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Literature summary for 3.1.3.2 extracted from

  • 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 (2005), Proc. Natl. Acad. Sci. USA, 102, 273-278.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Ipomoea batatas

Inhibitors

Inhibitors Comment Organism Structure
phosphate competitive, moderate to weak bonding interactions to the enzyme Ipomoea batatas

Metals/Ions

Metals/Ions Comment Organism Structure
Fe3+ phosphate forms an unusual tripodal complex with the Fe(III)-Mn(II) center, structure, oxygen binding and bridging at the metal ion center Ipomoea batatas
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 Ipomoea batatas
phosphate forms an unusual tripodal complex with the Fe(III)-Mn(II) center, structure Ipomoea batatas

Organism

Organism UniProt Comment Textmining
Ipomoea batatas Q9SE00 cv. Golden
-

Purification (Commentary)

Purification (Comment) Organism
to over 95% purity Ipomoea batatas

Reaction

Reaction Comment Organism Reaction ID
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 Ipomoea batatas

Synonyms

Synonyms Comment Organism
More the enzyme belongs to the family of binuclear metalloenzymes Ipomoea batatas
PAP
-
Ipomoea batatas
purple acid phosphatase
-
Ipomoea batatas

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information maximal turnover at neutral pH Ipomoea batatas

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
forms a micro-oxo-bridge at pH 4.9, maximal turnover at neutral pH Ipomoea batatas
4.5
-
maximal catalytic efficiency Ipomoea batatas

pH Range

pH Minimum pH Maximum Comment Organism
3 8.5 activity range Ipomoea batatas

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.028
-
phosphate pH 7.0 Ipomoea batatas
0.196
-
phosphate pH 3.5 Ipomoea batatas
0.31
-
phosphate pH 4.9 Ipomoea batatas