Any feedback?
Information on EC 3.1.3.2 - acid phosphatase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9SFU3
for references in articles please use BRENDA:EC3.1.3.2Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.1.3.2 acid phosphataseIUBMB Comments
Wide specificity. Also catalyses transphosphorylations.
Specify your search results
Word Map
- 3.1.3.2
- osteoclast
- lysosomal
- resorption
- marrow
-
cytochemical
- rankl
-
osteoclastogenesis
- cathepsin
-
multinucleated
- collagen
- osteoporosis
- granule
- beta-glucuronidase
- osteocalcin
- lymphocyte
- monocyte
-
prostate-specific
- osteoprotegerin
-
histochemistry
- periodontal
- metastases
- phosphorus
- phagocytic
- alveolar
-
trabecular
-
seminal
-
rankl-induced
- parathyroid
-
ovariectomized
- tibia
- femur
-
cytochemistry
-
lumbar
- osteolysis
- nfatc1
-
resorb
- tooth
- calcitonin
- m-csf
-
dentin
- calvaria
-
bone-specific
-
orthodontic
-
telopeptide
-
postmenopausal
-
histomorphometric
-
micro-ct
-
micro-computed
- medicine
- synthesis
- molecular biology
- phytase
- diagnostics
-
n-acetyl-beta-d-glucosaminidase
- biotechnology
- agriculture
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid monophosphatase
-
-
-
-
acid nucleoside diphosphate phosphatase
-
-
-
-
acid 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
-
-
-
-
glycerophosphatase
-
-
-
-
HPAP
-
-
-
-
LAP
-
-
-
-
Low molecular weight phosphotyrosine protein phosphatase
-
-
-
-
Minor phosphate-irrepressible acid phosphatase
-
-
-
-
NSAP
-
-
-
-
P56
-
-
-
-
P60
-
-
-
-
PAP
-
-
-
-
pH 2.5 acid phosphatase
-
-
-
-
pH 6-optimum acid phosphatase
-
-
-
-
phosphomonoesterase
-
-
-
-
purple acid phosphatase
Stationary-phase survival protein surE
-
-
-
-
Tartrate-resistant acid ATPase
-
-
-
-
TR-AP
-
-
-
-
TrATPase
-
-
-
-
uteroferrin
-
-
-
-
APase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
SYSTEMATIC NAME
IUBMB Comments
phosphate-monoester phosphohydrolase (acid optimum)
Wide specificity. Also catalyses transphosphorylations.
CAS REGISTRY NUMBER
COMMENTARY
9001-77-8
-
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
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
further substrates: 3-phosphoglyceric acid, ADP, dGTP, glucose 3-phosphate, dTTP, dCTP, dATP, O-phospho-Tyr, O-phospho-Ser, glucose 6-phosphate, CMP, O-phospho-Thr, ribose 5-phosphate, ATP, fructose 6-phosphate, AMP, GMP
-
-
?
1-oleoyl lysophosphatidic acid + H2O
1-oleoyl glycerol + phosphate
-
further substrates: lauroyl-, myristoyl-, palmitoyl- and stearoyl lysophosphatidic acid
-
-
?
5-bromo-4-chloro-3-indolyl phosphate + H2O
5-bromo-4-chloro-3-hydroxyindole + phosphate
-
-
-
-
?
6,8 difluoro-4-methylumbelliferyl phosphate + H2O
6,8 difluoro-4-methylumbelliferol + phosphate
-
-
-
?
Ac-RK(pS)AGKPKN + H2O
?
synthetic phosphorylated oligopeptide
-
-
?
ADP + H2O
?
-
58% of the activity with 4-nitrophenyl phosphate
-
?
ADP + H2O
? + phosphate
50% of the activity with 4-nitrophenylphosphate
-
-
?
AMP + H2O
adenosine + phosphate
9% activity compared to phosphoenolpyruvate
-
-
?
ATP + H2O
?
-
68% of the activity with 4-nitrophenyl phosphate
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
-
8.3% of the activity with 4-nitrophenyl phosphate
-
?
dAMP + H2O
2'-deoxyadenosine + phosphate
16% activity compared to phosphoenolpyruvate
-
-
?
dATP + H2O
? + phosphate
31% of the activity with 4-nitrophenylphosphate
-
-
?
dCTP + H2O
? + phosphate
35% of the activity with 4-nitrophenylphosphate
-
-
?
dGTP + H2O
? + phosphate
52% of the activity with 4-nitrophenylphosphate
-
-
?
dTTP + H2O
? + phosphate
37% of the activity with 4-nitrophenylphosphate
-
-
?
myo-inositol hexakisphosphate + H2O
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 1D-myo-inositol-1,2,5,6 tetrakisphosphate + phosphate
7% of the activity with 4-nitrophenylphosphate
-
-
?
NADP+ + H2O
NAD+ + phosphate
55% activity compared to phosphoenolpyruvate
-
-
?
O-phospho-L-tyrosine + H2O
L-tyrosine + phosphate
28% of the activity with 4-nitrophenylphosphate
-
-
?
phenylphosphate + H2O
phenol + phosphate
100% activity compared to phosphoenolpyruvate
-
-
?
phosphoenolpyruvate + H2O
?
-
83.5% of the activity with 4-nitrophenyl phosphate
-
?
phosphothreonine + H2O
threonine + phosphate
39% activity compared to phosphoenolpyruvate
-
-
?
phosphotyrosine + H2O
tyrosine + phosphate
51% activity compared to phosphoenolpyruvate
-
-
?
polyphosphate + H2O
?
-
72% of the activity with 4-nitrophenyl phosphate
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
relative activity: 43% compared to phosphoenolpyruvate as substrate
-
-
?
1-naphthyl phosphate + H2O
1-naphthol + phosphate
-
relative activity: 53% compared to phosphoenolpyruvate as substrate
-
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
relative activity: 116% compared to phosphoenolpyruvate as substrate
-
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
-
relative activity: 118% compared to phosphoenolpyruvate as substrate
-
-
?
3-phosphoglycerate + H2O
glycerate + phosphate
69% of the activity with 4-nitrophenylphosphate
-
-
?
3-phosphoglycerate + H2O
glycerate + phosphate
-
relative activity: 38% compared to phosphoenolpyruvate as substrate
-
-
?
3-phosphoglycerate + H2O
glycerate + phosphate
-
relative activity: 67% compared to phosphoenolpyruvate as substrate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
relative activity: 101% compared to phosphoenolpyruvate as substrate
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
relative activity: 83% compared to phosphoenolpyruvate as substrate
-
-
?
6-phospho-D-gluconate + H2O
gluconate + phosphate
-
relative activity: 67% compared to phosphoenolpyruvate as substrate
-
-
?
6-phospho-D-gluconate + H2O
gluconate + phosphate
-
relative activity: 69% compared to phosphoenolpyruvate as substrate
-
-
?
ADP + H2O
AMP + phosphate
-
relative activity: 68% compared to phosphoenolpyruvate as substrate
-
-
?
ADP + H2O
AMP + phosphate
-
relative activity: 77% compared to phosphoenolpyruvate as substrate
-
-
?
ATP + H2O
ADP + phosphate
17% activity compared to phosphoenolpyruvate
-
-
?
ATP + H2O
ADP + phosphate
-
relative activity: 52% compared to phosphoenolpyruvate as substrate
-
-
?
ATP + H2O
ADP + phosphate
-
relative activity: 81% compared to phosphoenolpyruvate as substrate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
17% of the activity with 4-nitrophenyl phosphate
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
19% activity compared to phosphoenolpyruvate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
46% activity compared to phosphoenolpyruvate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
20% of the activity with 4-nitrophenylphosphate
-
-
?
D-ribose 3-phosphate + H2O
D-ribose + phosphate
-
relative activity: 25% compared to phosphoenolpyruvate as substrate
-
-
?
D-ribose 3-phosphate + H2O
D-ribose + phosphate
-
relative activity: 41% compared to phosphoenolpyruvate as substrate
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
40% activity compared to phosphoenolpyruvate
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
relative activity: 50% compared to phosphoenolpyruvate as substrate
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
relative activity: 9% compared to phosphoenolpyruvate as substrate
-
-
?
dAMP + H2O
deoxyadenosine + phosphate
-
relative activity: 12% compared to phosphoenolpyruvate as substrate
-
-
?
dAMP + H2O
deoxyadenosine + phosphate
-
relative activity: 19% compared to phosphoenolpyruvate as substrate
-
-
?
diphosphate + H2O
2 phosphate
-
169% of the activity with 4-nitrophenyl phosphate
-
?
diphosphate + H2O
2 phosphate
86% activity compared to phosphoenolpyruvate
-
-
?
diphosphate + H2O
2 phosphate
95% of the activity with 4-nitrophenylphosphate
-
-
?
glycerol 3-phosphate + H2O
glycerol + phosphate
43% of the activity with 4-nitrophenylphosphate
-
-
?
glycerol 3-phosphate + H2O
glycerol + phosphate
-
relative activity: 44% compared to phosphoenolpyruvate as substrate
-
-
?
glycerol 3-phosphate + H2O
glycerol + phosphate
-
relative activity: 59% compared to phosphoenolpyruvate as substrate
-
-
?
GTP + H2O
GDP + phosphate
16% activity compared to phosphoenolpyruvate
-
-
?
GTP + H2O
GDP + phosphate
-
relative activity: 29% compared to phosphoenolpyruvate as substrate
-
-
?
GTP + H2O
GDP + phosphate
-
relative activity: 45% compared to phosphoenolpyruvate as substrate
-
-
?
L-phosphoserine + H2O
L-serine + phosphate
-
relative activity: 14% compared to phosphoenolpyruvate as substrate
-
-
?
L-phosphoserine + H2O
L-serine + phosphate
-
relative activity: 26% compared to phosphoenolpyruvate as substrate
-
-
?
L-phosphothreonine + H2O
L-threonine + phosphate
-
relative activity: 29% compared to phosphoenolpyruvate as substrate
-
-
?
L-phosphothreonine + H2O
L-threonine + phosphate
-
relative activity: 49% compared to phosphoenolpyruvate as substrate
-
-
?
Na diphosphate + H2O
?
-
relative activity: 41% compared to phosphoenolpyruvate as substrate
-
-
?
Na diphosphate + H2O
?
-
relative activity: 63% compared to phosphoenolpyruvate as substrate
-
-
?
O-phospho-L-serine + H2O
L-serine + phosphate
25% of the activity with 4-nitrophenylphosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
89% activity compared to phosphoenolpyruvate
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
relative activity: 96% compared to phosphoenolpyruvate as substrate
-
-
?
phenyl phosphate + H2O
phenol + phosphate
-
relative activity: 98% compared to phosphoenolpyruvate as substrate
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
100% activity
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
92% of the activity with 4-nitrophenylphosphate
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
-
relative activity: 100% compared to phosphoenolpyruvate as substrate
-
-
?
tyrosine phosphate + H2O
tyrosine + phosphate
-
relative activity: 60% compared to phosphoenolpyruvate as substrate
-
-
?
tyrosine phosphate + H2O
tyrosine + phosphate
-
relative activity: 71% compared to phosphoenolpyruvate as substrate
-
-
?
additional information
?
-
-
roots respond to the absence of an exogenous phosphate source with an increase in the specific activities of secreted acid phosphatases. The enzyme may have a role in mobilizing organic phosphate in the soil
-
?
additional information
?
-
no activity with phytic acid, phosphocholine, or bis-p-nitrophenyl phosphate (5 mM each)
-
-
?
NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
-
roots respond to the absence of an exogenous phosphate source with an increase in the specific activities of secreted acid phosphatases. The enzyme may have a role in mobilizing organic phosphate in the soil
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Fe
-
Fe and Zn show a molar ratio of 1:0.75. AtPAP10 contains a bimetal nucleus composed of Fe and Zn
Mg2+
Mn2+
Zn
-
Fe and Zn show a molar ratio of 1:0.75. AtPAP10 contains a bimetal nucleus composed of Fe and Zn
additional information
no effect on APase activity when the reaction mixture (lacking Mg2+) contains 5 mM KCl or 5 mM EDTA
Mg2+
preferred divalent cation activator, 90% increase of activity at 5 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
neither inhibitory nor stimulating: Mn2+, Mg2+, Ni2+, SO4-, and NO3-
-
additional information
neither inhibitory nor stimulating: Mn2+, Mg2+, Ni2+, SO4-, and NO3-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ethylene
-
under phosphate deficiency ethylene mainly enhances enzymatic activity of isoform PAP10 on the root surface, but not PAP10 transcription and protein accumulation. The effect of ethylene on the induction of root-associated PAP10 activity depends on sucrose, but the effect of sucrose does not depend on ethylene
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12.49
Ac-(pT)AILER
synthetic phosphorylated oligopeptide, pH 4, 37°C
16.57
Ac-(pT)IALGK
synthetic phosphorylated oligopeptide, pH 4, 37°C
13.88
Ac-RK(pS)AGKPKN
synthetic phosphorylated oligopeptide, pH 4, 37°C
12.56
KR(pT)IRR
synthetic phosphorylated oligopeptide, pH 4, 37°C
11.89
RRA(pT)VA
synthetic phosphorylated oligopeptide, pH 4, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
421
after 957fold purification, using phosphoenolpyruvate as a substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
strong expression in the early stages of seedling growth and pollen germination
-
AtPAP10 is predominantly associated with the root surface after secretion rather than being released into the rhizosphere
-
a decrease of local, external phosphate availability is sufficient to induce isoform PAP10 transcription in roots in the presence of sucrose, a systemic signal from shoots, whereas the magnitude of the induction is affected by the phosphate status of the whole plant. Once the PAP10 mRNAs are synthesized in roots, subsequent accumulation of PAP10 proteins in root cells and increase in PAP10 activity on the root surface are mainly controlled by local signalling. Under phosphate deficiency ethylene mainly modulates enzymatic activity of PAP10 on the root surface, but not PAP10 transcription and protein accumulation
strong expression in the early stages of seedling growth and pollen germination
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
a low acid phosphatase 3 mutant is identified and characterized from an Arabidopsis activation-tagged (Weigel) population. The roots of the lap3 plants show lower acid phosphatase activity compared to wild-type ones under low-Pi conditions
malfunction
-
analysis of atpap12 and atpap26 T-DNA mutants verifies that AtPAP12 and AtPAP26 account for most of the secreted acid phosphatase activity of phosphate-deficient wild-type seedlings
malfunction
-
functional analyses of multiple atpap10 mutant alleles and overexpressing lines show that AtPAP10 plays an important role in plant tolerance to phosphate limitation
malfunction
-
growth of Atpap10 mutants is reduced under phosphate limitation
physiological function
gene disruption mutants show a lower phytase and phophatase activity in seedlings and germinating pollen and lower pollen germination rate
physiological function
-
AtPAP26 is dual targeted during phosphate stress because it is also the principal intracellular (vacuolar) PAP up-regulated by phosphate-deficient Arabidopsis
physiological function
-
changes in the phosphatase enzymes might play an important role in the acclimation of Arabidopsis seeds to the changing environmental conditions
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PPA15_ARATH
532
0
60435
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
250000
-
oligomer structure, using in-gel assays (electrophoresis under non-reducing conditions)
55000
60000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
monomer
additional information
-
two proteins of 52000 Da and 63000 Da are detected by SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
differential glycosylation influences the subcellular targeting and substrate selectivity of AtPAP26
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
AtTLP18.3 proteins are crystallized by the hanging drop vapor diffusion method at 23°C. X-ray crystallography reveal the folding of AtTLP18.3 as a three-layer sandwich with 3 alpha-helices in the upper layer, 4 beta-sheets in the middle layer, and 2 alpha-helices in the lower layer, which resembles a Rossmann fold
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A385V
-
mutation in metallophosphatase domain results in complete loss of enzymatic activity
D167N
-
mutation in metallophosphatase domain results in complete loss of enzymatic activity
E340K
-
mutation in metallophosphatase domain results in complete loss of enzymatic activity
E363K
-
mutation in metallophosphatase domain results in complete loss of enzymatic activity
G169E
-
mutation in metallophosphatase domain results in complete loss of enzymatic activity
G195D
-
mutation in metallophosphatase domain results in complete loss of enzymatic activity
G27E
-
mutation not in metallophosphatase domain results in partial loss of enzymatic activity
G420R
-
mutation in metallophosphatase domain results in complete loss of enzymatic activity
G55D
-
mutation not metallophosphatase domain results in partial loss of enzymatic activity
G67R
-
mutation not metallophosphatase domain results in complete loss of enzymatic activity
P250L
-
mutation in metallophosphatase domain results in complete loss of enzymatic activity
R274K
-
mutation in metallophosphatase domain results in complete loss of enzymatic activity
R415K
-
mutation in metallophosphatase domain results in complete loss of enzymatic activity
R455K
-
mutation in metallophosphatase domain results in complete loss of enzymatic activity
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cation-exchange chromatography, Ni2+ affinity chromatography, gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged version expressed inNicotiana tabacum, GST-fusion protein (without any enzyme activity) expressed in Escherichia coli
expressed in Escherichia coli strain BL21 and Saccharomyces cerevisiae
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a decrease of local, external phosphate availability is sufficient to induce isoform PAP10 transcription in roots in the presence of sucrose, a systemic signal from shoots, whereas the magnitude of the induction is affected by the phosphate status of the whole plant. Once the PAP10 mRNAs are synthesized in roots, subsequent accumulation of PAP10 proteins in root cells and increase in PAP10 activity on the root surface are mainly controlled by local signalling
-
expression of AtPAP10 is specifically induced by phosphate limitation at both transcriptional and posttranscriptional levels
-
in the presence of 50 mM NaCl, acid phosphatase activity of salt-tolerant Arabidopsis thaliana ecotype Columbia is increased in the first 24 h
-
Northern blot analysis reveal AtTLP18.3 with a diurnally fluctuating expression pattern in wild-type plants. The transcripts show 2 high expression peaks, at 8 and 16 h after lights are 14 turned on
salt stress (50 mM NaCl) causes inhibition in acid phosphatase activity of salt-sensitive Arabidopsis thaliana ecotypes NOK2, N1438, and N1380
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Coello, P.
Purification and characterization of secreted acid phosphatase in phosphorus-deficient Arabidopsis thaliana
Physiol. Plant.
116
293-298
2002
Arabidopsis thaliana
-
Veljanovski, V.; Vanderbeld, B.; Knowles, V.L.; Snedden, W.A.; Plaxton, W.C.
Biochemical and molecular characterization of AtPAP26, a vacuolar purple acid phosphatase up-regulated in phosphate-deprived Arabidopsis suspension cells and seedlings
Plant Physiol.
142
1282-1293
2006
Arabidopsis thaliana (Q949Y3)
Zhang, W.; Gruszewski, H.A.; Chevone, B.I.; Nessler, C.L.
An Arabidopsis purple acid phosphatase with phytase activity increases foliar ascorbate
Plant Physiol.
146
431-440
2008
Arabidopsis thaliana
Siddique, S.; Endres, S.; Atkins, J.M.; Szakasits, D.; Wieczorek, K.; Hofmann, J.; Blaukopf, C.; Urwin, P.E.; Tenhaken, R.; Grundler, F.M.; Kreil, D.P.; Bohlmann, H.
Myo-inositol oxygenase genes are involved in the development of syncytia induced by Heterodera schachtii in Arabidopsis roots
New Phytol.
184
457-472
2009
Arabidopsis thaliana (O48840), Arabidopsis thaliana (Q6TPH1), Arabidopsis thaliana (Q9SFU3)
Reddy, V.S.; Rao, D.K.; Rajasekharan, R.
Functional characterization of lysophosphatidic acid phosphatase from Arabidopsis thaliana
Biochim. Biophys. Acta
1801
455-461
2010
Arabidopsis thaliana
Kuang, R.; Chan, K.H.; Yeung, E.; Lim, B.L.
Molecular and biochemical characterization of AtPAP15, a purple acid phosphatase with phytase activity, in Arabidopsis
Plant Physiol.
151
199-209
2009
Arabidopsis thaliana, Arabidopsis thaliana (Q9SFU3)
Jin, Y.; Won, S.; Jeon, H.; Park, S.; Kim, M.
Identification and molecular characterization of a low acid phosphatase 3 (lap3) mutant based on the screening of an Arabidopsis activation-tagged population
Plant Biotechnol. Rep.
5
45-51
2011
Arabidopsis thaliana
-
Tran, H.T.; Qian, W.; Hurley, B.A.; She, Y.M.; Wang, D.; Plaxton, W.C.
Biochemical and molecular characterization of AtPAP12 and AtPAP26: the predominant purple acid phosphatase isozymes secreted by phosphate-starved Arabidopsis thaliana
Plant Cell Environ.
33
1789-1803
2010
Arabidopsis thaliana
Wu, H.Y.; Liu, M.S.; Lin, T.P.; Cheng, Y.S.
Structural and functional assays of AtTLP18.3 identify its novel acid phosphatase activity in thylakoid lumen
Plant Physiol.
157
1015-1025
2011
Arabidopsis thaliana (Q9ZVL6)
Wang, L.; Li, Z.; Qian, W.; Guo, W.; Gao, X.; Huang, L.; Wang, H.; Zhu, H.; Wu, J.W.; Wang, D.; Liu, D.
Arabidopsis purple acid phosphatase AtPAP10 is predominantly associated with the root surface and plays an important role in plant tolerance to phosphate limitation
Plant Physiol.
157
1283-99
2011
Arabidopsis thaliana
Zhang, Y.; Wang, X.; Lu, S.; Liu, D.
A major root-associated acid phosphatase in Arabidopsis, AtPAP10, is regulated by both local and systemic signals under phosphate starvation
J. Exp. Bot.
65
6577-6588
2014
Arabidopsis thaliana
Nasri, N.; Maatallah, S.; Kaddour, R.; Lachaal, M.
Effect of salinity on Arabidopsis thaliana seed germination and acid phosphatase activity
Arch. Biol. Sci.
68
17-23
2016
Arabidopsis thaliana
-
EXTERNAL LINKS (specific for EC-Number 3.1.3.2)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
