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Information on EC 3.1.3.2 - acid phosphatase and Organism(s) Phaseolus vulgaris and UniProt Accession P80366

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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:
Phaseolus vulgaris
UNIPROT: P80366
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Word Map
The taxonomic range for the selected organisms is: Phaseolus vulgaris
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
-
acid monophosphatase
-
-
-
-
acid nucleoside diphosphate phosphatase
-
-
-
-
Acid phosphatase PII
-
-
-
-
acid phosphohydrolase
-
-
-
-
acid phosphomoesterase
-
-
-
-
acid phosphomonoester hydrolase
-
-
-
-
ACP1
-
-
-
-
AcPase
-
-
-
-
Adipocyte acid phosphatase, isozyme alpha
-
-
-
-
Adipocyte acid phosphatase, isozyme beta
-
-
-
-
APase
-
-
-
-
APASE6
-
-
-
-
colorless acid phosphatase
-
glycerophosphatase
-
-
-
-
HPAP
-
-
-
-
kbPAP
O24319
-
KhACP
-
shows also chloroperoxidase activity
LAP
-
-
-
-
Low molecular weight phosphotyrosine protein phosphatase
-
-
-
-
Minor phosphate-irrepressible acid phosphatase
-
-
-
-
non-specific acid phosphatase
-
-
NSAP
-
-
-
-
P56
-
-
-
-
P60
-
-
-
-
pH 2.5 acid phosphatase
-
-
-
-
pH 6-optimum acid phosphatase
-
-
-
-
phosphomonoesterase
-
-
-
-
purple acid phosphatase
purple acid phosphatase PvPAP3
-
rkbPAP
Stationary-phase survival protein surE
-
-
-
-
Tartrate-resistant acid ATPase
-
-
-
-
tartrate-resistant acid phosphatase
-
-
TR-AP
-
-
-
-
TrATPase
-
-
-
-
uteroferrin
-
-
-
-
additional information
the colorless acid phosphatase is distinct from the purple acid phosphatase
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
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
(naphthalen-1-ylmethyl)phosphonic acid + H2O
?
show the reaction diagram
-
-
-
-
?
2-phosphoglycerate + H2O
glycerate + phosphate
show the reaction diagram
-
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
show the reaction diagram
-
32% activity compared to p-nitrophenyl phosphate
-
-
?
3-phosphoglycerate + H2O
glycerate + phosphate
show the reaction diagram
-
-
-
?
3-phosphoglycerate + H2O
glycerol + phosphate
show the reaction diagram
-
34% activity compared to p-nitrophenyl phosphate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
ADP + H2O
AMP + phosphate
show the reaction diagram
alpha-naphthyl phosphate + H2O
alpha-naphthol + phosphate
show the reaction diagram
alpha-naphthylphosphate + H2O
alpha-naphthol + phosphate
show the reaction diagram
-
32% activity compared to p-nitrophenyl phosphate
-
-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
ATP + H2O
ADP + phosphate
show the reaction diagram
beta-naphthyl phosphate + H2O
beta-naphthol + phosphate
show the reaction diagram
-
-
-
?
beta-naphthylphosphate + H2O
beta-naphthol + phosphate
show the reaction diagram
-
59% activity compared to p-nitrophenyl phosphate
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
diphosphate + H2O
2 phosphate
show the reaction diagram
-
65% activity compared to phosphoenolpyruvate
-
-
?
FMN + H2O
? + phosphate
show the reaction diagram
-
-
-
-
?
GTP + H2O
GDP + phosphate
show the reaction diagram
-
16% activity compared to phosphoenolpyruvate
-
-
?
methyl-p-nitrophenyl phosphate + H2O
p-nitrophenol + methyl phosphate
show the reaction diagram
-
-
-
-
?
methylphosphate + H2O
methanol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
phospho-L-serine + H2O
L-serine + phosphate
show the reaction diagram
low activity
-
-
?
phospho-L-threonine + H2O
L-threonine + phosphate
show the reaction diagram
-
-
-
?
phospho-L-tyrosine + H2O
L-tyrosine + phosphate
show the reaction diagram
phosphoenolpyruvate + H2O
pyruvate + phosphate
show the reaction diagram
phosphothreonine + H2O
threonine + phosphate
show the reaction diagram
-
42% activity compared to p-nitrophenyl phosphate
-
-
?
phosphotyrosine + H2O
tyrosine + phosphate
show the reaction diagram
-
63% activity compared to p-nitrophenyl phosphate
-
-
?
phytate + H2O
? + phosphate
show the reaction diagram
ribulose 1,5-bisphosphate + H2O
? + phosphate
show the reaction diagram
-
high activity
-
-
?
uridine 5'-phosphate + H2O
uridine + phosphate
show the reaction diagram
-
-
-
-
?
[(decyloxy)(naphthalen-1-yl)methyl]phosphonic acid + H2O
?
show the reaction diagram
-
-
-
-
?
[(hexyloxy)(naphthalen-1-yl)methyl]phosphonic acid + H2O
?
show the reaction diagram
-
-
-
-
?
[hydroxy(naphthalen-1-yl)methyl]phosphonic acid + H2O
?
show the reaction diagram
-
-
-
-
?
[naphthalen-1-yl(octyloxy)methyl]phosphonic acid + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe3+
Fe(III)Zn(II) center in the active site
Zn2+
Fe(III)Zn(II) center in the active site
Fe2+
O24319
native enzyme with an iron-zinc center is not activated upon reduction of the enzyme with ferrous ions and ascorbate, but the activity of recombinant enzyme is increased about 4fold
Fe3+
-
108% activity at 0.01 mM
Iron
O24319
native enzyme with an iron-zinc center is not activated upon reduction of the enzyme with ferrous ions and ascorbate, but the activity of recombinant enzyme is increased about 4fold
Mn2+
-
106% activity at 0.01 mM
Zinc
O24319
native enzyme with an iron-zinc center is not activated upon reduction of the enzyme with ferrous ions and ascorbate, but the activity of recombinant enzyme is increased about 4fold
Zn2+
-
101% activity at 0.01 mM
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
((4-methoxyphenyl)(octylsulfonamido)methyl)phosphonic acid
-
very weak inhibitor
(dodecylsulfonamido(4-methoxyphenyl)methyl)phosphonic acid
-
-
(hexadecylsulfonamido(4-methoxyphenyl)methyl)phosphonic acid
-
-
(hexylsulfonamido(4-methoxyphenyl)methyl)phosphonic acid
-
very weak inhibitor
(naphthalen-1-ylmethyl)phosphonic acid
-
-
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-methylphenyl)methyl]-1H-1,2,3-triazole-4-carboxylic acid
-
-
1-[(naphthalen-1-yl)methyl]-1H-1,2,3-triazole-4-carboxylic acid
-
-
4'-O-(2-fluoromalonyl)-L-tyrosine-containing peptides
-
inhibitory potency, overview
4'-O-(2-malonyl)-L-tyrosine-containing peptides
-
inhibitory potency, overview
Al3+
-
strong inhibition of leaf and root nodule isozymes
Co2+
-
inhibition of leaf and root nodule isozymes
Cu2+
-
strong inhibition of leaf and root nodule isozymes
Diethyl (hexadecylsulfonamido(4-methoxyphenyl)methyl)phosphonate
-
-
diethyl((4-methoxyphenyl)(octylsulfonamido)methyl)phosphonate
-
very weak inhibitor
diethyl(dodecylsulfonamido(4-methoxyphenyl)methyl)phosphonate
-
-
diethyl(hexadecylsulfonamido(4-methoxyphenyl)methyl)phosphonate
-
-
diethyl(hexylsulfonamido(4-methoxyphenyl)methyl)phosphonate
-
very weak inhibitor
fluoride
-
competitive inhibitor independent of pH
H2O2
O24319
native and recombinant enzyme
Hg2+
-
strong inhibition of leaf and root nodule isozymes
K+
-
slight inhibition of root nodule isozymes
L-Tartrate
-
-
Li+
-
inhibits isozyme alpha from leaf
Mo6+
-
13% residual activity at 0.1 mM
molybdate
NH4+
-
slight inhibition of root nodule isozymes
Pb2+
-
strong inhibition of leaf and root nodule isozymes
phosphate
-
-
phospho-L-tyrosine peptide analogues
-
inhibitory potency of several Fmoc-O,O-tert-butyl phospho-L-tyrosine analogue peptides, overview
vanadate
VO43-
-
5% residual activity at 0.01 mM
[(butanoylamino)(naphthalen-1-yl)methyl]phosphonic acid
-
-
[(decanoylamino)(naphthalen-1-yl)methyl]phosphonic acid
-
-
[(decyloxy)(naphthalen-1-yl)methyl]phosphonic acid
-
-
[(dodecanoylamino)(naphthalen-1-yl)methyl]phosphonic acid
-
-
[(heptanoylamino)(naphthalen-1-yl)methyl]phosphonic acid
-
-
[(hexadecanoylamino)(naphthalen-1-yl)methyl]phosphonic acid
-
-
[(hexyloxy)(naphthalen-1-yl)methyl]phosphonic acid
-
-
[hydroxy(naphthalen-1-yl)methyl]phosphonic acid
-
-
[naphthalen-1-yl(octanoylamino)methyl]phosphonic acid
-
-
[naphthalen-1-yl(octyloxy)methyl]phosphonic acid
-
-
[naphthalen-1-yl(tetradecanoylamino)methyl]phosphonic acid
-
-
additional information
-
inhibitor-enzyme interaction
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
-
104% activity at 0.1 mM
NaF
-
114% activity at 0.01 mM
Tartrate
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.78
(naphthalen-1-ylmethyl)phosphonic acid
-
pH 6.2
356
methyl-p-nitrophenyl phosphate
-
at pH 6.25
281
methylphosphate
-
at pH 6.25
0.56 - 5.9
p-nitrophenyl phosphate
3.1
[(decyloxy)(naphthalen-1-yl)methyl]phosphonic acid
-
pH 6.2
4.28
[(hexyloxy)(naphthalen-1-yl)methyl]phosphonic acid
-
pH 6.2
5.31
[hydroxy(naphthalen-1-yl)methyl]phosphonic acid
-
pH 6.2
3.41
[naphthalen-1-yl(octyloxy)methyl]phosphonic acid
-
pH 6.2
additional information
additional information
-
kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
542
methyl-p-nitrophenyl phosphate
-
at pH 6.25
20
methylphosphate
-
at pH 6.25
850
p-nitrophenyl phosphate
-
at pH 6.25
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.17
fluoride
at pH 4.9
0.095
(dodecylsulfonamido(4-methoxyphenyl)methyl)phosphonic acid
-
at pH 4.9 and 25°C
0.0011
(hexadecylsulfonamido(4-methoxyphenyl)methyl)phosphonic acid
-
at pH 4.9 and 25°C
0.963
1-benzyl-1H-1,2,3-triazole-4-carboxylic acid
-
at pH 4.9 and 25°C
0.438
1-[(2-chlorophenyl)methyl]-1H-1,2,3-triazole-4-carboxylic acid
-
at pH 4.9 and 25°C
1.073
1-[(4-chlorophenyl)methyl]-1H-1,2,3-triazole-4-carboxylic acid
-
at pH 4.9 and 25°C
0.951
1-[(4-methylphenyl)methyl]-1H-1,2,3-triazole-4-carboxylic acid
-
at pH 4.9 and 25°C
2.276
1-[(naphthalen-1-yl)methyl]-1H-1,2,3-triazole-4-carboxylic acid
-
at pH 4.9 and 25°C
0.202
diethyl(dodecylsulfonamido(4-methoxyphenyl)methyl)phosphonate
-
at pH 4.9 and 25°C
0.013
diethyl(hexadecylsulfonamido(4-methoxyphenyl)methyl)phosphonate
-
at pH 4.9 and 25°C
1.1
fluoride
-
competitive inhibition at pH 6.2
0.783
L-Tartrate
-
at pH 4.9 and 25°C
0.8 - 1.8
phosphate
0.0295
vanadate
-
competitive inhibition at pH 6.2
0.238
[(butanoylamino)(naphthalen-1-yl)methyl]phosphonic acid
-
pH 4.9, competitive inhibition constant, temperature not specified in the publication
0.057
[(decanoylamino)(naphthalen-1-yl)methyl]phosphonic acid
-
pH 4.9, competitive inhibition constant, temperature not specified in the publication
0.005
[(dodecanoylamino)(naphthalen-1-yl)methyl]phosphonic acid
-
pH 4.9, competitive inhibition constant, temperature not specified in the publication
0.222
[(heptanoylamino)(naphthalen-1-yl)methyl]phosphonic acid
-
pH 4.9, competitive inhibition constant, temperature not specified in the publication
0.031
[(hexadecanoylamino)(naphthalen-1-yl)methyl]phosphonic acid
-
pH 4.9, competitive inhibition constant, temperature not specified in the publication
0.195
[naphthalen-1-yl(octanoylamino)methyl]phosphonic acid
-
pH 4.9, competitive inhibition constant, temperature not specified in the publication
0.011
[naphthalen-1-yl(tetradecanoylamino)methyl]phosphonic acid
-
pH 4.9, competitive inhibition constant, temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.421
(dodecylsulfonamido(4-methoxyphenyl)methyl)phosphonic acid
Phaseolus vulgaris
-
at pH 4.9 and 25°C
0.013
(hexadecylsulfonamido(4-methoxyphenyl)methyl)phosphonic acid
Phaseolus vulgaris
-
at pH 4.9 and 25°C
7
(naphthalen-1-ylmethyl)phosphonic acid
Phaseolus vulgaris
-
value above 7
0.759
diethyl(dodecylsulfonamido(4-methoxyphenyl)methyl)phosphonate
Phaseolus vulgaris
-
at pH 4.9 and 25°C
0.092
diethyl(hexadecylsulfonamido(4-methoxyphenyl)methyl)phosphonate
Phaseolus vulgaris
-
at pH 4.9 and 25°C
3.315
L-Tartrate
Phaseolus vulgaris
-
at pH 4.9 and 25°C
0.008
[(decyloxy)(naphthalen-1-yl)methyl]phosphonic acid
Phaseolus vulgaris
-
pH 6.2
1
[(hexyloxy)(naphthalen-1-yl)methyl]phosphonic acid
Phaseolus vulgaris
-
pH 6.2
5
[hydroxy(naphthalen-1-yl)methyl]phosphonic acid
Phaseolus vulgaris
-
pH 6.2
0.1
[naphthalen-1-yl(octyloxy)methyl]phosphonic acid
Phaseolus vulgaris
-
pH 6.2
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.3
-
after 1fold purification, using p-nitrophenyl phosphate as a substrate
106.3
-
purified enzyme
265.8
O24319
-
32.2
-
after 25fold purification, using p-nitrophenyl phosphate as a substrate
383.3
purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 3.5
-
highest catalytic efficiency
6.1
O24319
native and recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
variety red kidney bean
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expression during elongation in germination
Manually annotated by BRENDA team
-
two isozymes beta and gamma
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PPAF_PHAVU
459
0
52857
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
116000
-
leaf isozyme alpha, gel filtration
120000
-
SDS-PAGE, recombinant enzyme
123000
-
isozyme gamma of root nodule, gel filtration
34000
41000
-
2 * 41000 + 1 * 34000, root nodule isozyme gamma enzyme, SDS-PAGE
45000
49000
-
1 * 51000 + 1 * 72000, leaf isozyme alpha, SDS-PAGE, 1 * 49000 + 1 * 72000, root nodule isozyme beta, SDS-PAGE
51000
-
1 * 51000 + 1 * 72000, leaf isozyme alpha, SDS-PAGE, 1 * 49000 + 1 * 72000, root nodule isozyme beta, SDS-PAGE
56000
72000
-
1 * 51000 + 1 * 72000, leaf isozyme alpha, SDS-PAGE, 1 * 49000 + 1 * 72000, root nodule isozyme beta, SDS-PAGE
96000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
monomer
1 * 34000, SDS-PAGE, gel filtration
trimer
-
2 * 41000 + 1 * 34000, root nodule isozyme gamma enzyme, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, co-crystallization of PAP in the presence of 50 mM NaF
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K301N
-
activity comparable to the wild type enzyme
N108S
-
inactive
N108S/N170S
-
inactive
N108S/N423S
-
inactive
N108SS/N170S/N423S
-
inactive
N170S
-
inactive
N170S/N423S
-
inactive
N423S
-
inactive
S110A
-
reduced activity
S110P
-
reduced activity
S110T
-
activity comparable to the wild type enzyme
T172A
-
inactive
T172S
-
activity comparable to the wild type enzyme
T425A
-
inactive
T425P
-
inactive
T425S
-
activity comparable to the wild type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 70
activity decreases by 80% at 70°C compared with 30°C after 30 min of incubation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
120.7fold from root nodules and leaves by ammonium sulfate fractionation, DEAE ion exchange chromatography, ultrafiltration, and gel filtration
-
852fold to homogeneity from embryonic axes by DEAE ion exchange and concanavalin A affinity chromatography
CM-cellulose column chromatography and Sephadex S-300 gel filtration
-
CM-cellulose resin chromatography and Sephadex S-300 gel filtration
-
from roots: ammonium sulfate precipitation, nondenaturing PAGE, ion-exchange chromatography
ProBond resin nickel affinity column chromatography
-
recombinant enzyme
O24319
to over 95% purity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris
-
expressed in Sf9 TriEx insect cells
-
expression in High Five insect cells
O24319
gene KeACP, DNA and amino acid sequence determination and analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
induced by phosphate starvation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vogel, A.; Borchers, T.; Marcus, K.; Meyer, H.E.; Krebs, B.; Spener, F.
Heterologous expression and characterization of recombinant purple acid phosphatase from red kidney bean
Arch. Biochem. Biophys.
401
164-172
2002
Phaseolus vulgaris (O24319), Phaseolus vulgaris
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
Yoneyama, T.; Shiozawa, M.; Nakamura, M.; Suzuki, T.; Sagane, Y.; Katoh, Y.; Watanabe, T.; Ohyama, T.
Characterization of a novel acid phosphatase from embryonic axes of kidney bean exhibiting vanadate-dependent chloroperoxidase activity
J. Biol. Chem.
279
37477-37484
2004
Phaseolus vulgaris (Q764C1), Phaseolus vulgaris
Manually annotated by BRENDA team
Tejera Garcia, N.A.; Olivera, M.; Iribarne, C.; Lluch, C.
Partial purification and characterization of a non-specific acid phosphatase in leaves and root nodules of Phaseolus vulgaris
Plant Physiol. Biochem.
42
585-591
2004
Phaseolus vulgaris
Manually annotated by BRENDA team
Olczak, M.; Olczak, T.
N-glycosylation sites of plant purple acid phosphatases important for protein expression and secretion in insect cells
Arch. Biochem. Biophys.
461
247-254
2007
Lupinus luteus, Phaseolus vulgaris
Manually annotated by BRENDA team
Schenk, G.; Elliott, T.W.; Leung, E.; Carrington, L.E.; Mitic, N.; Gahan, L.R.; Guddat, L.W.
Crystal structures of a purple acid phosphatase, representing different steps of this enzymes catalytic cycle
BMC Struct. Biol.
8
6
2008
Phaseolus vulgaris (P80366)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
Yoneyama, T.; Taira, M.; Suzuki, T.; Nakamura, M.; Niwa, K.; Watanabe, T.; Ohyama, T.
Expression and characterization of a recombinant unique acid phosphatase from kidney bean hypocotyl exhibiting chloroperoxidase activity in the yeast Pichia pastoris
Protein Expr. Purif.
53
31-39
2007
Phaseolus vulgaris
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Liang, C.; Tian, J.; Lam, H.M.; Lim, B.L.; Yan, X.; Liao, H.
Biochemical and molecular characterization of PvPAP3, a novel purple acid phosphatase isolated from common bean enhancing extracellular ATP utilization
Plant Physiol.
152
854-865
2010
Phaseolus vulgaris (D2D4J4)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Alimoradi, N.; Ashrafi-Kooshk, M.R.; Shahlaei, M.; Maghsoudi, S.; Adibi, H.; McGeary, R.P.; Khodarahmi, R.
Diethyl (alkylsulfonamido(4-methoxyphenyl)methyl)phosphonate/phosphonic acid derivatives act as acid phosphatase inhibitors synthesis accompanied by experimental and molecular modeling assessments
J. Enzyme Inhib. Med. Chem.
32
20-28
2017
Phaseolus vulgaris
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team