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Information on EC 3.1.3.1 - alkaline phosphatase and Organism(s) Rattus norvegicus and UniProt Accession P08289
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3.1.3.1 alkaline phosphataseIUBMB 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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Word Map
- 3.1.3.1
- osteoblast
- osteocalcin
-
osteogenic
- collagen
- aminotransferase
- bilirubin
- women
- mesenchymal
- albumin
- pancreatitis
- marrow
- parathyroid
- phosphorus
- urinary
- cholesterol
- osteoporosis
- creatinine
- resorption
- arterial
- fracture
- children
-
alt
- necrosis
- pain
- femoral
- spine
- transaminase
-
osteogenesis
-
lumbar
- biliary
-
morphogenetic
- osteopontin
- anterior
- bile
- femur
- periodontal
-
radiological
-
gamma-glutamyl
- calcification
- dental
-
postoperative
-
biocompatibility
- gg
-
preoperative
- transpeptidase
- ligament
-
admission
-
postmenopausal
- trabecular
-
hepatoprotective
- biotechnology
- agriculture
- medicine
- food industry
- environmental protection
- analysis
- molecular biology
- diagnostics
- synthesis
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alkaline phenyl phosphatase
-
-
-
-
alkaline phosphohydrolase
-
-
-
-
alkaline phosphomonoesterase
-
-
-
-
ALP
AP-TNAP
-
-
-
-
APase
-
-
-
-
APASED
-
-
-
-
BC6
-
-
-
-
EAP
-
-
-
-
Germ-cell alkaline phosphatase
-
-
-
-
glycerophosphatase
-
-
-
-
H-AP
-
-
-
-
High molecular weight phosphatase
-
-
-
-
IAP
-
-
-
-
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
-
-
-
-
TNSALP
-
-
-
-
ALP
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a phosphate monoester + H2O = an alcohol + phosphate
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
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
9001-78-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
additional information
?
-
-
enzyme is impportant in bone formation and mineralization
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
enzyme is impportant in bone formation and mineralization
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Al3+
-
inhibits high molecular weight and low molecular weight alkaline phosphatase non-competitively
Mg2+
Zn2+
additional information
Mg2+
-
metalloprotein contains Zn2+ and Mg2+, both of which are necessary for catalytic function
Zn2+
-
metalloprotein contains Zn2+ and Mg2+, both of which are necessary for catalytic function
additional information
-
the SWISS-MODEL program is used to construct a model of isoenzyme rIAP-I. Analysis of the active site of the enzyme and the effect of various combinations of metals at the active site. The model shows the possibility of a Zn triad at the metal-binding position of the active site in rIAP-I
additional information
-
the SWISS-MODEL program is used to construct a model of isoenzyme rIAP-II. Analysis of the active site of the enzyme and the effect of various combinations of metals at the active site
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alendronate
-
0.01-0.1 mM, coincubation with excess Zn2+ or Mg2+ completely abolish inhibition
Cd2+
-
chronic cadmium exposure (32.5 ppm Cd2+ in purified water over 3 months) leads to noncompetitive inhibition of serum and hepatic enzyme activity. The addition of 5 mM of Zn2+ shows almost 58% reactivation of the enzyme
pamidronate
-
0.01-0.1 mM, coincubation with excess Zn2+ or Mg2+ completely abolish inhibition
Phe
-
20 mM, 82-99% inhibition of the soluble enzyme form, 68-95% inhibition of the particulate enzyme form
zoledronate
-
0.01-0.1 mM, coincubation with excess Zn2+ or Mg2+ completely abolish inhibition
L-homoarginine
-
powerful inhibitor of the bone/liver/kidney isoenzyme and for the osteosarcoma cell enzyme
levamisole
-
inhibits brush border membrane enzyme activity in the upper villus but is less effective in the middle villus and has no effect on alkaline phosphatase activity in the mucus gel
levamisole
-
hydrolysis of pyrophosphate by rat aortic rings is inhibited about half by the nonspecific alkaline phosphatase inhibitor levamisole. Hydrolysis is increased in aortic rings from uremic rats and all of this increase is inhibited by levamisole
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.05 - 3.62
-
isozymes in intestine segmented into 20 segments, highest activity in the apical part, lowest in the basal, overview
additional information
additional information
-
56% of intestinal activity is retained using HPLC for separation
additional information
56% of intestinal activity is retained using HPLC for separation
additional information
-
56% of intestinal activity is retained using HPLC for separation
additional information
56% of intestinal activity is retained using HPLC for separation
additional information
-
57% of intestinal activity is retained using HPLC for separation. Increased activity is detected after cleaving ALP from the cellular membrane by GPI-specific phospholipase C
additional information
57% of intestinal activity is retained using HPLC for separation. Increased activity is detected after cleaving ALP from the cellular membrane by GPI-specific phospholipase C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.2 - 11
-
pH 9.2: about 40% of maximal activity, pH 11.0: about 60% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
initial expression of mAPase occurs as cells progressed into S phase
-
matrix, articular, of proximal tibiae, highest activity in the hypertrophic zone
-
no activity in resting chondrocytes and the matrix of reserve zone
-
villous surface. HCO3- secretion increases alkaline phosphatase activity by increasing local pH at its catalytic site. Alkaline phosphatase hydrolyzes luminal phosphates, presumably ATP, which increases HCO3- secretion via activation of P2 receptors
-
elevated levels of alkaline phosphatase activity when grown on 45S5 bioactive glass as compared to standard tissue culture plastic. Similarly, exposure to the dissolution products of 45S5 elevates alkaline phosphatase activity and other osteogenic markers in these cells
-
the soluble and the membranous form are closely related but distinct isoenzymes
-
several isozymes, high activity in the upper part compared to the lower one
-
brush border of intestinal epithelial cells. Vitamin K1 and K2 as nutritional factors enhance intestinal alkaline phosphatase activity
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
ALP is localized in the Golgi area of the cytoplasm in solitary McA-RH 7777 cells cultured at low concentration. Contact between McA-RH 7777 cells promotes the translocation of ALP from the Golgi area of the cytoplasm to the plasma membrane. Colchicine caused siruption of the Golgi complex into fragments, which scatters throughout the cytoplasm, does not interfere with translocation of ALP to the plasma membrane
-
hepatocytes cultured in colchicine-containing medium
additional information
-
in hepatocytes cultured in the same medium containing colchicine, the structure of microtubules in the cytoplasm is lost, ALP is localized in coarse granular sites of the cytoplasm
-
ALP is found in the soluble form as well as in the insoluble form bound to the mebrane via a GPI anchor
-
in hepatocytes cultured in basal medium, ALP is localized in the perinuclear cytoplasm
-
-
when hepatocytes are cultured in dexamethasone-supplemented medium, ALP is also localized in the plasma membrane surrounding the bile canaliculus-like structure that is formed between adjacent cells
-
hepatocytes cultured in dexamethason-supplemented medium
ALP is found in the soluble form as well as in the insoluble form bound to the mebrane via a GPI anchor
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PPBT_RAT
524
0
57659
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
160000
80000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
side-chain modification
-
glycoprotein, the soluble form contains more fucose and N-acetylgalactosamine than does the membranous form. The soluble enzyme form contains 19.8% carbohydrate, the membranous enzyme form contains 16% carbohydrate
side-chain modification
-
glycoprotein, contains at least 20% by weight of carbohydrate
side-chain modification
-
glycoprotein is anchored to the membrane by the glycosyl-phosphatidylinositol linkage
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
TNAP activity increases twofold in intact aortas and in aortic homogenates from rats made uremic by feeding adenine or by 5/6 nephrectomy. Immunoblotting showsS an increase in protein abundance but there is no increase in TNAP mRNA. An increase in TNAP activity and pyrophosphate hydrolysis also occurres when aortic rings from normal rats are incubated with uremic rat plasma
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
denaturation follows first order kinetics with t1/2 values ranging from 3.5 min to 57.7 min
55
56
65
-
50% inactivation of the placental enzyme after 0.42 min, 50% inactivation of the liver enzyme after 0.84 min
additional information
55
-
16 min, 92% inactivation of enzyme from 20 day term fetal placentae, 86% loss of activity of enzyme from anestrus control uteri, 30% inactivation of the enzyme from small intestine
56
-
50% inactivation of the placental enzyme after 2.2 min, 50% inactivation of the liver enzyme after 5.0 min
additional information
-
high molecular weight alkaline phosphatase is less heat and urea stable than low molecular weight alkaline phosphatase
additional information
-
low molecular weight alkaline phosphatase is more heat and urea stable than high molecular weight alkaline phosphatase
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by using HPLC separation of a rat liver homogenate three peaks are obtained (rTL1, rTL2 and rTL3)
by using HPLC separation of a intestinal homogenate two ALP peaks (rTI2A and rTI2B) are obtained
by using HPLC separation of a rat bone homogenate one peak is obtained
by using HPLC separation of a rat liver homogenate three peaks are obtained (rTL1, rTL2 and rTL3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in vivo studies show that injection of AlCl3 in male rats results in an increased expression of serum alkaline phosphatase
-
in vivo studies show that injection of AlCl3 in male rats results in decreased expression of brain and liver alkaline phosphatase. Gel filtration experiments disclose a high level of high molecular weight alkaline phosphatase compared to control animals
-
in vivo studies show that injection of AlCl3 in male rats results in decreased expression of brain and liver alkaline phosphatase. Gel filtration studies show a significant reduction in low molecular weight alkaline phosphatase compared to control groups
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
development of a simple in situ duodenal alkaline phosphatase activity assay based on the fluorogenic substrate ELF
medicine
-
a circulating factor causes pyrophosphate deficiency by regulating TNAP activity and vascular calcification in renal failure may result from the action of this factor
molecular biology
-
colchicine inhibits the dexamethasone-promoted translocation of ALP to the plasma membrane surrounding the bile canaliculus-like structure in primary cultures of fetal rat hepatocytes by disassembling microtubules and discomposing the Golgi complex
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Wang, H.; Gilles-Baillien, M.
Alkaline phosphatase and ATPases in brush border membranes of rat jejunum: distinct effects of divalent cations and of some inhibitors
Arch. Int. Physiol. Biochim. Biophys.
100
289-294
1992
Rattus norvegicus
Wright, P.J.; Leathwood, P.D.; Plummer, D.T.
Enzymes in rat urine: alkaline phosphatase
Enzymologia
42
317-327
1972
Rattus norvegicus
Manning, J.P.; Green, S.; Inglis, N.R.; Fishman, W.H.
Characterization of alkaline phosphatase from rat pregnant and pseudopregnant deciduae, fetal placentae, anestrus uteri and small intestine
Enzymologia
37
262-272
1969
Rattus norvegicus
Chandran Nair, B.; Majeska, R.J.; Rodan, G.A.
Rat alkaline phosphatase. I. Purification and characterization of the enzyme from osteosarcoma: generation of monoclonal and polyclonal antibodies
Arch. Biochem. Biophys.
254
18-27
1987
Rattus norvegicus
Yedlin, S.T.; Young, G.P.; Seetharam, B.; Seetharam, S.; Alpers, D.H.
Characterization and comparison of soluble and membranous forms of intestinal alkaline phosphatase from the suckling rat
J. Biol. Chem.
256
5620-5626
1981
Rattus norvegicus
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
Malik, N.; Butterworth, P.J.
Molecular properties of rat intestinal alkaline phosphatase
Biochim. Biophys. Acta
446
105-114
1976
Rattus norvegicus
Say, J.C.; Ciuffi, K.; Furriel, R.P.M.; Ciancaglini, P.; Leone, F.A.
Alkaline phosphatase from rat osseous plates: purification and biochemical characterization of a soluble form
Biochim. Biophys. Acta
1074
256-262
1991
Rattus norvegicus
Fernandes, S.S.; Furriel, R.P.M.; Petenusci, S.O.; Leone, F.A.
Streptozotocin-induced diabetes: significant changes in the kinetic properties of the soluble form of rat bone alkaline phosphatase
Biochem. Pharmacol.
58
841-849
1999
Rattus norvegicus
Feldbush, T.L.; Lafrenz, D.
Alkaline phosphatase on activated B cells characterization of the expression of alkaline phosphatase on activated B cells
J. Immunol.
147
3690-3695
1991
Rattus norvegicus
Wada, H.; Yagami, I.; Niwa, N.; Hayakawa, T.; Tsuge, H.
Distribution and properties of rat intestinal alkaline phosphatase isoenzymes
Exp. Anim.
50
153-158
2001
Rattus norvegicus
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
Vaisman, D.N.; McCarthy, A.D.; Cortizo, A.M.
Bone-specific alkaline phosphatase activity is inhibited by bisphosphonates: role of divalent cations
Biol. Trace Elem. Res.
104
131-140
2005
Rattus norvegicus
Harada, T.; Koyama, I.; Matsunaga, T.; Kikuno, A.; Kasahara, T.; Hassimoto, M.; Alpers, D.H.; Komoda, T.
Characterization of structural and catalytic differences in rat intestinal alkaline phosphatase isozymes
FEBS J.
272
2477-2486
2005
Rattus norvegicus
Akiba, Y.; Mizumori, M.; Guth, P.H.; Engel, E.; Kaunitz, J.D.
Duodenal brush border intestinal alkaline phosphatase activity affects bicarbonate secretion in rats
Am. J. Physiol. Gastrointest. Liver Physiol.
293
G1223-G1233
2007
Rattus norvegicus
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
Lee, M.W.; Muramatsu, T.; Uekusa, T.; Lee, J.H.; Shimono, M.
Heat stress induces alkaline phosphatase activity and heat shock protein 25 expression in cultured pulp cells
Int. Endod. J.
41
158-162
2008
Rattus norvegicus
Sogabe, N.; Maruyama, R.; Hosori, T.; Goseki-Sone, M.
Enhancement effects of vitamin K1 (phylloquinone) or vitamin K2 (menaquinone-4) on intestinal alkaline phosphatase activity in rats
J. Nutr. Sci. Vitaminol.
53
219-224
2007
Rattus norvegicus
Chida, K.; Taguchi, M.
Change in localization of alkaline phosphatase and mannosidase II by colchicine treatment of primary cultures of fetal rat hepatocytes
Acta Histochem. Cytochem.
41
1-5
2008
Rattus norvegicus
Taguchi, M.; Chida, K.
Effects of Colchicine on Localization of Alkaline Phosphatase in McA-RH 7777 Rat Hepatoma Cells
Acta Histochem. Cytochem.
41
149-155
2008
Rattus norvegicus
Dziedziejko, V.; Safranow, K.; Slowik-Zylka, D.; Machoy-Mokrzynska, A.; Millo, B.; Machoy, Z.; Chlubek, D.
Characterisation of rat and human tissue alkaline phosphatase isoforms by high-performance liquid chromatography and agarose gel electrophoresis
Biochimie
91
445-452
2009
Rattus norvegicus, Rattus norvegicus (P08289)
Mota, A.; Silva, P.; Neves, D.; Lemos, C.; Calhau, C.; Torres, D.; Martel, F.; Fraga, H.; Ribeiro, L.; Alcada, M.N.; Pinho, M.J.; Negrao, M.R.; Pedrosa, R.; Guerreiro, S.; Guimaraes, J.T.; Azevedo, I.; Martins, M.J.
Characterization of rat heart alkaline phosphatase isoenzymes and modulation of activity
Braz. J. Med. Biol. Res.
41
600-609
2008
Rattus norvegicus
Lomashvili, K.A.; Garg, P.; Narisawa, S.; Millan, J.L.; ONeill, W.C.
Upregulation of alkaline phosphatase and pyrophosphate hydrolysis: potential mechanism for uremic vascular calcification
Kidney Int.
73
1024-1030
2008
Mus musculus, Rattus norvegicus
Mirhashemi, S.; Moshtaghie, A.; Ani, M.; Aarabi, M.
In vivo and in vitro studies of kinetic changes of serum, liver and brain high and low molecular weight alkaline phosphatase following aluminium exposure in rat
Asian J. Biochem.
5
1-11
2010
Rattus norvegicus
-
Trevino, S.; Andrade-Garcia, A.; Herrera Camacho, I.; Leon-Chavez, B.; Aguilar-Alonso, P.; Flores, G.; Brambila, E.
Chronic cadmium exposure lead to inhibition of serum and hepatic alkaline phosphatase activity in Wistar rats
J. Biochem. Mol. Toxicol.
29
587-594
2015
Rattus norvegicus
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