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Literature summary extracted from

  • 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 (2004), J. Biol. Chem., 279, 37477-37484.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.3.2 Tartrate slight activation Phaseolus vulgaris

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.2 gene KeACP, DNA and amino acid sequence determination and analysis Phaseolus vulgaris

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.2 molybdate complete inhibition at 0.1 mM Phaseolus vulgaris
3.1.3.2 vanadate 30 min, 30°C, leads to complete loss of phosphatase activity of the enzyme at 0.1 mM and gain of chloroperoxidase activity by the enzyme, overview Phaseolus vulgaris

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.2 additional information the enzyme is not affected by citrate, EDTA, fluoride, Zn2+, Fe3+, and Mn2+ Phaseolus vulgaris

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.3.2 45000
-
1 * 45000 + 1 * 56000, SDS-PAGE Phaseolus vulgaris
3.1.3.2 56000
-
1 * 45000 + 1 * 56000, SDS-PAGE Phaseolus vulgaris
3.1.3.2 96000
-
gel filtration Phaseolus vulgaris

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.2 Phaseolus vulgaris Q764C1
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.3.2 glycoprotein both subunit types are glycosylated Phaseolus vulgaris

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.2 852fold to homogeneity from embryonic axes by DEAE ion exchange and concanavalin A affinity chromatography Phaseolus vulgaris

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.3.2 embryo expression during elongation in germination Phaseolus vulgaris
-
3.1.3.2 seed embryonic axes, expression during elongation in germination Phaseolus vulgaris
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.3.2 383.3
-
purified enzyme Phaseolus vulgaris

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.2 2-phosphoglycerate + H2O
-
Phaseolus vulgaris glycerate + phosphate
-
?
3.1.3.2 3-phosphoglycerate + H2O
-
Phaseolus vulgaris glycerate + phosphate
-
?
3.1.3.2 4-nitrophenyl phosphate + H2O
-
Phaseolus vulgaris 4-nitrophenol + phosphate
-
?
3.1.3.2 ADP + H2O low activity Phaseolus vulgaris AMP + phosphate
-
?
3.1.3.2 alpha-naphthyl phosphate + H2O
-
Phaseolus vulgaris alpha-naphthol + phosphate
-
?
3.1.3.2 AMP + H2O
-
Phaseolus vulgaris adenosine + phosphate
-
?
3.1.3.2 ATP + H2O
-
Phaseolus vulgaris ADP + phosphate
-
?
3.1.3.2 beta-naphthyl phosphate + H2O
-
Phaseolus vulgaris beta-naphthol + phosphate
-
?
3.1.3.2 D-glucose 1-phosphate + H2O
-
Phaseolus vulgaris D-glucose + phosphate
-
?
3.1.3.2 D-glucose 6-phosphate + H2O
-
Phaseolus vulgaris D-glucose + phosphate
-
?
3.1.3.2 additional information substrate specificity, overview, vanadate leads to loss of phosphatase activity of the enzyme and gain of chloroperoxidase activity by the enzyme, overview Phaseolus vulgaris ?
-
?
3.1.3.2 phospho-L-serine + H2O low activity Phaseolus vulgaris L-serine + phosphate
-
?
3.1.3.2 phospho-L-threonine + H2O
-
Phaseolus vulgaris L-threonine + phosphate
-
?
3.1.3.2 phospho-L-tyrosine + H2O
-
Phaseolus vulgaris L-tyrosine + phosphate
-
?
3.1.3.2 phosphoenolpyruvate + H2O
-
Phaseolus vulgaris pyruvate + phosphate
-
?
3.1.3.2 phytate + H2O low activity Phaseolus vulgaris ? + phosphate
-
?

Subunits

EC Number Subunits Comment Organism
3.1.3.2 dimer 1 * 45000 + 1 * 56000, SDS-PAGE Phaseolus vulgaris
3.1.3.2 More three combinations of the two subunit types occur with the 56 kDa subunit dominating, no intersubunit disulfide linkages Phaseolus vulgaris

Synonyms

EC Number Synonyms Comment Organism
3.1.3.2 colorless acid phosphatase
-
Phaseolus vulgaris
3.1.3.2 KeACP
-
Phaseolus vulgaris
3.1.3.2 More the colorless acid phosphatase is distinct from the purple acid phosphatase Phaseolus vulgaris

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.2 30
-
assay at Phaseolus vulgaris

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.2 6
-
-
Phaseolus vulgaris