from human placental tissue extract. The purity of PLAP after a gel filtration step is above 97%
-
recombinant
recombinant enzyme from expression in insect cells
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Tet-On CHO cells
expression in COS-1 cell
expression in COS-1 cells and CHO K1 Tet-On cells
transient expression in COS-1 cell
two transgenic rabbit lines are created by pronuclear microinjection with the whey acidic protein promoter-humanTNAP minigene (WAP-hTNAP). lactating females of both lines produce biologically active human TNAP. The recombinant alkaline phosphatase is associated with the membrane of milk fat globules. Use of transgenic rabbits as bioreactors for bulk production of human tissue-nonspecific alkaline phosphatase in milk
allozyme D, ALPP, of placental enzyme form PALP, DNA and amino acid sequence determination of PALP and allozymes, comparison and analysis, substitutions from PALP to ALPP are found at P209R and E429G, subcloning in Escherichia coli XL1-blue, and expression of allozymes D, ALPP, in CHO cells
-
expressed enzyme-deficient Mus musculus
-
expressed in COS-1 cells
-
expressed in transiently transfected COS-1 cells and in stable CHO-K1 Tet-On cells
-
expression in Pichia pastoris
expression in Spodoptera frugiperda Sf9 and Trichoplusia ni BTI-Tn-5B1-4 insect cells via infection with recombinant Autographa california multiple nuclear polyhedrovirus expressing SEAP under control of the polyhedrin promotor, the recombinant enzyme expressed in the 2 different insect cell lines show differing N-glycan structures
-
human 1.6 kb IAP cDNA is subcloned into the pIRES2-EGFP vector, and the construct thus obtained (pIRES2-IAP-EGFP) is used to transfect into IEC-6, T84, and HT-29 cell lines. Stable cell lines are selected by G418 exposure
-
liver and milk isoenzymes have similar or perhaps identical peptide structures and may be coded by the same gene
-
three gene loci seem to be involved in determining the various forms of alkaline phosphatase, one coding for the placental form, at least one coding for the intestinal forms, and at least one for the liver, bone and kidney forms
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression by human dental pulp stromal cells is increased at high cell density
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
medicine
molecular biology
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
Herz, F.
Alkaline phosphatase isozymes in cultured human cancer cells
Experientia
41
1357-1361
1985
Homo sapiens
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
Heimo, H.; Palmu, K.; Suominen, I.
Human placental alkaline phosphatase: expression in Pichia pastoris, purification and characterization
Protein Expr. Purif.
12
85-92
1998
Homo sapiens
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
Spencer, T.; Macrae, S.L.
Some properties of the alkaline phosphatase of HeLa cells
Enzymologia
42
329-341
1972
Homo sapiens
Manually annotated by BRENDA team
Ghosh, N.K.; Kotowitz, L.
On the intracellular distribution of alkaline phosphatase in human liver and intestine
Enzymologia
36
54-58
1969
Homo sapiens
Manually annotated by BRENDA team
Scutt, P.B.; Moss, D.W.
Reversible inactivation of alkaline phosphatase in acid solution
Enzymologia
35
157-167
1968
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Eaton, R.H.; Moss, D.W.
Partial purification and some properties of human bone alkaline phosphatase
Enzymologia
35
31-39
1968
Homo sapiens
Manually annotated by BRENDA team
Ghosh, N.K.; Goldman, S.S.; Fishman, W.H.
Human placental alkaline phosphatase; a sialoprotein
Enzymologia
33
113-124
1967
Homo sapiens
Manually annotated by BRENDA team
Butterworth, P.J.; Moss, D.W.
The effect of urea on human alkaline-phosphatase preparations
Enzymologia
32
269-277
1967
Homo sapiens
-
Manually annotated by BRENDA team
Fedde, K.N.; Lane, C.C.; Whyte, M.P.
Alkaline phosphatase is an ectoenzyme that acts on micromolar concentrations of natural substrates at physiologic pH in human osteosarcoma (SAOS-2) cells
Arch. Biochem. Biophys.
264
400-409
1988
Homo sapiens
Manually annotated by BRENDA team
Garattini, E.; Hua, J.C.; Pan, Y.C.E.; Udenfriend, S.
Human liver alkaline phosphatase, purification and partial sequencing: homology with the placental isozyme
Arch. Biochem. Biophys.
245
331-337
1986
Homo sapiens
Manually annotated by BRENDA team
Chakrabartty, A.; Stinson, R.A.
Properties of membrane-bound and solubilized forms of alkaline phosphatase from human liver
Biochim. Biophys. Acta
839
174-180
1983
Homo sapiens
Manually annotated by BRENDA team
Kobori, H.; Taga, N.
Extracellular alkaline phosphatase from marine bacteria: purification and properties of extracellular phosphatase from a marine Pseudomonas sp.
Can. J. Microbiol.
26
833-838
1980
Homo sapiens, Pseudomonas sp.
-
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
Hamilton, T.A.; Gornicki, S.Z.; Sussman, H.H.
Alkaline phosphatase from human milk. Comparison with isoenzymes from placenta and liver
Biochem. J.
177
197-201
1979
Homo sapiens
Manually annotated by BRENDA team
Harkness, D.R.
Studies on human placental alkaline phosphatase. II. Kinetic properties and studies on the apoenzyme
Arch. Biochem. Biophys.
126
513-523
1968
Homo sapiens
Manually annotated by BRENDA team
Kihn, L.; Rutkowski, D.; Nakatsui, T.; Stinson, R.A.
Properties of amphiphilic and hydrophilic forms of alkaline phosphatase from human liver
Enzyme
45
155-164
1991
Homo sapiens
Manually annotated by BRENDA team
Chuang, N.N.; Yang, B.C.
A comparative study of alkaline phosphatases among human placenta, bovine milk, hepatopancreas of shrimp Penaeus monodon (Crustacea: decapoda) and clam Meretrix lusoria (bivalvia: veneidae): to obtain an alkaline phosphatase with improved characteristics as a reporter
Comp. Biochem. Physiol. B
96
787-789
1990
Homo sapiens, Meretrix lusoria, Penaeus monodon
Manually annotated by BRENDA team
Belland, L.; Visser, L.; Poppema, S.; Stinson, R.A.
Characterization of the alkaline phosphatase expressed on the surface of a Hodgki's lymphoma cell line
Enzyme Protein
47
73-82
1993
Homo sapiens
Manually annotated by BRENDA team
Hoylaerts, M.F.; Manes, T.; Millan, J.L.
Molecular mechanism of uncompetitive inhibition of human placental and germ-cell alkaline phosphatase
Biochem. J.
286
23-30
1992
Homo sapiens
Manually annotated by BRENDA team
Hojring, N.; Svensmark, O.
Carboxylesterases of human brain extract. Purification and properties of a butyrylesterase
Biochim. Biophys. Acta
481
500-514
1977
Homo sapiens
Manually annotated by BRENDA team
Wolf, P.L.; Horwitz, J.P.; Vazquez, J.; von der Muehll, E.
A new histochemical stain for neutrophilic leukocyte alkaline phosphatase
Enzymologia
35
154-156
1968
Homo sapiens
Manually annotated by BRENDA team
Zhang, F.; Murhammer, D.W.; Linhardt, R.J.
Enzyme kinetics and glycan structural characterization of secreted alkaline phosphatase prepared using the baculovirus expression vector system
Appl. Biochem. Biotechnol.
101
197-210
2002
Homo sapiens
Manually annotated by BRENDA team
Magnusson, P.; Farley, J.R.
Differences in sialic acid residues among bone alkaline phosphatase isoforms: a physical, biochemical, and immunological characterization
Calcif. Tissue Int.
71
508-518
2002
Homo sapiens
Manually annotated by BRENDA team
Wennberg, C.; Kozlenkov, A.; Di Mauro, S.; Frohlander, N.; Beckman, L.; Hoylaerts, M.F.; Millan, J.L.
Structure, genomic DNA typing, and kinetic characterization of the D allozyme of placental alkaline phosphatase (PLAP/ALPP)
Hum. Mutat.
19
258-267
2002
Homo sapiens
Manually annotated by BRENDA team
Le Du, M.H.; Stigbrand, T.; Taussig, M.J.; Menez, A.; Stura, E.A.
Crystal structure of alkaline phosphatase from human placenta at 1.8 A resolution. Implication for a substrate specificity
J. Biol. Chem.
276
9158-9165
2001
Homo sapiens (P05187), Homo sapiens
Manually annotated by BRENDA team
Miao, D.; Scutt, A.
Histochemical localization of alkaline phosphatase activity in decalcified bone and cartilage
J. Histochem. Cytochem.
50
333-340
2002
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
O'Riordan, S.; Baker, A.J.; Sherwood, R.A.
Isoenzyme characterization in isolated elevation of alkaline phosphatase after liver transplantation in children
Transplantation
74
1030-1034
2002
Homo sapiens
Manually annotated by BRENDA team
Brun-Heath, I.; Taillandier, A.; Serre, J.L.; Mornet, E.
Characterization of 11 novel mutations in the tissue non-specific alkaline phosphatase gene responsible for hypophosphatasia and genotype-phenotype correlations
Mol. Genet. Metab.
84
273-277
2005
Homo sapiens
Manually annotated by BRENDA team
Nishioka, T.; Tomatsu, S.; Gutierrez, M.A.; Miyamoto, K.I.; Trandafirescu, G.G.; Lopez, P.L.; Grubb, J.H.; Kanai, R.; Kobayashi, H.; Yamaguchi, S.; Gottesman, G.S.; Cahill, R.; Noguchi, A.; Sly, W.S.
Enhancement of drug delivery to bone: Characterization of human tissue-nonspecific alkaline phosphatase tagged with an acidic oligopeptide
Mol. Genet. Metab.
88
244-255
2006
Homo sapiens
Manually annotated by BRENDA team
Chen, Y.H.; Chang, T.C.; Chang, G.G.
Functional expression, purification, and characterization of the extra stable human placental alkaline phosphatase in the Pichia pastoris system
Protein Expr. Purif.
36
90-99
2004
Homo sapiens (P05187), Homo sapiens
Manually annotated by BRENDA team
Ali, A.T.; Penny, C.B.; Paiker, J.E.; Psaras, G.; Ikram, F.; Crowther, N.J.
The relationship between alkaline phosphatase activity and intracellular lipid accumulation in murine 3T3-L1 cells and human preadipocytes
Anal. Biochem.
354
247-254
2006
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Hoylaerts, M.F.; Ding, L.; Narisawa, S.; Van Kerckhoven, S.; Millan, J.L.
Mammalian alkaline phosphatase catalysis requires active site structure stabilization via the N-terminal amino acid microenvironment
Biochemistry
45
9756-9766
2006
Homo sapiens (P05187), Homo sapiens
Manually annotated by BRENDA team
Reilly, G.C.; Radin, S.; Chen, A.T.; Ducheyne, P.
Differential alkaline phosphatase responses of rat and human bone marrow derived mesenchymal stem cells to 45S5 bioactive glass
Biomaterials
28
4091-4097
2007
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Iino, N.; Matsunaga, T.; Harada, T.; Igarashi, S.; Koyama, I.; Komoda, T.
Comparative characterization of pulmonary surfactant aggregates and alkaline phosphatase isozymes in human lung carcinoma tissue
Cell Tissue Res.
328
355-363
2007
Homo sapiens
Manually annotated by BRENDA team
Claassen, H.; Moenig, H.; Sel, S.; Werner, J.A.; Paulsen, F.
Androgen receptors and gender-specific distribution of alkaline phosphatase in human thyroid cartilage
Histochem. Cell Biol.
126
381-388
2006
Homo sapiens
Manually annotated by BRENDA team
So, P.P.; Tsui, F.W.; Vieth, R.; Tupy, J.H.; Pritzker, K.P.
Inhibition of alkaline phosphatase by cysteine: implications for calcium pyrophosphate dihydrate crystal deposition disease
J. Rheumatol.
34
1313-1322
2007
Homo sapiens
Manually annotated by BRENDA team
Bednarska, K.; Klink, M.; Sulowska, Z.
Application of intracellular alkaline phosphatase activity measurement in detection of neutrophil adherence in vitro
Mediators Inflamm.
2006
19307
2006
Homo sapiens
Manually annotated by BRENDA team
Bodrogi, L.; Brands, R.; Raaben, W.; Seinen, W.; Baranyi, M.; Fiechter, D.; Bosze, Z.
High level expression of tissue-nonspecific alkaline phosphatase in the milk of transgenic rabbits
Transgenic Res.
15
627-636
2006
Homo sapiens (P05186), Homo sapiens
Manually annotated by BRENDA team
Sesana, S.; Re, F.; Bulbarelli, A.; Salerno, D.; Cazzaniga, E.; Masserini, M.
Membrane features and activity of GPI-anchored enzymes: alkaline phosphatase reconstituted in model membranes
Biochemistry
47
5433-5440
2008
Homo sapiens
Manually annotated by BRENDA team
Hossain, A.; Jung, L.K.
Expression of bone specific alkaline phosphatase on human B cells
Cell. Immunol.
253
66-70
2008
Homo sapiens
Manually annotated by BRENDA team
Numa, N.; Ishida, Y.; Nasu, M.; Sohda, M.; Misumi, Y.; Noda, T.; Oda, K.
Molecular basis of perinatal hypophosphatasia with tissue-nonspecific alkaline phosphatase bearing a conservative replacement of valine by alanine at position 406. Structural importance of the crown domain
FEBS J.
275
2727-2737
2008
Homo sapiens
Manually annotated by BRENDA team
Orimo, H.; Goseki-Sone, M.; Hosoi, T.; Shimada, T.
Functional assay of the mutant tissue-nonspecific alkaline phosphatase gene using U2OS osteoblast-like cells
Mol. Genet. Metab.
94
375-381
2008
Homo sapiens
Manually annotated by BRENDA team
Goldberg, R.F.; Austen, W.G.; Zhang, X.; Munene, G.; Mostafa, G.; Biswas, S.; McCormack, M.; Eberlin, K.R.; Nguyen, J.T.; Tatlidede, H.S.; Warren, H.S.; Narisawa, S.; Millan, J.L.; Hodin, R.A.
Intestinal alkaline phosphatase is a gut mucosal defense factor maintained by enteral nutrition
Proc. Natl. Acad. Sci. USA
105
3551-3556
2008
Homo sapiens
Manually annotated by BRENDA team
Lanier, M.; Sergienko, E.; Simao, A.M.; Su, Y.; Chung, T.; Millan, J.L.; Cashman, J.R.
Design and synthesis of selective inhibitors of Placental Alkaline Phosphatase
Bioorg. Med. Chem.
18
573-579
2010
Homo sapiens
Manually annotated by BRENDA team
Dahl, R.; Sergienko, E.A.; Su, Y.; Mostofi, Y.S.; Yang, L.; Simao, A.M.; Narisawa, S.; Brown, B.; Mangravita-Novo, A.; Vicchiarelli, M.; Smith, L.H.; ONeill, W.C.; Millan, J.L.; Cosford, N.D.
Discovery and validation of a series of aryl sulfonamides as selective inhibitors of tissue-nonspecific alkaline phosphatase (TNAP)
J. Med. Chem.
52
6919-6925
2009
Homo sapiens
Manually annotated by BRENDA team
Ding, J.; Ghali, O.; Lencel, P.; Broux, O.; Chauveau, C.; Devedjian, J.C.; Hardouin, P.; Magne, D.
TNF-alpha and IL-1beta inhibit RUNX2 and collagen expression but increase alkaline phosphatase activity and mineralization in human mesenchymal stem cells
Life Sci.
84
499-504
2009
Homo sapiens
Manually annotated by BRENDA team
Ishida, Y.; Komaru, K.; Oda, K.
Molecular characterization of tissue-nonspecific alkaline phosphatase with an Ala to Thr substitution at position 116 associated with dominantly inherited hypophosphatasia
Biochim. Biophys. Acta
1812
326-332
2011
Homo sapiens
Manually annotated by BRENDA team
Brun-Heath, I.; Ermonval, M.; Chabrol, E.; Xiao, J.; Palkovits, M.; Lyck, R.; Miller, F.; Couraud, P.; Mornet, E.; Fonta, C.
Differential expression of the bone and the liver tissue non-specific alkaline phosphatase isoforms in brain tissues
Cell Tissue Res.
343
521-536
2011
Callithrix jacchus, Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Satou, Y.; Al-Shawafi, H.A.; Sultana, S.; Makita, S.; Sohda, M.; Oda, K.
Disulfide bonds are critical for tissue-nonspecific alkaline phosphatase function revealed by analysis of mutant proteins bearing a C(201)-Y or C(489)-S substitution associated with severe hypophosphatasia
Biochim. Biophys. Acta
1822
581-588
2012
Homo sapiens (P05186), Homo sapiens
Manually annotated by BRENDA team
Makita, S.; Al-Shawafi, H.A.; Sultana, S.; Sohda, M.; Nomura, S.; Oda, K.
A dimerization defect caused by a glycine substitution at position 420 by serine in tissue-nonspecific alkaline phosphatase associated with perinatal hypophosphatasia
FEBS J.
279
4327-4337
2012
Homo sapiens (P05186)
Manually annotated by BRENDA team
Pettengill, M.; Robson, S.; Tresenriter, M.; Millan, J.L.; Usheva, A.; Bingham, T.; Belderbos, M.; Bergelson, I.; Burl, S.; Kampmann, B.; Gelinas, L.; Kollmann, T.; Bont, L.; Levy, O.
Soluble ecto-5-nucleotidase (5-NT), alkaline phosphatase, and adenosine deaminase (ADA1) activities in neonatal blood favor elevated extracellular adenosine
J. Biol. Chem.
288
27315-27326
2013
Homo sapiens
Manually annotated by BRENDA team
Sultana, S.; Al-Shawafi, H.A.; Makita, S.; Sohda, M.; Amizuka, N.; Takagi, R.; Oda, K.
An asparagine at position 417 of tissue-nonspecific alkaline phosphatase is essential for its structure and function as revealed by analysis of the N417S mutation associated with severe hypophosphatasia
Mol. Genet. Metab.
109
282-288
2013
Homo sapiens (P05186)
Manually annotated by BRENDA team
Jazaeri, M.; Malekzadeh, H.; Abdolsamadi, H.; Rezaei-Soufi, L.; Samami, M.
Relationship between salivary alkaline phosphatase enzyme activity and the concentrations of salivary calcium and phosphate ions
Cell J.
17
159-162
2015
Homo sapiens
Manually annotated by BRENDA team
Tomlinson, M.; Dennis, C.; Yang, X.; Kirkham, J.
Tissue non-specific alkaline phosphatase production by human dental pulp stromal cells is enhanced by high density cell culture
Cell Tissue Res.
361
529-540
2015
Homo sapiens (P05186), Homo sapiens
Manually annotated by BRENDA team
Herman, D.S.; Ranjitkar, P.; Yamaguchi, D.; Grenache, D.G.; Greene, D.N.
Endogenous alkaline phosphatase interference in cardiac troponin I and other sensitive chemiluminescence immunoassays that use alkaline phosphatase activity for signal amplification
Clin. Biochem.
49
1118-1121
2016
Homo sapiens
Manually annotated by BRENDA team
Jafari, B.; Ospanov, M.; Ejaz, S.A.; Yelibayeva, N.; Khan, S.U.; Amjad, S.T.; Safarov, S.; Abilov, Z.A.; Turmukhanova, M.Z.; Kalugin, S.N.; Ehlers, P.; Lecka, J.; Sevigny, J.; Iqbal, J.; Langer, P.
2-Substituted 7-trifluoromethyl-thiadiazolopyrimidones as alkaline phosphatase inhibitors. Synthesis, structure activity relationship and molecular docking study
Eur. J. Med. Chem.
144
116-127
2018
Homo sapiens (P09487), Homo sapiens (P19111)
Manually annotated by BRENDA team
Nam, H.; Sharma, M.; Liu, J.; Hatch, N.
Tissue nonspecific alkaline phosphatase (TNAP) regulates cranial base growth and synchondrosis maturation
Front. Physiol.
8
161
2017
Homo sapiens
Manually annotated by BRENDA team
Numa-Kinjoh, N.; Komaru, K.; Ishida, Y.; Sohda, M.; Oda, K.
Molecular phenotype of tissue-nonspecific alkaline phosphatase with a proline (108) to leucine substitution associated with dominant odontohypophosphatasia
Mol. Genet. Metab.
115
180-185
2015
Homo sapiens (P05186)
Manually annotated by BRENDA team