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Information on EC 3.1.3.2 - acid phosphatase and Organism(s) Homo sapiens and UniProt Accession P13686

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.2 acid phosphatase
IUBMB Comments
Wide specificity. Also catalyses transphosphorylations.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P13686
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
purple acid phosphatase
-
type 5 acid phosphatase
-
acid monophosphatase
-
-
-
-
acid nucleoside diphosphate phosphatase
-
-
-
-
acid phosphatase
Acid phosphatase PII
-
-
-
-
acid phosphohydrolase
-
-
-
-
acid phosphomoesterase
-
-
-
-
acid phosphomonoester hydrolase
-
-
-
-
acid phosphotyrosine phosphatase
-
-
ACP1
-
-
-
-
AcPase
-
-
-
-
Adipocyte acid phosphatase, isozyme alpha
-
-
-
-
Adipocyte acid phosphatase, isozyme beta
-
-
-
-
APase
-
-
-
-
APASE6
-
-
-
-
cPAcP
-
-
erythrocyte-specific acid phosphatase
-
ESAP, isozyme
glycerophosphatase
-
-
-
-
HPAP
-
-
-
-
human prostatic acid phosphatase
-
-
LAP
-
-
-
-
Low molecular weight phosphotyrosine protein phosphatase
-
-
-
-
LPA-phosphatase
-
-
Minor phosphate-irrepressible acid phosphatase
-
-
-
-
NSAP
-
-
-
-
P56
-
-
-
-
P60
-
-
-
-
pH 2.5 acid phosphatase
-
-
-
-
pH 6-optimum acid phosphatase
-
-
-
-
phosphomonoesterase
-
-
-
-
phosphotyrosine phosphatase
-
-
prostate acid phosphatase
-
prostatic acid phosphatase
purple acid phosphatase
-
-
serum tartrate-resistant acid phosphatase
-
-
Stationary-phase survival protein surE
-
-
-
-
Tartrate-resistant acid ATPase
-
-
-
-
tartrate-resistant acid phosphatase
TR-AP
-
-
-
-
TRACP 5a
-
-
TRACP 5b
-
-
TRACP5b
-
-
TRAP 5a
-
-
TRAP 5b
-
-
TrATPase
-
-
-
-
type 5 acid phosphatase
-
-
type-5 tartrate-resistant phosphatase
-
-
uteroferrin
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
phosphate-monoester phosphohydrolase (acid optimum)
Wide specificity. Also catalyses transphosphorylations.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-77-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-umbelliferyl phosphate + H2O
2-umbelliferol + phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
show the reaction diagram
2-glycerophosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
show the reaction diagram
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate
4-nitrophenol + 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
least efficient substrate
-
-
?
5'-GMP + H2O
guanosine + phosphate
show the reaction diagram
-
-
-
?
5'-IMP + H2O
inosine + phosphate
show the reaction diagram
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
AMP + H2O
adenosine + phosphate
show the reaction diagram
ATP + H2O
ADP + phosphate
show the reaction diagram
CDP + H2O
CMP + phosphate
show the reaction diagram
-
-
-
-
?
CTP + H2O
CDP + phosphate
show the reaction diagram
-
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
4% of the activity with p-nitrophenyl phosphate
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
GDP + H2O
GMP + phosphate
show the reaction diagram
-
-
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
show the reaction diagram
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
show the reaction diagram
GMP + H2O
guanosine + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
NADP+ + H2O
NAD+ + phosphate
show the reaction diagram
-
no activity
-
-
?
o-carboxyphenyl phosphoric acid + H2O
o-carboxyphenol + phosphate
show the reaction diagram
-
-
-
-
?
O-phospho-L-tyrosine + H2O
phosphate + L-tyrosine
show the reaction diagram
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
phenolphthalein diphosphate + H2O
phenolphthalein monophosphate + phosphate
show the reaction diagram
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
show the reaction diagram
-
-
-
-
?
phospho-L-tyrosine + H2O
L-tyrosine + phosphate
show the reaction diagram
-
-
-
-
?
phosphocholine + H2O
choline + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
show the reaction diagram
-
-
-
-
?
phosphopyruvate + H2O
pyruvate + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated-ErbB-2 + H2O
?
show the reaction diagram
-
cPAcP interacts with and dephosphorylates ErbB-2 primarily at Tyr1221/2 and hence blocks downstream signaling, leading to reduced cell growth
-
-
?
TDP + H2O
TMP + phosphate
show the reaction diagram
-
-
-
-
?
thymolphthalein monophosphate + H2O
thymolphthalein + phosphate
show the reaction diagram
-
-
-
-
?
TTP + H2O
TDP + phosphate
show the reaction diagram
-
-
-
-
?
UDP + H2O
UDP + phosphate
show the reaction diagram
-
-
-
-
?
UTP + 2 H2O
UMP + 2 phosphate
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
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
-
in seminal plasma mainly 16:0- or 18:0-lysophosphatidic acid
-
-
?
phospho-L-tyrosine + H2O
L-tyrosine + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated-ErbB-2 + H2O
?
show the reaction diagram
-
cPAcP interacts with and dephosphorylates ErbB-2 primarily at Tyr1221/2 and hence blocks downstream signaling, leading to reduced cell growth
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
the 22 iron ions bound at the active site are Fe2+ in the active enzyme state, and Fe3+ in the inactive state influencing the conformation of the repression loop, binding and structure overview
Fe3+
-
the enzyme possesses a mixed-valent di-iron center
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1R)-1-phenyl-N-[(S)-phenyl(phosphono)methyl]ethanaminium chloride
-
(1R)-N-[(S)-(4-methoxyphenyl)(phosphono)methyl]-1-phenylethanaminium chloride
-
(1S)-1-phenyl-N-[(R)-phenyl(phosphono)methyl]ethanaminium chloride
-
(1S)-N-[(R)-(4-methoxyphenyl)(phosphono)methyl]-1-phenylethanaminium chloride
-
(R)-N-benzyl(phenyl)phosphonomethanaminium chloride
-
(S)-N-benzyl(phenyl)phosphonomethanaminium chloride
-
1,2-dimethyl-3-hydroxypyrid-4-one
-
-
2,2'-dipyridyl
-
-
2-hydroyxy-5-nitrobenzyl bromide
-
-
2-mercaptoethanol
-
-
4'-O-(2-fluoromalonyl)-L-tyrosine-containing peptides
-
inhibitory potency, overview
4'-O-(2-malonyl)-L-tyrosine-containing peptides
-
inhibitory potency, overview
AlCl3
-
-
arsenate
-
-
ascorbate
-
-
Au3+
-
-
Benzylarsonic acid
-
-
Benzylphosphonic acid
-
-
Bromosuccinimide
-
-
Ca2+
-
isoenzyme PAP-II is inhibited, isoenzyme PAP-I is not inhibited
Cupric sulfate
-
-
cyanide
-
-
diisopropyl flurophosphate
-
-
Dithionite
-
-
dithiothreitol
-
-
DL-tartrate
-
-
Fe3+
-
-
Ferrous ammonium sulfate
-
-
Glutaraldehyde
-
-
H2O2
-
-
Hg2+
-
-
iodoacetamide
-
-
iodoacetate
-
-
La3+
-
isoenzyme PAP-II is inhibited, isoenzyme PAP-I is not inhibited
Ni2+
-
-
oxalate
-
-
p-mercuribenzoate
-
-
Pb2+
-
1 mM, complete inhibition of hydrolysis of p-nitrophenyl phosphate
phospho-L-tyrosine peptide analogues
-
inhibitory potency of several Fmoc-O,O-tert-butyl phospho-L-tyrosine analogue peptides, overview
plasmin
-
plasmin or serine protease inhibitors are able to protect against the inactivation of the prostatic acid phosphatase
-
salicylate
-
competitive inhibition of hydrolysis of p-nitrophenyl phosphate, no effect on hydrolysis of 3'-AMP
Sodium chloroaurate
-
-
Sodium dithionite
-
-
Tartrate
taurocholate
-
-
vanadate
Zn2+
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
6-ethylmercaptopurine
-
stimulates hydrolysis of p-nitrophenyl phosphate
ascorbic acid
-
activates, enhancement of the enzyme activity by reducing agents might be expressed via the reduction of Fe2+ at the metal center
citrate
-
slight activation
dithiothreitol
-
activates, enhancement of the enzyme activity by reducing agents might be expressed via the reduction of Fe2+ at the metal center
L-ascorbic acid
-
3fold activation of kcat
Trypsin
-
2fold activation of kcat by trypsin cleavage, 14fold activition combined with 2-mercaptoethanol addition
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.14
1-naphthyl phosphate
-
2.9 - 66.7
2-glycerophosphate
0.091
3'-AMP
-
-
0.284
4-methylumbelliferyl phosphate
-
-
1.9 - 35
4-nitrophenyl phosphate
0.333
ADP
-
-
0.092 - 0.909
Alpha-naphthyl phosphate
1 - 2
AMP
0.265
ATP
-
-
0.606
CDP
-
-
0.377
CTP
-
-
0.348
GDP
-
-
1.5 - 3.3
GMP
0.26
GTP
-
-
0.195
o-carboxyphenyl phosphoric acid
-
-
1.95
O-phospho-L-tyrosine
-
0.07 - 1
p-nitrophenyl phosphate
0.276
Phenolphthalein diphosphate
-
-
0.606
Phenyl phosphate
-
-
0.339
phosphoenolpyruvate
-
-
4.6
phosphoryl choline
-
urinary enzyme
3.3 - 10
phosphorylcholine
0.476
TDP
-
-
0.53 - 5
thymolphthalein monophosphate
0.299
TTP
-
-
0.615
UDP
-
-
0.714
UTP
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
248
3'-AMP
at pH 5.0 and 20°C
121
4-methylumbelliferyl phosphate
-
-
14.1 - 760
4-nitrophenyl phosphate
225
5'-AMP
at pH 5.0 and 20°C
244
5'-GMP
at pH 5.0 and 20°C
254
5'-IMP
at pH 5.0 and 20°C
73
ADP
-
-
53
Alpha-naphthyl phosphate
-
-
119
ATP
-
-
58
CDP
-
-
93
CTP
-
-
86
GDP
-
-
113
GTP
-
-
198
p-nitrophenyl phosphate
-
-
109
Phenolphthalein diphosphate
-
-
62
Phenyl phosphate
-
-
2
phosphoenolpyruvate
-
-
69
TDP
-
-
107
TTP
-
-
79
UDP
-
-
119
UTP
-
-
additional information
additional information
-
pH dependency of kcat of recombinant wild-type and mutant enzymes
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
775
3'-AMP
at pH 5.0 and 20°C
292
5'-AMP
at pH 5.0 and 20°C
580
5'-GMP
at pH 5.0 and 20°C
370
5'-IMP
at pH 5.0 and 20°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00121
(1R)-1-phenyl-N-[(S)-phenyl(phosphono)methyl]ethanaminium chloride
Homo sapiens
determined by O-phosphotyrosine enzyme assay
0.00107
(1R)-N-[(S)-(4-methoxyphenyl)(phosphono)methyl]-1-phenylethanaminium chloride
Homo sapiens
determined by O-phosphotyrosine enzyme assay
0.000026
(1S)-1-phenyl-N-[(R)-phenyl(phosphono)methyl]ethanaminium chloride
Homo sapiens
determined by O-phosphotyrosine enzyme assay
0.000018
(1S)-N-[(R)-(4-methoxyphenyl)(phosphono)methyl]-1-phenylethanaminium chloride
Homo sapiens
determined by O-phosphotyrosine enzyme assay
0.000005
(R)-N-benzyl(phenyl)phosphonomethanaminium chloride
Homo sapiens
determined by O-phosphotyrosine enzyme assay
0.000198
(S)-N-benzyl(phenyl)phosphonomethanaminium chloride
Homo sapiens
determined by O-phosphotyrosine enzyme assay
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
133.3
-
-
333
-
urinary enzyme
49
-
isoenzyme A
92.1
-
purified recombinant enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.8
-
recombinant mutant H92A
4.4
-
recombinant mutant H92N
4.8 - 5
-
hydrolysis of p-nitrophenyl phosphate in acetate buffer
5 - 5.5
-
MES buffer, recombinant enzyme
5.2 - 5.3
-
hydrolysis of p-nitrophenyl phosphate in citrate buffer
5.4 - 5.6
-
-
5.5 - 5.7
-
in sodium acetate buffer for all substrates
6
-
isoenzyme PAP-II
6 - 6.5
-
MES buffer, enzyme from placenta
6.2 - 6.4
-
pH optimum is shifted in presence of ascorbate or by trypsin cleavage
additional information
-
pH profile and influence of kinetics for recombinant wild-type and mutant enzymes
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 7
-
-
4 - 8
-
-
4.8 - 6.6
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
sinusoidal cells
Manually annotated by BRENDA team
-
capsular small arteries of the endothelium
Manually annotated by BRENDA team
-
interlobular
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
secreted into medium by infected insect cells
Manually annotated by BRENDA team
-
normal and mucolipidosis II fibroblasts
Manually annotated by BRENDA team
-
cortical capillaries, medulla, glomeruli, distribution
Manually annotated by BRENDA team
-
fetal osteoblastic cells hFOB1.19: TRAP activity and the reduced glutathione-dependent microenvironment are modulated during osteoblastic differentiation. During this phase, TRAP activity, as well as alkaline phosphatase and glutathione increases progressively up to the 21st day, decreasing thereafter
Manually annotated by BRENDA team
additional information
-
tissue distribution of enzyme activity, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
isozyme 5a
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
expression of wild type cPAcP by cDNA in cPAcP-null LNCaP C-81 cells results in decreased tyrosine phosphorylation of ErbB-2. Phosphorylation of p52Shc, proliferating cell nuclear antigen expression, and cell growth are decreased in these cells. Decreased cPAcP expression by short hairpin RNA in LNCaP C-33 cells is associated with elevated phosphorylation of ErbB-2. Its downstream p52Shc, ERK1/2, Akt, Src, STAT-3, and STAT-5 are activated, and cell proliferation, proliferating cell nuclear antigen, and cyclin D1 expression are increased
physiological function
-
in mice, intrathecal injection of human PAP reduces PIP2 levels in dorsal root ganglionss, inhibits thermosensation through TRPV1, and enduringly reduces thermal hyperalgesia and mechanical allodynia caused by inflammation, nerve injury, and pronociceptive receptor activation. This includes inhibitory effects on lysophosphatidic acid, purinergic (ATP), bradykinin, and protease-activated (thrombin) receptors
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PPA5_HUMAN
325
0
36599
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
120000
-
isoenzyme PAP-II, gel filtration
17000 - 18000
-
gel filtration
30000
34000
-
x * 34000, SDS-PAGE
35850
-
mass spectroscopy
36000
-
1 * 36000, SDS-PAGE
48000
-
2 * 48000, urinary enzyme, SDS-PAGE
50000
-
2 * 50000, SDS-PAGE
55000
89100
-
sucrose density gradient centrifugation
90000
-
gel filtration
93000
-
gel filtration
97000
-
urinary enzyme, sucrose density gradient ultracentrifugation
additional information
-
two peaks over a broad range
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
-
the high-molecular weight precursor polypeptide of 69000 Da is rapidly glycosylated and processed to a mature enzyme of 45000-53000 Da
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme expressed in Escherichia coli and Pichia pastoris, the enzyme is in its oxidized, inactive state with both iron ions at the active site are Fe3+, X-ray diffraction structure determination and analysis at 2.2 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H92A
-
site-directed mutagenesis, the mutation shifts the pH optimum, and eliminates the polar interactions of His92 with the active site and decreases the activity by 10fold at optimal pH
H92N
-
site-directed mutagenesis, the mutation shifts the pH optimum, and alters interactions of His92 with the active site and increases the activity by 3fold at optimal pH
N91A
-
site-directed mutagenesis
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 7
-
stable
134695
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
20 h, stable
50
-
90 min, 74% loss of activity
54
-
5 min, rapid loss of about 35% of activity
63
-
heat denaturation of isoenzyme Cf
66
-
heat denaturation of isoenzyme Cs
70
-
10 min, more than 95% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
loses more than 90% of activity in 3 M urea at 25°C, pH 7.0
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20 days, 60% loss of activity
-
-20°C, 50% glycerol, 15 months, stable
-
-25°C, pH 6.0, stable for years
-
4°C, 48 h, complete loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
acid phosphatase III
-
from seminal plasma by anion exchange chromatography and gel filtration
-
recombinant enzyme
-
recombinant enzyme 84fold from Sf9 insect cells by cation exchange chromatography and 2-step gel filtration
-
recombinant enzyme to over 95% purity
-
thiophilic absorption chromatography, preparative SDS-PAGE
-
TRAP 5a and 5b are highly purified from human blood and femur extracts, respectively, and after purifying the TRAPs by successive chromatography on a series of lectin affinity columns, the chromatographs obtained are used to estimate the composition of their sugar chain structure. TRAP 5a mainly contains a high-mannose-type sugar chain, while TRAP 5b has multi-antennary complex-type sugar chain. These results indicate that the differences between TRAP 5a and 5b consist not only of a difference in modification by sialic acid but differences in other sugar chain structures
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli and Pichia pastoris
expression in Sf9 insect cells
-
expression in Spodopetra frugiperda Sf9 cells using the baculovirus infection system
-
expression of TRACP in Spodopetra frugiperda Sf9 cells using the baculovirus infection system
-
gene structure and promoter organization
-
transfection of the human ACP 5 gene into CHO cells and cloning of a stable cell line (CHO/TRAP 8F5) that expresses high levels of TRACP activity both intracellularly and as a secreted product. Secreted recombinant TRACPs have all characteristics of natural serum TRACP 5a. The intracellular TRACPs have all the same characteristics of natiral serum TRACP 5b
-
type 5 acid phospahatase, expression in Sf9 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
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isozyme 5 a is a biomarker for chromic inflammatory disease e.g. rheumatoid arthritis
medicine
molecular biology
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TRAP activity is modulated during osteoblastic differentiation, possibly in response to the redox state of the cell
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lin, M.F.; Clinton, G.M.
Human prostatic acid phosphatase and its phosphotyrosol phosphatase activity
Adv. Protein Phosphatases
4
199-228
1987
Homo sapiens
-
Manually annotated by BRENDA team
Geier, C.; von Figura, K.; Pohlmann, R.
Structure of the human lysosomal acid phosphatase gene
Eur. J. Biochem.
183
611-616
1989
Homo sapiens
Manually annotated by BRENDA team
Hayman, A.R.; Warburton, M.J.; Pringle, J.A.S.; Coles, B.; Chambers, T.J.
Purification and characterization of a tartrate-resistant acid phosphatase from human osteoclastomas
Biochem. J.
261
601-609
1989
Homo sapiens
Manually annotated by BRENDA team
Shirai, Y.; Takenouchi, J.; Yamashita, S.; Wakabayashi, M.
Effects of some cations and of fructose on human prostatic acid phosphatase
Enzymologia
39
125-128
1970
Homo sapiens
Manually annotated by BRENDA team
Waheed, A.; van Etten, R.
Biosynthesis and processing of lysosomal acid phosphatase in cultured human cells
Arch. Biochem. Biophys.
243
274-283
1985
Homo sapiens
Manually annotated by BRENDA team
Ketcham, C.M.; Baumbach, G.A.; Bazer, F.W.; Roberts, R.M.
The type 5, acid phosphatase from spleen of humans with hairy cell leukemia. Purification, properties, immunological characterization, and comparison with porcine uteroferrin
J. Biol. Chem.
260
5768-5776
1985
Homo sapiens
Manually annotated by BRENDA team
Gieselmann, V.; Hasilik, A.; von Figura, K.
Tartrate-inhibitable acid phosphatase. Purification from placenta, characterization and subcellular distribution in fibroblasts
Hoppe-Seyler's Z. Physiol. Chem.
365
651-660
1984
Homo sapiens
Manually annotated by BRENDA team
Lin, M.F.; Lee, C.L.; Li, S.S.L.; Chu, T.M.
Purification and characterization of a new human prostatic acid phosphatase isoenzyme
Biochemistry
22
1055-1062
1983
Homo sapiens
Manually annotated by BRENDA team
Wang, C.C.; Touster, O.
Acid phosphatases of HeLa cells: properties and regulation of lysosomal activity by serum
Arch. Biochem. Biophys.
172
191-201
1976
Homo sapiens
Manually annotated by BRENDA team
Wojcieszyn, J.W.; Wang, M.C.; Lee, C.L.; Murphy, G.P.; Chu, T.M.
Purification and characterization of a human urinary acid phosphatase
J. Appl. Biochem.
1
223-234
1979
Homo sapiens
-
Manually annotated by BRENDA team
Saini, M.S.; van Etten, R.L.
A homogeneous isoenzyme of human liver acid phosphatase
Arch. Biochem. Biophys.
191
613-624
1978
Homo sapiens
Manually annotated by BRENDA team
Hollander, V.P.
Acid phosphatases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
4
449-498
1971
Bos taurus, Saccharomyces cerevisiae, Chaos carolinense, Drosophila melanogaster, Escherichia coli, Homo sapiens, Lupinus luteus, Staphylococcus aureus, Mus musculus, Neurospora crassa, Nicotiana tabacum, Rattus norvegicus, Saccharomyces mellis, Staphylococcus aureus PS 55
-
Manually annotated by BRENDA team
Belfield, A.; Ellis, G.; Goldberg, D.M.
Human prostatic acid phosphatase. Studies on the mechanism of catalysis and on the nature of inhibition by purines and pyrimidines
Enzymologia
42
91-106
1972
Homo sapiens
Manually annotated by BRENDA team
Dipietro, D.L.
Purification and properties of human placental acid phosphatase III
Biochim. Biophys. Acta
235
458-465
1971
Homo sapiens
Manually annotated by BRENDA team
Hayman, A.R.; Warburton, M.J.; Pringle, J.A.S.; Chambers, T.J.
Tartrate-resistant acid phosphatase: purification and characterization of the human osteaclastoma enzyme
Biochem. Soc. Trans.
16
895
1988
Homo sapiens
-
Manually annotated by BRENDA team
Hayman, A.R.; Cox, T.M.
Purple acid phosphatase of the human macrophage and osteoclast. Characterization, molecular properties, and crystallization of the recombinant di-iron-oxo protein secreted by baculovirus-infected insect cells
J. Biol. Chem.
269
1294-1300
1994
Homo sapiens
Manually annotated by BRENDA team
Kaija, H.; Jia, J.; Lindqvist, Y.; Andersson, G.; Vihko, P.
Tartrate-resistant bone acid phosphatase: large-scale production and purification of the recombinant enzyme, characterization, and crystallization
J. Bone Miner. Res.
14
424-430
1999
Homo sapiens
Manually annotated by BRENDA team
Ostrowski, W.S.; Kuciel, R.
Human prostatic acid phosphatase: selected properties and practical applications
Clin. Chim. Acta
226
121-129
1994
Homo sapiens
Manually annotated by BRENDA team
Dissing, J.; Svensmark, O.
Human red cell acid phosphatase: purification and properties of the A, B, and C isozymes
Biochim. Biophys. Acta
1041
232-242
1990
Homo sapiens
Manually annotated by BRENDA team
Waheed, A.; Van Etten, R.L.
Protection of prostatic acid phosphatase activity in human serum samples by plasmin inhibitors
Clin. Chim. Acta
320
127-131
2002
Homo sapiens
Manually annotated by BRENDA team
Janckila, A.J.; Parthasarathy, R.N.; Parthasarathy, L.K.; Seelan, R.S.; Yam, L.T.
Stable expression of human tartrate-resistant acid phosphatase isoforms by CHO cells
Clin. Chim. Acta
326
113-122
2002
Homo sapiens
Manually annotated by BRENDA team
Miyazaki, S.; Igarashi, M.; Nagata, A.; Komoda, T.
Characterizations of recombinant human tartrate-resistant acid phosphatase from osteosarcoma: comparison study between recombinant and placental proteins
Methods Find. Exp. Clin. Pharmacol.
23
433-439
2001
Homo sapiens
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Fagerlund, K.M.; Ylipahkala, H.; Tiitinen, S.L.; Janckila, A.J.; Hamilton, S.; Maentausta, O.; Vaananen, H.K.; Halleen, J.M.
Effects of proteolysis and reduction on phosphatase and ROS-generating activity of human tartrate-resistant acid phosphatase
Arch. Biochem. Biophys.
449
1-7
2006
Homo sapiens
Manually annotated by BRENDA team
Funhoff, E.G.; Wang, Y.; Andersson, G.; Averill, B.A.
Substrate positioning by His92 is important in catalysis by purple acid phosphatase
FEBS J.
272
2968-2977
2005
Homo sapiens
Manually annotated by BRENDA team
Tanaka, M.; Kishi, Y.; Takanezawa, Y.; Kakehi, Y.; Aoki, J.; Arai, H.
Prostatic acid phosphatase degrades lysophosphatidic acid in seminal plasma
FEBS Lett.
571
197-204
2004
Homo sapiens
Manually annotated by BRENDA team
Janckila, A.J.; Parthasarathy, R.N.; Parthasarathy, L.K.; Seelan, R.S.; Hsueh, Y.C.; Rissanen, J.; Alatalo, S.L.; Halleen, J.M.; Yam, L.T.
Properties and expression of human tartrate-resistant acid phosphatase isoform 5a by monocyte-derived cells
J. Leukocyte Biol.
77
209-218
2005
Homo sapiens
Manually annotated by BRENDA team
Strater, N.; Jasper, B.; Scholte, M.; Krebs, B.; Duff, A.P.; Langley, D.B.; Han, R.; Averill, B.A.; Freeman, H.C.; Guss, J.M.
Crystal structures of recombinant human purple acid phosphatase with and without an inhibitory conformation of the repression loop
J. Mol. Biol.
351
233-246
2005
Homo sapiens (P13686)
Manually annotated by BRENDA team
Partanen, S.
Localisation of high acid phosphotyrosine phosphatase activity in afferent arterioles and glomeruli of human kidney
J. Mol. Histol.
36
225-233
2005
Homo sapiens
Manually annotated by BRENDA team
Garba, I.H.; Gatsing, D.; Ubom, G.
Elevated total and isoenzyme forms of acid phosphatase in falciparum malaria
C. R. Biol.
329
75-78
2006
Homo sapiens
Manually annotated by BRENDA team
Adams, L.M.; Warburton, M.J.; Hayman, A.R.
Human breast cancer cell lines and tissues express tartrate-resistant acid phosphatase (TRAP)
Cell Biol. Int.
31
191-195
2007
Homo sapiens
Manually annotated by BRENDA team
Flanagan, J.U.; Cassady, A.I.; Schenk, G.; Guddat, L.W.; Hume, D.A.
Identification and molecular modeling of a novel, plant-like, human purple acid phosphatase
Gene
377
12-20
2006
Homo sapiens (P13686)
Manually annotated by BRENDA team
Vovk, A.I.; Mischenko, I.M.; Tanchuk, V.Y.; Kachkovskii, G.A.; Sheiko, S.Y.; Kolodyazhnyi, O.I.; Kukhar, V.P.
Stereoselectivity of binding of alpha-(N-benzylamino)benzylphosphonic acids to prostatic acid phosphatase
Bioorg. Med. Chem. Lett.
18
4620-4623
2008
Homo sapiens (P15309), Homo sapiens
Manually annotated by BRENDA team
Kawaguchi, T.; Nakano, T.; Sasagawa, K.; Ohashi, T.; Miura, T.; Komoda, T.
Tartrate-resistant acid phosphatase 5a and 5b contain distinct sugar moieties
Clin. Biochem.
41
1245-1249
2008
Homo sapiens
Manually annotated by BRENDA team
Yamada, S.; Inaba, M.; Kurajoh, M.; Shidara, K.; Imanishi, Y.; Ishimura, E.; Nishizawa, Y.
Utility of serum tartrate-resistant acid phosphatase (TRACP5b) as a bone resorption marker in patients with chronic kidney disease: independence from renal dysfunction
Clin. Endocrinol. (Oxf.)
69
189-196
2008
Homo sapiens
Manually annotated by BRENDA team
Sharma, S.; Rauk, A.; Juffer, A.H.
A DFT study on the formation of a phosphohistidine intermediate in prostatic acid phosphatase
J. Am. Chem. Soc.
130
9708-9716
2008
Homo sapiens (P15309)
Manually annotated by BRENDA team
de Souza Malaspina, T.S.; dos Santos, C.X.; Campanelli, A.P.; Laurindo, F.R.; Sogayar, M.C.; Granjeiro, J.M.
Tartrate-resistant acid phosphatase activity and glutathione levels are modulated during hFOB 1.19 osteoblastic differentiation
J. Mol. Histol.
39
627-634
2008
Homo sapiens
Manually annotated by BRENDA team
White, K.Y.; Rodemich, L.; Nyalwidhe, J.O.; Comunale, M.A.; Clements, M.A.; Lance, R.S.; Schellhammer, P.F.; Mehta, A.S.; Semmes, O.J.; Drake, R.R.
Glycomic characterization of prostate-specific antigen and prostatic acid phosphatase in prostate cancer and benign disease seminal plasma fluids
J. Proteome Res.
8
620-630
2009
Homo sapiens
Manually annotated by BRENDA team
Chuang, T.D.; Chen, S.J.; Lin, F.F.; Veeramani, S.; Kumar, S.; Batra, S.K.; Tu, Y.; Lin, M.F.
Human prostatic acid phosphatase, an authentic tyrosine phosphatase, dephosphorylates ErbB-2 and regulates prostate cancer cell growth
J. Biol. Chem.
285
23598-23606
2010
Homo sapiens
Manually annotated by BRENDA team
Sowa, N.A.; Street, S.E.; Vihko, P.; Zylka, M.J.
Prostatic acid phosphatase reduces thermal sensitivity and chronic pain sensitization by depleting phosphatidylinositol 4,5-bisphosphate
J. Neurosci.
30
10282-10293
2010
Homo sapiens
Manually annotated by BRENDA team
Luchter-Wasylewska, E.; Grny, M.; Usachova, T.; Usachov, V.
Homotropic allostery of nucleotidase activity of human prostatic acid phosphatase
J. Mol. Catal. B
128
73-77
2016
Homo sapiens (P15309)
-
Manually annotated by BRENDA team