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EC Tree
The taxonomic range for the selected organisms is: Sus scrofa 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
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acid monophosphatase
-
-
-
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acid nucleoside diphosphate phosphatase
-
-
-
-
Acid phosphatase PII
-
-
-
-
acid phosphohydrolase
-
-
-
-
acid phosphomoesterase
-
-
-
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acid phosphomonoester hydrolase
-
-
-
-
Adipocyte acid phosphatase, isozyme alpha
-
-
-
-
Adipocyte acid phosphatase, isozyme beta
-
-
-
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glycerophosphatase
-
-
-
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Low molecular weight phosphotyrosine protein phosphatase
-
-
-
-
Minor phosphate-irrepressible acid phosphatase
-
-
-
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pH 2.5 acid phosphatase
-
-
-
-
pH 6-optimum acid phosphatase
-
-
-
-
phosphomonoesterase
-
-
-
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purple acid phosphatase
-
-
Stationary-phase survival protein surE
-
-
-
-
Tartrate-resistant acid ATPase
-
-
-
-
tartrate-resistant acid phosphatase
-
-
PAP
-
-
-
-
uteroferrin
-
-
-
-
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phosphate-monoester phosphohydrolase (acid optimum)
Wide specificity. Also catalyses transphosphorylations.
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4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
EEY(P)AA + H2O
EEYAA + phosphate
-
-
-
?
Fmoc-AAY(P)AA + H2O
Fmoc-AAYAA + phosphate
-
-
-
?
Fmoc-EEY(P)AA + H2O
Fmoc-EEYAA + phosphate
-
-
-
?
Fmoc-EY(P)A + H2O
Fmoc-EYA + phosphate
-
-
-
?
Fmoc-KKAY(P)AA + H2O
Fmoc-KKAYAA + phosphate
-
-
-
?
Fmoc-KKY(P)AA + H2O
Fmoc-KKYAA + phosphate
-
-
-
?
phospho-L-tyrosine + H2O
L-tyrosine + phosphate
-
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
methyl-p-nitrophenyl phosphate + H2O
p-nitrophenol + methyl phosphate
-
-
-
-
?
methylphosphate + H2O
methanol + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
[(decyloxy)(naphthalen-1-yl)methyl]phosphonic acid + H2O
?
-
-
-
-
?
[(hexyloxy)(naphthalen-1-yl)methyl]phosphonic acid + H2O
?
-
-
-
-
?
[naphthalen-1-yl(octyloxy)methyl]phosphonic acid + H2O
?
-
-
-
-
?
additional information
?
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additional information
?
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substrate specificity
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-
?
additional information
?
-
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the enzyme is an iron-binding protein required for maternal/fetal iron transport
-
-
?
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additional information
?
-
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the enzyme is an iron-binding protein required for maternal/fetal iron transport
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-
?
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Fe2+
-
two iron ions per enzyme molecule
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4'-O-(2-fluoromalonyl)-L-tyrosine-containing peptides
inhibitory potency, overview
4'-O-(2-malonyl)-L-tyrosine-containing peptides
inhibitory potency, overview
phospho-L-tyrosine peptide analogues
inhibitory potency of several Fmoc-O,O-tert-butyl phospho-L-tyrosine analogue peptides, overview
1-benzyl-1H-1,2,3-triazole-4-carboxylic acid
-
-
1-[(2-chlorophenyl)methyl]-1H-1,2,3-triazole-4-carboxylic acid
-
-
1-[(4-chlorophenyl)methyl]-1H-1,2,3-triazole-4-carboxylic acid
-
-
1-[(4-methoxyphenyl)methyl]-1H-1,2,3-triazole-4-carboxylic acid
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-
1-[(4-methylphenyl)methyl]-1H-1,2,3-triazole-4-carboxylic acid
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-
1-[(naphthalen-1-yl)methyl]-1H-1,2,3-triazole-4-carboxylic acid
-
-
fluoride
-
competitive inhibitor independent of pH
Pepsin
-
partial cleavage results in enzyme inhibition
-
vanadate
-
non-competitive inhibitor at low pH and non-competitive inhibitor at higher pH
[(butanoylamino)(naphthalen-1-yl)methyl]phosphonic acid
-
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[(decanoylamino)(naphthalen-1-yl)methyl]phosphonic acid
-
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[(decyloxy)(naphthalen-1-yl)methyl]phosphonic acid
-
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[(dodecanoylamino)(naphthalen-1-yl)methyl]phosphonic acid
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[(heptanoylamino)(naphthalen-1-yl)methyl]phosphonic acid
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[(hexadecanoylamino)(naphthalen-1-yl)methyl]phosphonic acid
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[(hexyloxy)(naphthalen-1-yl)methyl]phosphonic acid
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[naphthalen-1-yl(octanoylamino)methyl]phosphonic acid
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[naphthalen-1-yl(octyloxy)methyl]phosphonic acid
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[naphthalen-1-yl(tetradecanoylamino)methyl]phosphonic acid
-
-
additional information
inhibitor-enzyme interaction
-
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Trypsin
-
partial cleavage results in 1.7fold enzyme activation
-
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0.12
Fmoc-AAY(P)AA
pH 4.9, 25°C
0.006 - 0.075
Fmoc-EEY(P)AA
0.008 - 0.048
Fmoc-EY(P)A
0.95
Fmoc-KKAY(P)AA
pH 4.9, 25°C
0.02
4-methylumbelliferyl phosphate
-
-
110
methyl-p-nitrophenyl phosphate
-
at pH 4.9
138
methylphosphate
-
at pH 4.9
1.25 - 7
p-nitrophenyl phosphate
0.02
[(decyloxy)(naphthalen-1-yl)methyl]phosphonic acid
-
pH 4.9
2.65
[(hexyloxy)(naphthalen-1-yl)methyl]phosphonic acid
-
pH 4.9
0.03
[naphthalen-1-yl(octyloxy)methyl]phosphonic acid
-
pH 4.9
additional information
additional information
kinetics
-
0.14
EEY(P)AA
pH 2.5, 25°C
0.31
EEY(P)AA
pH 4.9, 25°C
0.006
Fmoc-EEY(P)AA
pH 2.5, 25°C
0.075
Fmoc-EEY(P)AA
pH 4.9, 25°C
0.008
Fmoc-EY(P)A
pH 2.5, 25°C
0.048
Fmoc-EY(P)A
pH 4.9, 25°C
1.25
p-nitrophenyl phosphate
-
at pH 4.9
3.7
p-nitrophenyl phosphate
-
at pH 4.9
7
p-nitrophenyl phosphate
-
at pH 6.2
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100
Fmoc-AAY(P)AA
pH 4.9, 25°C
170
Fmoc-KKAY(P)AA
pH 4.9, 25°C
542
methyl-p-nitrophenyl phosphate
-
at pH 4.9
17
methylphosphate
-
at pH 4.9
470
p-nitrophenyl phosphate
-
at pH 4.9
65
EEY(P)AA
pH 2.5, 25°C
35
Fmoc-EEY(P)AA
pH 2.5, 25°C
120
Fmoc-EEY(P)AA
pH 4.9, 25°C
25
Fmoc-EY(P)A
pH 2.5, 25°C
31
Fmoc-EY(P)A
pH 4.9, 25°C
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0.023
1-benzyl-1H-1,2,3-triazole-4-carboxylic acid
-
at pH 4.9 and 25°C
0.276
1-[(2-chlorophenyl)methyl]-1H-1,2,3-triazole-4-carboxylic acid
-
at pH 4.9 and 25°C
0.013
1-[(4-chlorophenyl)methyl]-1H-1,2,3-triazole-4-carboxylic acid
-
at pH 4.9 and 25°C
0.048
1-[(4-methoxyphenyl)methyl]-1H-1,2,3-triazole-4-carboxylic acid
-
at pH 4.9 and 25°C
0.076
1-[(4-methylphenyl)methyl]-1H-1,2,3-triazole-4-carboxylic acid
-
at pH 4.9 and 25°C
0.184
1-[(naphthalen-1-yl)methyl]-1H-1,2,3-triazole-4-carboxylic acid
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at pH 4.9 and 25°C
5.99
fluoride
-
competitive inhibition at pH 6.2
4.1
phosphate
-
using methyl-p-nitrophenyl phosphate as a substrate, at pH 4.9
0.04
vanadate
-
at pH 5.5
0.363
[(butanoylamino)(naphthalen-1-yl)methyl]phosphonic acid
-
pH 4.9, competitive inhibition constant, temperature not specified in the publication
0.01
[(decanoylamino)(naphthalen-1-yl)methyl]phosphonic acid
-
pH 4.9, competitive inhibition constant, temperature not specified in the publication
0.021
[(dodecanoylamino)(naphthalen-1-yl)methyl]phosphonic acid
-
pH 4.9, competitive inhibition constant, temperature not specified in the publication
0.116
[(heptanoylamino)(naphthalen-1-yl)methyl]phosphonic acid
-
pH 4.9, competitive inhibition constant, temperature not specified in the publication
0.013
[(hexadecanoylamino)(naphthalen-1-yl)methyl]phosphonic acid
-
pH 4.9, competitive inhibition constant, temperature not specified in the publication
0.044
[naphthalen-1-yl(octanoylamino)methyl]phosphonic acid
-
pH 4.9, competitive inhibition constant, temperature not specified in the publication
0.008
[naphthalen-1-yl(tetradecanoylamino)methyl]phosphonic acid
-
pH 4.9, competitive inhibition constant, temperature not specified in the publication
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0.02
[(decyloxy)(naphthalen-1-yl)methyl]phosphonic acid
Sus scrofa
-
pH 4.9
0.43
[(hexyloxy)(naphthalen-1-yl)methyl]phosphonic acid
Sus scrofa
-
pH 4.9
0.03
[naphthalen-1-yl(octyloxy)methyl]phosphonic acid
Sus scrofa
-
pH 4.9
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1.5
-
recombinant enzyme in cell culture medium
233
-
purified recombinant enzyme
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3 - 3.5
highest catalytic efficiency
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Uniprot
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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-
-
brenda
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PPA5_PIG
340
0
38012
Swiss-Prot
Secretory Pathway (Reliability: 1 )
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67000
-
1 * 35000-37000 + 1 * 67000, SDS-PAGE
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dimer
-
1 * 35000-37000 + 1 * 67000, SDS-PAGE
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glycoprotein
-
recombinant enzyme
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CM-cellulose column chromatography and Sephadex S-300 gel filtration
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CM-cellulose resin chromatography and Sephadex G-75 gel filtration
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recombinant secreted enzyme 155fold from Sf9 insect cell culture expressing the enzyme by ion exchange, adsorption, and affinity chromatography, and gel filtration
-
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expression in Spodopetra frugiperda Sf9 cells using the baculovirus infection system, the recombinant enzyme is secreted from the cell culture
-
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Leake, D.S.; Heald, B.; Peters, T.J.
Properties and subcellular localization of acid phosphatase activity in cultured arterial smooth muscle cells
Eur. J. Biochem.
128
557-563
1982
Sus scrofa
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
Naseri, J.I.; Truong, N.T.; Horentrup, J.; Kuballa, P.; Vogel, A.; Rompel, A.; Spener, F.; Krebs, B.
Porcine purple acid phosphatase: heterologous expression, characterization, and proteolytic analysis
Arch. Biochem. Biophys.
432
25-36
2004
Sus scrofa
brenda
Cox, R.S.; Schenk, G.; Mitic, N.; Gahan, L.R.; Hengge, A.C.
Diesterase activity and substrate binding in purple acid phosphatases
J. Am. Chem. Soc.
129
9550-9551
2007
Phaseolus vulgaris, Sus scrofa
brenda
Elliott, T.W.; Mitic, N.; Gahan, L.R.; Guddat, L.W.; Schenk, G.
Inhibition studies of purple acid phosphatases: implications for the catalytic mechanism
J. Braz. Chem. Soc.
17
1558-1565
2006
Phaseolus vulgaris, Sus scrofa
-
brenda
McGeary, R.P.; Vella, P.; Mak, J.Y.; Guddat, L.W.; Schenk, G.
Inhibition of purple acid phosphatase with alpha-alkoxynaphthylmethylphosphonic acids
Bioorg. Med. Chem. Lett.
19
163-166
2009
Phaseolus vulgaris, Sus scrofa
brenda
Mohd-Pahmi, S.H.; Hussein, W.M.; Schenk, G.; McGeary, R.P.
Synthesis, modelling and kinetic assays of potent inhibitors of purple acid phosphatase
Bioorg. Med. Chem. Lett.
21
3092-3094
2011
Phaseolus vulgaris, Sus scrofa
brenda
Hussein, W.; Feder, D.; Schenk, G.; Guddat, L.; McGeary, R.
Synthesis and evaluation of novel purple acid phosphatase inhibitors
MedChemComm
10
61-71
2019
Phaseolus vulgaris, Sus scrofa
brenda