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EC Tree
The taxonomic range for the selected organisms is: Ipomoea batatas The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
acid phosphatase, tartrate-resistant acid phosphatase, prostatic acid phosphatase, tracp, acpase, uteroferrin, tracp 5b, phosphatidic acid phosphatase, tracp5b, pp2a phosphatase,
more
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purple acid phosphatase
-
acid monophosphatase
-
-
-
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acid nucleoside diphosphate phosphatase
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-
-
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Acid phosphatase PII
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-
-
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acid phosphohydrolase
-
-
-
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acid phosphomoesterase
-
-
-
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acid phosphomonoester hydrolase
-
-
-
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Adipocyte acid phosphatase, isozyme alpha
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-
-
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Adipocyte acid phosphatase, isozyme beta
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-
-
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glycerophosphatase
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-
-
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Low molecular weight phosphotyrosine protein phosphatase
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-
-
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Minor phosphate-irrepressible acid phosphatase
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-
-
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orthophosphoric monoester phosphohydrolase (acid optimum)
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pH 2.5 acid phosphatase
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-
-
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pH 6-optimum acid phosphatase
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-
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phosphomonoesterase
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-
-
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Stationary-phase survival protein surE
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-
-
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Tartrate-resistant acid ATPase
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-
-
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additional information
the enzyme belongs to the family of binuclear metalloenzymes
PAP
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-
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purple acid phosphatase
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purple acid phosphatase
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a phosphate monoester + H2O = an alcohol + phosphate
active site structure analysis, substrate binding, H295 and E365 are involved in substrate orientation and stabilization of the transition state, oxygen binding and bridging at the metal ion center, overview, reaction mechanism
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phosphate-monoester phosphohydrolase (acid optimum)
Wide specificity. Also catalyses transphosphorylations.
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2'-AMP + H2O
adenosine + phosphate
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6% of the activity with p-nitrophenyl phosphate
-
-
?
2-glycerophosphate + H2O
glycerol + phosphate
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69% of the activity with p-nitrophenyl phosphate
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
60% of the activity with p-nitrophenyl phosphate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
5'-ADP + H2O
AMP + phosphate
-
15% of the activity with p-nitrophenyl phosphate
-
-
?
5'-AMP + H2O
adenosine + phosphate
alpha-glycerophosphate + H2O
glycerol + phosphate
-
48% of the activity with p-nitrophenyl phosphate
-
-
?
AMP + H2O
adenosine + phosphate
ATP + H2O
ADP + phosphate
D-fructose 1,6-diphosphate + H2O
?
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69% of the activity with p-nitrophenyl phosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
D-glucose 6-phosphate + H2O
D-glucose + phosphate
-
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
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25% of the activity with p-nitrophenyl phosphate
-
-
?
D-sucrose 6-phosphate + H2O
D-sucrose + phosphate
-
-
-
?
diphosphate + H2O
2 phosphate
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93% of the activity with p-nitrophenyl phosphate
-
-
?
FMN + H2O
?
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35% of the activity with p-nitrophenyl phosphate
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
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33% of the activity with p-nitrophenyl phosphate
-
-
?
NADP+ + H2O
NAD+ + phosphate
O-phosphoserine + H2O
Ser + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
phenyl phosphate + H2O
phenol + phosphate
-
-
-
-
?
phospho-L-tyrosine + H2O
L-tyrosine + phosphate
-
-
-
-
?
phosphothreonine + H2O
Thr + phosphate
-
-
-
-
?
additional information
?
-
-
substrate specificity of the 6 cell wall isoenzymes: isoenzyme PI-III has the lowest specificity among the six isoenzymes
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
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3% of the activity with p-nitrophenyl phosphate
-
-
?
AMP + H2O
adenosine + phosphate
-
-
-
-
?
AMP + H2O
adenosine + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
38% of the activity with p-nitrophenyl phosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
29% of the activity with p-nitrophenyl phosphate
-
-
?
NADP+ + H2O
NAD+ + phosphate
-
-
-
-
?
NADP+ + H2O
NAD+ + phosphate
-
-
-
?
NADP+ + H2O
NAD+ + phosphate
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68% of the activity with p-nitrophenyl phosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
?
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Fe3+
phosphate forms an unusual tripodal complex with the Fe(III)-Mn(II) center, structure, oxygen binding and bridging at the metal ion center
Mn2+
strictly required, phosphate forms an unusual tripodal complex with the Fe(III)-Mn(II) center, structure, oxygen binding and bridging at the metal ion center
phosphate
forms an unusual tripodal complex with the Fe(III)-Mn(II) center, structure
Fe3+
-
can substitute Mn3+ in the native enzyme
Fe3+
isozyme 3 contains a diiron metal center in contrast to isozymes 1 and 2 which contain Fe(III)-Mn(II) centers, analysis of prosthetic metal ions/groups
Mn3+
-
Mn3+ may play an important role on effective binding of phosphate and acceleration of hydrolysis of phosphomonoesters at pH 4-6
Mn3+
-
enzyme contains one atom of Mn(III) per 110000 Da enzyme
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phosphate
competitive, moderate to weak bonding interactions to the enzyme
4'-O-(2-fluoromalonyl)-L-tyrosine-containing peptides
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inhibitory potency, overview
4'-O-(2-malonyl)-L-tyrosine-containing peptides
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inhibitory potency, overview
nitrilotriacetic acid
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phospho-L-tyrosine peptide analogues
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inhibitory potency of several Fmoc-O,O-tert-butyl phospho-L-tyrosine analogue peptides, overview
additional information
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inhibitor-enzyme interaction
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Cu2+
-
-
Zn2+
-
-
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L-ascorbic acid
activates
additional information
-
immobilization of the purified enzyme on glutaraldehyde-activated aminopropyl controlled-pore glass activates the enzyme
-
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0.049 - 0.71
p-nitrophenyl phosphate
additional information
additional information
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0.089
ATP
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isoenzyme PI-II
0.18
ATP
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isoenzyme PI-III
0.235
ATP
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isoenzyme PII-I and PIII-I
0.049
p-nitrophenyl phosphate
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pH 4.4, Mn(III)-acid phosphatase
0.077
p-nitrophenyl phosphate
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pH 4.4, Fe(III)-substituted acid phosphatase
0.5
p-nitrophenyl phosphate
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isoenzyme PI-II and PI-III
0.71
p-nitrophenyl phosphate
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isoenzyme PII and PIII-I
additional information
additional information
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kinetics
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additional information
additional information
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pH-dependence of Km-values of Mn(III)-acid phosphatase and Fe(III)substituted acid phosphatase with p-nitrophenyl phosphate
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171
D-fructose 6-phosphate
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pH 5.6
218
D-glucose 6-phosphate
-
pH 5.6
35
D-sucrose 6-phosphate
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pH 5.6
531
p-nitrophenyl phosphate
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pH 5.6
additional information
additional information
maximal turnover at neutral pH
-
45
AMP
-
pH 5.6
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0.028
phosphate
pH 7.0
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321.8
purified recombinant wild-type enzyme
545
purified recombinant wild-type enzyme in presence of L-ascorbic acid at 10 mM
additional information
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additional information
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additional information
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4.5
maximal catalytic efficiency
4.5 - 5.5
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isoenzyme PII-II
5 - 5.5
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isoenzyme PII-I
additional information
forms a micro-oxo-bridge at pH 4.9, maximal turnover at neutral pH
5.5
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-
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45 - 55
-
isoenzyme PI-II and PII-I
45 - 60
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isoenzyme PII-II
50 - 60
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isoenzyme PI-III and PIII-I
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cv. Golden
Uniprot
brenda
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-
purified enzyme
brenda
-
-
brenda
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-
6 isoenzymes
brenda
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PPAF1_IPOBA
473
0
53815
Swiss-Prot
Secretory Pathway (Reliability: 3 )
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250000
-
isoenzyme PI-III and PIII-I, gel filtration
320000
-
isoenzyme PI-I and PI-II, gel filtration
400000
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isoenzyme PII-I, gel filtration
60000
-
2 * 60000, SDS-PAGE
110000
-
gel filtration
110000
isozyme 3, gel filtration
55000
-
2 * 55000, SDS-PAGE
55000
2 * 55000, isozyme 3, SDS-PAGE
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dimer
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2 * 55000, SDS-PAGE
dimer
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2 * 60000, SDS-PAGE
dimer
2 * 55000, isozyme 3, SDS-PAGE
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purified enzyme, 22 mg/ml protein in 0.1 M acetate, pH 4.9, mixed with well solution containing 0.1 M citric acid, pH 3.5-4.0, 7.5% PEG 6000, 10% isopropanol, 50 mM phosphate, and 10% glycerol, 4°C, cryoprotection by increase of glycerol concentration to 20%, X-ray diffraction structure determination and analysis at 2.5 A resolution
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Y291A
site-directed mutagenesis of an substrate binding ssite residue to the correspondent residue of isozyme 1, the mutant shows decreased activity compared to the wild-type isozyme 3
Y291H
site-directed mutagenesis of an substrate binding ssite residue to the correspondent residue of isozyme 1, the mutant shows increased activity compared to the wild-type isozyme 3
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25 - 30
-
30 min, stable up to
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the cogelled enzyme is mechanically stable over a wide range of temperature
-
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recombinant isozyme 3 199fold from Sf9 insect cells in two steps by QBB-resin and hydrophobic interaction chromatography
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subcloning in Escherichia coli, expression of wild-type and mutant isozyme 3 in Spodoptera frugiperda Sf9 cells using the baculovirus infection system
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biotechnology
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immobilization of the purified enzyme on glutaraldehyde-activated aminopropyl controlled-pore glass activates the enzyme, assay automatization, system evaluation, overview
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Kawabe, H.; Sugiura, Y.; Terauchi, M.; Tanaka, H.
Mn(III)-containing acid phosphatase. Properties of Fe(III)-substituted enzyme and function of Mn(III) and Fe(III) in plant and mammalian acid phosphatases
Biochim. Biophys. Acta
784
81-89
1984
Ipomoea batatas
brenda
Sugiura, Y.; Kawabe, H.; Tanaka, H.; Fujimoto, S.; Ohara, A.
Purification, enzymatic properties, and active site environment of a novel manganese(III)-containing acid phosphatase
J. Biol. Chem.
256
10664-10670
1981
Ipomoea batatas
brenda
Sugawara, S.; Inamoto, Y.; Ushijima, M.
Resolution and some properties of acid phosphatase isoenzymes bound to the cell wall of potato tubers
Agric. Biol. Chem.
45
1767-1773
1981
Ipomoea batatas
-
brenda
Alfani, F.; Albanesi, D.; Cantarella, M.; Scardi, V.
Effects of temperature and shear on the activity of acid phosphatase in a tubular membrane reactor
Enzyme Microb. Technol.
4
181-184
1982
Ipomoea batatas
-
brenda
Kusudo, T.; Sakaki, T.; Inouye, K.
Purification and characterization of purple acid phosphatase PAP1 from dry powder of sweet potato
Biosci. Biotechnol. Biochem.
67
1609-1611
2003
Ipomoea batatas
brenda
Valizadeh, M.; Schenk, G.; Nash, K.; Oddie, G.W.; Guddat, L.W.; Hume, D.A.; de Jersey, J.; Burke, T.R.; Hamilton, S.
Phosphotyrosyl peptides and analogues as substrates and inhibitors of purple acid phosphatases
Arch. Biochem. Biophys.
424
154-162
2004
Homo sapiens, Ipomoea batatas, Mus musculus, Phaseolus vulgaris, Sus scrofa (P09889)
brenda
Yamato, S.; Kawakami, N.; Shimada, K.; Ono, M.; Idei, N.; Itoh, Y.; Tachikawa, E.
Sweet potato acid phosphatase immobilized on glutaraldehyde-activated aminopropyl controlled-pore glass: activation, repeated use and enzyme fatigue
Biol. Pharm. Bull.
27
210-215
2004
Ipomoea batatas
brenda
Waratrujiwong, T.; Krebs, B.; Spener, F.; Visoottiviseth, P.
Recombinant purple acid phosphatase isoform 3 from sweet potato is an enzyme with a diiron metal center
FEBS J.
273
1649-1659
2006
Ipomoea batatas (Q9ZS50)
brenda
Schenk, G.; Gahan, L.R.; Carrington, L.E.; Mitic, N.; Valizadeh, M.; Hamilton, S.E.; de Jersey, J.; Guddat, L.W.
Phosphate forms an unusual tripodal complex with the Fe-Mn center of sweet potato purple acid phosphatase
Proc. Natl. Acad. Sci. USA
102
273-278
2005
Ipomoea batatas (Q9SE00)
brenda