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Information on EC 3.1.3.1 - alkaline phosphatase and Organism(s) Halobacterium salinarum and UniProt Accession B0R9W3
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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: Halobacterium salinarum
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
OE5192R
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
-
-
-
-
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
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
hydrolysis of 4-nitrophenylphosphate is nonlinear with time when the enzyme is microinjected into reversed micelles (of hexadecyltrimethylammoniumbromide in cyclohexane, with 1-butanol as cosurfactant) that contain substrate
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
-
the kinetic behaviour is determined by the ratio between concentration of Mn2+ and concentration of Na+ or K+. When the Mn2+ increases and Na+ or K+ decreases, the kinetics show cooperative behaviour
Mn2+
-
the kinetic behaviour is determined by the ratio between concentration of Mn2+ and concentration of Na+ or K+. When the Mn2+ increases and Na+ or K+ decreases, the kinetics show cooperative behaviour
Na+
-
the kinetic behaviour is determined by the ratio between concentration of Mn2+ and concentration of Na+ or K+. When the Mn2+ increases and Na+ or K+ decreases, the kinetics show cooperative behaviour
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Tris
dephosphorylation of substrate is doubled when the Tris concentration in the reaction buffer is increased from 20 mM to 500 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.7
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 384 mM NaCl, without Mn2+
4.9
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 680 mM NaCl, without Mn2+
8.6
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 680 mM NaCl, 2.5 mM Mn2+
9
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 384 mM K+, 2.5 mM MnCl2
9.7
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 680 mM K+, 2.5 mM MnCl2
11.6
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 384 mM NaCl, 2.5 mM Mn2+
13.9
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 192 mM NaCl, 2.5 mM Mn2+
14.4
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 680 mM NaCl, 5 mM Mn2+
16.7
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 192 mM NaCl, without Mn2+
16.8
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 680 mM NaCl, 8 mM Mn2+
25.4
4-nitrophenyl phosphate
-
pH 8.5, 40°C, enzyme in reversed micelles, 192 mM K+, 2.5 mM MnCl2
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
deletion of OE5192R produces a mutant strain with virtually no phosphatase activity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
mass spectrometric analysis of SDS-PAGE-separated protein
50000
mass spectrometric analysis of SDS-PAGE-separated protein
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
enzyme forms dimers composed of dominant beta-sheet structures sandwiched by alpha-helices. Active sites are well-accessible
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
diffracting crystals are grown using the hanging-drop vapor diffusion method. Crystallographic data are collected to a resolution of 1.7 A
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
stability impaired at pH 10.5. Highest stability at pH 7.5
715915
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is more stable in reversed micelles of hexadecyltrimethylammonium bromide in cyclohexane, with 1-butanol as co-surfactant than in bulk aqueous solution at 25°C. When the enzyme is dialysed against Mn2+-free buffer it loses all the activity within 90 min in aqueous medium, but it retains approximately 72% of the initial enzymatic activity for 90 min in reversed micelles
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wende, A.; Johansson, P.; Vollrath, R.; Dyall-Smith, M.; Oesterhelt, D.; Grininger, M.
Structural and biochemical characterization of a halophilic archaeal alkaline phosphatase
J. Mol. Biol.
400
52-62
2010
Halobacterium salinarum (B0R9W3), Halobacterium salinarum
Marhuenda-Egea, F.C.; Piera-Velaquez, S.; Cadenas, C.; Cadenas, E.
Mechanism of adaptation of an atypical alkaline p-nitrophenyl phosphatase from the archaeon Halobacterium salinarum at low-water environments
Biotechnol. Bioeng.
78
497-502
2002
Halobacterium salinarum, Halobacterium salinarum NRC 36014
Marhuenda-Egea, F.C.; Piera-Velazquez, S.; Cadenas, C.; Cadenas, E.
Kinetic regulation of an alkaline p-nitrophenylphosphate phosphatase from Halobacterium salinarum in low water system by Mn2+ and monovalent cations
FEMS Microbiol. Lett.
198
111-115
2001
Halobacterium salinarum, Halobacterium salinarum NRC 36014
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