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Information on EC 3.1.3.2 - acid phosphatase and Organism(s) Ipomoea batatas and UniProt Accession Q9SE00
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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: Ipomoea batatas
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
-
-
-
-
purple acid phosphatase
Stationary-phase survival protein surE
-
-
-
-
Tartrate-resistant acid ATPase
-
-
-
-
TR-AP
-
-
-
-
TrATPase
-
-
-
-
uteroferrin
-
-
-
-
additional information
the enzyme belongs to the family of binuclear metalloenzymes
PAP
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a phosphate monoester + H2O = an alcohol + phosphate
active site structure analysis, substrate binding, H295 and E365 are involved in substrate orientation and stabilization of the transition state, oxygen binding and bridging at the metal ion center, overview, reaction mechanism
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
2'-AMP + H2O
adenosine + phosphate
-
6% of the activity with p-nitrophenyl phosphate
-
-
?
2-glycerophosphate + H2O
glycerol + phosphate
-
69% of the activity with p-nitrophenyl phosphate
-
-
?
3'-AMP + H2O
adenosine + phosphate
-
60% of the activity with p-nitrophenyl phosphate
-
-
?
5'-ADP + H2O
AMP + phosphate
-
15% of the activity with p-nitrophenyl phosphate
-
-
?
alpha-glycerophosphate + H2O
glycerol + phosphate
-
48% of the activity with p-nitrophenyl phosphate
-
-
?
D-fructose 1,6-diphosphate + H2O
?
-
69% of the activity with p-nitrophenyl phosphate
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
-
25% of the activity with p-nitrophenyl phosphate
-
-
?
diphosphate + H2O
2 phosphate
-
93% of the activity with p-nitrophenyl phosphate
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
-
33% of the activity with p-nitrophenyl phosphate
-
-
?
additional information
?
-
-
substrate specificity of the 6 cell wall isoenzymes: isoenzyme PI-III has the lowest specificity among the six isoenzymes
-
-
?
5'-AMP + H2O
adenosine + phosphate
-
3% of the activity with p-nitrophenyl phosphate
-
-
?
ATP + H2O
ADP + phosphate
-
38% of the activity with p-nitrophenyl phosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
29% of the activity with p-nitrophenyl phosphate
-
-
?
NADP+ + H2O
NAD+ + phosphate
-
68% of the activity with p-nitrophenyl phosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe3+
phosphate forms an unusual tripodal complex with the Fe(III)-Mn(II) center, structure, oxygen binding and bridging at the metal ion center
Mn2+
strictly required, phosphate forms an unusual tripodal complex with the Fe(III)-Mn(II) center, structure, oxygen binding and bridging at the metal ion center
phosphate
forms an unusual tripodal complex with the Fe(III)-Mn(II) center, structure
Fe3+
Mn3+
Fe3+
isozyme 3 contains a diiron metal center in contrast to isozymes 1 and 2 which contain Fe(III)-Mn(II) centers, analysis of prosthetic metal ions/groups
Mn3+
-
Mn3+ may play an important role on effective binding of phosphate and acceleration of hydrolysis of phosphomonoesters at pH 4-6
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphate
competitive, moderate to weak bonding interactions to the enzyme
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
immobilization of the purified enzyme on glutaraldehyde-activated aminopropyl controlled-pore glass activates the enzyme
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
pH-dependence of Km-values of Mn(III)-acid phosphatase and Fe(III)substituted acid phosphatase with p-nitrophenyl phosphate
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
maximal turnover at neutral pH
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
545
purified recombinant wild-type enzyme in presence of L-ascorbic acid at 10 mM
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
additional information
forms a micro-oxo-bridge at pH 4.9, maximal turnover at neutral pH
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). PPAF1_IPOBA
473
0
53815
Swiss-Prot
Secretory Pathway (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
55000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme, 22 mg/ml protein in 0.1 M acetate, pH 4.9, mixed with well solution containing 0.1 M citric acid, pH 3.5-4.0, 7.5% PEG 6000, 10% isopropanol, 50 mM phosphate, and 10% glycerol, 4°C, cryoprotection by increase of glycerol concentration to 20%, X-ray diffraction structure determination and analysis at 2.5 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y291A
site-directed mutagenesis of an substrate binding ssite residue to the correspondent residue of isozyme 1, the mutant shows decreased activity compared to the wild-type isozyme 3
Y291H
site-directed mutagenesis of an substrate binding ssite residue to the correspondent residue of isozyme 1, the mutant shows increased activity compared to the wild-type isozyme 3
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the cogelled enzyme is mechanically stable over a wide range of temperature
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant isozyme 3 199fold from Sf9 insect cells in two steps by QBB-resin and hydrophobic interaction chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
subcloning in Escherichia coli, expression of wild-type and mutant isozyme 3 in Spodoptera frugiperda Sf9 cells using the baculovirus infection system
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
immobilization of the purified enzyme on glutaraldehyde-activated aminopropyl controlled-pore glass activates the enzyme, assay automatization, system evaluation, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kawabe, H.; Sugiura, Y.; Terauchi, M.; Tanaka, H.
Mn(III)-containing acid phosphatase. Properties of Fe(III)-substituted enzyme and function of Mn(III) and Fe(III) in plant and mammalian acid phosphatases
Biochim. Biophys. Acta
784
81-89
1984
Ipomoea batatas
Sugiura, Y.; Kawabe, H.; Tanaka, H.; Fujimoto, S.; Ohara, A.
Purification, enzymatic properties, and active site environment of a novel manganese(III)-containing acid phosphatase
J. Biol. Chem.
256
10664-10670
1981
Ipomoea batatas
Sugawara, S.; Inamoto, Y.; Ushijima, M.
Resolution and some properties of acid phosphatase isoenzymes bound to the cell wall of potato tubers
Agric. Biol. Chem.
45
1767-1773
1981
Ipomoea batatas
-
Alfani, F.; Albanesi, D.; Cantarella, M.; Scardi, V.
Effects of temperature and shear on the activity of acid phosphatase in a tubular membrane reactor
Enzyme Microb. Technol.
4
181-184
1982
Ipomoea batatas
-
Kusudo, T.; Sakaki, T.; Inouye, K.
Purification and characterization of purple acid phosphatase PAP1 from dry powder of sweet potato
Biosci. Biotechnol. Biochem.
67
1609-1611
2003
Ipomoea batatas
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)
Yamato, S.; Kawakami, N.; Shimada, K.; Ono, M.; Idei, N.; Itoh, Y.; Tachikawa, E.
Sweet potato acid phosphatase immobilized on glutaraldehyde-activated aminopropyl controlled-pore glass: activation, repeated use and enzyme fatigue
Biol. Pharm. Bull.
27
210-215
2004
Ipomoea batatas
Waratrujiwong, T.; Krebs, B.; Spener, F.; Visoottiviseth, P.
Recombinant purple acid phosphatase isoform 3 from sweet potato is an enzyme with a diiron metal center
FEBS J.
273
1649-1659
2006
Ipomoea batatas (Q9ZS50)
Schenk, G.; Gahan, L.R.; Carrington, L.E.; Mitic, N.; Valizadeh, M.; Hamilton, S.E.; de Jersey, J.; Guddat, L.W.
Phosphate forms an unusual tripodal complex with the Fe-Mn center of sweet potato purple acid phosphatase
Proc. Natl. Acad. Sci. USA
102
273-278
2005
Ipomoea batatas (Q9SE00)
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