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Information on EC 3.1.3.2 - acid phosphatase and Organism(s) Escherichia coli and UniProt Accession P0AE22
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3.1.3.2 acid phosphataseIUBMB Comments
Wide specificity. Also catalyses transphosphorylations.
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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: Escherichia coli
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 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
-
-
-
-
Stationary-phase survival protein surE
-
-
-
-
Tartrate-resistant acid ATPase
-
-
-
-
TR-AP
-
-
-
-
TrATPase
-
-
-
-
uteroferrin
-
-
-
-
additional information
additional information
the enzyme belongs to the class B bacterial phosphatases as part of the DDDD superfamily of phosphohydrolases
additional information
the enzyme belongs to the class B bacterial phosphatases as part of the DDDD superfamily of phosphohydrolases
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a phosphate monoester + H2O = an alcohol + phosphate
detailed structure-based catalytic mechanism
a phosphate monoester + H2O = an alcohol + phosphate
modelling of substrate binding in the active site
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
-
-
-
-
?
additional information
?
-
substrate specificity of AphA, overview
-
-
?
additional information
?
-
-
synthesis starts as soon as cultures enter the stationary phase, strong negative control by cAMP, starvation for inorganic phosphate results in a premature full induction
-
-
?
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
?
-
-
synthesis starts as soon as cultures enter the stationary phase, strong negative control by cAMP, starvation for inorganic phosphate results in a premature full induction
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Br-
I-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady-state kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant AphA in complex with adenosine and phosphate, with dCMP, or with osmate, sitting drop method, 0.002 ml protein solution containing 10 mg/ml protein in sodium acetate buffer, pH 7.0, mixed with 0.1 ml of precipitant solution containing 17-22% w/v PEG 6000, and 1 mM MgCl2, 20°C, equilibration against 2 ml of precipitant solution, soaking in ligand solution containing 50 mM sodium acetate, pH 7.0, 35% w/v PEG 6000, and 50 mM ligand for ligand complexing, derivatizing with Au and spermine, X-ray diffraction structure determination and analysis at 1.25-2.14 A resolution
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant AphA from strain DH5alpha
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene aphA, overexpression in strain DH5alpha
expression in Solanum tuberosum under control of sweet potato sporamin promoter
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
transgenic expression of phytase in Solanum tuberosum leads to stable expression levels over several cycles of propagation. Field tests show that tuber size, number and yield increase in transgenic potato. Improved phosphorus acquisition when phytate is provided as a sole phosphorus source and enhanced microtuber formation in cultured transgenic potato seedlings when phytate is provided as an additional phosphorus source are observed. The potato-produced phytase supplement is as effective as a commercially available microbial phytase in increasing the availability of phytate-phosphorus to weanling pigs
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Touati, E.; Danchin, A.
Cloning and characterization of the pH 2.5 acid phosphatase gene, appA: cyclic AMP mediated negative regulation
Mol. Gen. Genet.
208
499-505
1987
Escherichia coli
Dassa, E.; Cahu, M.; Desjoyaux-Cherel, B.; Boquet, P.L.
The acid phosphatase with optimum pH of 2.5 of Escherichia coli. Physiological and biochemical study
J. Biol. Chem.
257
6669-6676
1982
Escherichia coli
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
-
Hafkenscheid, J.C.M.
Properties of an acid phosphatase in Escherichia coli
Biochim. Biophys. Acta
167
582-589
1968
Escherichia coli
Passariello, C.; Forleo, C.; Micheli, V.; Schippa, S.; Leone, R.; Mangani, S.; Thaller, M.C.; Rossolini, G.M.
Biochemical characterization of the class B acid phosphatase (AphA) of Escherichia coli MG1655
Biochim. Biophys. Acta
1764
13-19
2006
Escherichia coli (P0AE22), Escherichia coli, Escherichia coli MG1655 (P0AE22)
Calderone, V.; Forleo, C.; Benvenuti, M.; Thaller, M.C.; Rossolini, G.M.; Mangani, S.
A structure-based proposal for the catalytic mechanism of the bacterial acid phosphatase AphA belonging to the DDDD superfamily of phosphohydrolases
J. Mol. Biol.
355
708-721
2006
Escherichia coli (P0AE22), Escherichia coli
Hong, Y.F.; Liu, C.Y.; Cheng, K.J.; Hour, A.L.; Chan, M.T.; Tseng, T.H.; Chen, K.Y.; Shaw, J.F.; Yu, S.M.
The sweet potato sporamin promoter confers high-level phytase expression and improves organic phosphorus acquisition and tuber yield of transgenic potato
Plant Mol. Biol.
67
347-361
2008
Escherichia coli
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