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Literature summary for 3.6.1.5 extracted from

  • Sansom, F.M.; Riedmaier, P.; Newton, H.J.; Dunstone, M.A.; Mueller, C.E.; Stephan, H.; Byres, E.; Beddoe, T.; Rossjohn, J.; Cowan, P.J.; dApice, A.J.; Robson, S.C.; Hartland, E.L.
    Enzymatic properties of an ecto-nucleoside triphosphate diphosphohydrolase from Legionella pneumophila: substrate specificity and requirement for virulence (2008), J. Biol. Chem., 283, 12909-12918.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.1.5

Cloned(Commentary)

Cloned (Comment) Organism
expression of a His6-tagged Lpg1905 using plasmid pRSET:lpg1905 in Escherichia coli BL21(DE3) C41 strain Legionella pneumophila

Protein Variants

Protein Variants Comment Organism
E159A site-directed mutagenesis, inactive mutant Legionella pneumophila
additional information following intratracheal inoculation of A/J mice, none of the Lpg1905 mutants is able to restore virulence to an lpg1905 mutant during lung infection Legionella pneumophila
N168A site-directed mutagenesis, the mutant shows reduced activity due to decreased affinity for the nucleotide substrates, with a relatively increased Km 1.3fold for ATP hydrolysis and 3fold for ADP hydrolysis for the mutant enzyme, the mutant partially restores the ability of an enzyme-deficient Legionella pneumophila lpg1905 mutant strain to replicate in THP-1 macrophages Legionella pneumophila
Q193A site-directed mutagenesis, inactive mutant Legionella pneumophila
R122A site-directed mutagenesis, inactive mutant Legionella pneumophila
W384A site-directed mutagenesis, inactive mutant Legionella pneumophila

Inhibitors

Inhibitors Comment Organism Structure
POM-1 i.e. Na6[H2W12O40], a polyoxometalate Legionella pneumophila
POM-6 i.e. (NH4)18[NaSb9W21O86], a polyoxometalate Legionella pneumophila

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information substrate specificity and Michaelis-Menten kinetics, overview Legionella pneumophila
0.4
-
 ATP pH 7.4, 37°C, recombinant enzyme Legionella pneumophila
1
-
 ADP pH 7.4, 37°C, recombinant enzyme Legionella pneumophila

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates Legionella pneumophila
Mg2+ activates Legionella pneumophila
additional information Lpg1905 is dependent on divalent metal cations Legionella pneumophila
Zn2+ activates Legionella pneumophila

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Legionella pneumophila Lpg1905 is essentially required for intracellular replication of Legionella pneumophila in eukaryotic cells leading to the Legionnaires disease, a severe and potentially fatal form of pneumonia ?
-
 ?

Organism

Organism UniProt Comment Textmining
Legionella pneumophila
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged Lpg1905 from Escherichia coli BL21(DE3) C41 strain by nickel affinity chromatography Legionella pneumophila

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 catalytic efficiency Legionella pneumophila

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + 2 H2O
-
 Legionella pneumophila adenosine + 2 phosphate
-
 ?
ATP + 2 H2O slight preference for ATP as substrate Legionella pneumophila AMP + 2 phosphate
-
 ?
GDP + H2O
-
 Legionella pneumophila GMP + phosphate
-
 ?
GTP + 2 H2O
-
 Legionella pneumophila GMP + 2 phosphate
-
 ?
additional information Lpg1905 is essentially required for intracellular replication of Legionella pneumophila in eukaryotic cells leading to the Legionnaires disease, a severe and potentially fatal form of pneumonia Legionella pneumophila ?
-
 ?
additional information the enzyme shows the ability to hydrolyze nucleoside tri- and diphosphates, but has limited activity against CTP, CDP, UTP, and UDP Legionella pneumophila ?
-
 ?

Subunits

Subunits Comment Organism
More the enzyme contains five apyrase conserved regions Legionella pneumophila

Synonyms

Synonyms Comment Organism
ecto-nucleoside triphosphate diphosphohydrolase
-
 Legionella pneumophila
Lpg1905
-
 Legionella pneumophila
More Lpg1905 is a prokaryotic member of the CD39/NTPDase1 family of enzymes Legionella pneumophila
NTPDase
-
 Legionella pneumophila

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Legionella pneumophila

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
-
 Legionella pneumophila

pH Range

pH Minimum pH Maximum Comment Organism
5 9 significant hydrolysis of both ATP and ADP at pH 6.5-pH 8.0, negligible hydrolysis of ATP or ADP substrates occurs at pH 9.0 or at pH 6.0 or lower Legionella pneumophila

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.067
-
 POM-6 pH 7.4, 37°C, recombinant enzyme Legionella pneumophila
0.267
-
 POM-1 pH 7.4, 37°C, recombinant enzyme Legionella pneumophila