Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.3.2 extracted from

  • Ki, M.R.; Yun, S.K.; Choi, K.M.; Hwang, S.Y.
    Identification and characterization of the acid phosphatase HppA in Helicobacter pylori (2011), J. Microbiol. Biotechnol., 21, 483-493.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ inhibits enzymatic activity Helicobacter pylori
Mn2+ inhibits enzymatic activity Helicobacter pylori
Zn2+ inhibits enzymatic activity Helicobacter pylori

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.12
-
4-nitrophenyl phosphate pH 6.0, 37°C, periplasmic enzyme with 0.1 mM NiCl2 Helicobacter pylori
0.43
-
4-nitrophenyl phosphate pH 6.0, 37°C, periplasmic enzyme without Ni2+ Helicobacter pylori
0.67
-
4-nitrophenyl phosphate pH 6.0, 37°C, periplasmic enzyme with 0.1 mM NiCl2 Helicobacter pylori
0.76
-
4-nitrophenyl phosphate pH 6.0, 37°C, membrane-bound enzyme Helicobacter pylori
0.79
-
ATP pH 6.0, 37°C, membrane-bound enzyme Helicobacter pylori
4.14
-
4-nitrophenyl phosphate pH 6.0, 37°C, periplasmic enzyme without Ni2+ Helicobacter pylori

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Helicobacter pylori 16020
-
periplasm
-
Helicobacter pylori
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
K+ under acidic conditions (pH below 4.5) periplasmic enzymatic activity is dependent on the presence of mono- and/or divalent cations. Hydrolsis of 4-nitrophenyl phosphate is enhanced but not hydrolsis of ATP Helicobacter pylori
NH4+ under acidic conditions (pH below 4.5) periplasmic enzymatic activity is dependent on the presence of mono- and/or divalent cations Helicobacter pylori
Ni2+ under acidic conditions (pH below 4.5) periplasmic enzymatic activity is dependent on the presence of mono- and/or divalent cations. Ni2+ lowers Km without changing Vmax Helicobacter pylori

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
24000
-
SDS-PAGE, periplasmic fraction Helicobacter pylori
27000
-
SDS-PAGE, membrane-bound form Helicobacter pylori
72000
-
trimeric native from of the enzyme Helicobacter pylori

Organism

Organism UniProt Comment Textmining
Helicobacter pylori
-
-
-

Purification (Commentary)

Purification (Comment) Organism
purified 192- and 34fold from the periplasmic and membrane fractions of Helicobacter pylori. Purification steps of membrane enzyme: Solubilization, DEAE-Sepharose and Phe-Sepharose. Purification steps of periplasmic enzyme: (NH4)2SO4 precipitation, SP-Sepharose, Phe-Sepharose and Q-Sepharose Helicobacter pylori

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl phosphate + H2O
-
Helicobacter pylori 4-nitrophenol + phosphate
-
?
ATP + H2O periplasmic enzyme: stronger hydrolysis at pH 5.5 than at pH 6.0 Helicobacter pylori ADP + phosphate
-
?
CTP + H2O periplasmic enzyme: stronger hydrolysis at pH 6.0 than at pH 5.5 Helicobacter pylori CDP + phosphate
-
?
TTP + H2O periplasmic enzyme: stronger hydrolysis at pH 6.0 than at pH 5.5 Helicobacter pylori TDP + phosphate
-
?

Subunits

Subunits Comment Organism
trimer
-
Helicobacter pylori

Synonyms

Synonyms Comment Organism
HppA
-
Helicobacter pylori

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Helicobacter pylori

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
periplasmic enzyme: adenosine nucleotides are better hydrolyzed at pH 5.5 than at pH 6.0 Helicobacter pylori
6
-
assay at Helicobacter pylori
6
-
periplasmic enzyme: CTP and TTP are better hydrolyzed at pH 6 than at pH 5.5 Helicobacter pylori

pH Range

pH Minimum pH Maximum Comment Organism
4.5
-
periplasmic enzyme is inactive at pH below 4.5 but displays activity in the presence of NH4Cl and NiCl2 Helicobacter pylori

General Information

General Information Comment Organism
malfunction HppA knockout cells grow more slowly. Knockout cells import Mg2+ at a markedly lowered rate, but assimilate urea rapidly, with a subsequent increase in extracellular pH. Moreover, mutant cells are much more sensitive to extracellular potassium ions, as well as to metronidazole, omeprazole, or thiophenol, with considerably lowered MIC values, than wild-type cells Helicobacter pylori