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Information on EC 3.1.3.2 - acid phosphatase

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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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This record set is specific for:
UNIPROT: Q9ZVL6
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Word Map
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
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
-
-
-
-
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
-
-
-
-
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
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
6,8 difluoro-4-methylumbelliferyl phosphate + H2O
6,8 difluoro-4-methylumbelliferol + phosphate
show the reaction diagram
-
-
-
?
Ac-(pT)AILER + H2O
?
show the reaction diagram
synthetic phosphorylated oligopeptide
-
-
?
Ac-(pT)IALGK + H2O
?
show the reaction diagram
synthetic phosphorylated oligopeptide
-
-
?
Ac-RK(pS)AGKPKN + H2O
?
show the reaction diagram
synthetic phosphorylated oligopeptide
-
-
?
KR(pT)IRR + H2O
?
show the reaction diagram
synthetic phosphorylated oligopeptide
-
-
?
O-phospho-L-serine + H2O
L-serine + phosphate
show the reaction diagram
-
-
-
?
RRA(pT)VA + H2O
?
show the reaction diagram
synthetic phosphorylated oligopeptide
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
activity depends on divalent cations
Fe2+
activity depends on divalent cations
Mg2+
activity depends on divalent cations
Mn2+
activity depends on divalent cations
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
42.56
4-nitrophenyl phosphate
pH 4, 37°C
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
47.51
O-phospho-L-serine
pH 4, 37°C
11.89
RRA(pT)VA
synthetic phosphorylated oligopeptide, pH 4, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 4.5
highest activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 45
highest activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
U603_ARATH
285
0
31139
Swiss-Prot
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using a GSTrap FF column
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a GST-tagged fusion protein
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team