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Literature summary for 3.6.1.5 extracted from

  • Tanaka, K.; Nguyen, C.T.; Libault, M.; Cheng, J.; Stacey, G.
    Enzymatic activity of the soybean ecto-apyrase GS52 is essential for stimulation of nodulation (2011), Plant Physiol., 155, 1988-1998.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
quantitative real-time RT-PCR expression analysis, recombinant expression of HA-tagged wild-type and mutant enzymes in transgenic soybean roots via Agrobacterium rhizogenes-mediated hairy root transformation, expression of His-tagged wild-type and mutant enzymes in Escherichia coli Glycine max

Protein Variants

Protein Variants Comment Organism
D209A site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme Glycine max
E182A site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme Glycine max
Q216A site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme Glycine max
S214A site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme Glycine max

Inhibitors

Inhibitors Comment Organism Structure
EDTA complete inhibition at 1 M Glycine max

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.309
-
ADP pH and temperature not specified in the publication Glycine max
0.424
-
ATP pH and temperature not specified in the publication Glycine max

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ the most effective activating divalent cation Glycine max
additional information activating cations in descending effectivity order: Ca2+, Mg2+, Ni2+, Co2+ = Mn2+ = Cd2+, Zn2+ = Cu2+ for ATPase activity, and Ca2+, Mg2+, Ni2+ = Co2+, Mn2+ = Cu2+, Cd2+ = Zn2+ for ADPase activity Glycine max

Organism

Organism UniProt Comment Textmining
Glycine max
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli Glycine max

Source Tissue

Source Tissue Comment Organism Textmining
root
-
Glycine max
-
root hair
-
Glycine max
-
root nodule
-
Glycine max
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + H2O ADPase activity of GS52 is consistently more than 1.5fold higher than the ATPase activity Glycine max AMP + phosphate
-
?
ATP + 2 H2O ADPase activity of GS52 is consistently more than 1.5fold higher than the ATPase activity Glycine max AMP + 2 phosphate
-
?
CTP + 2 H2O
-
Glycine max CMP + 2 phosphate
-
?
GDP + H2O
-
Glycine max GMP + phosphate
-
?
GTP + 2 H2O
-
Glycine max GMP + 2 phosphate
-
?
ITP + 2 H2O
-
Glycine max IMP + 2 phosphate
-
?
additional information GS52 enzyme exhibits broad substrate specificity, but its activity on pyrimidine nucleotides and diphosphate nucleotides is significantly higher than on ATP due to low specificity for the adenine base within the substratebinding pocket of the enzyme. No hydrolytic activity with AMP Glycine max ?
-
?
UDP + H2O
-
Glycine max UMP + phosphate
-
?
UTP + 2 H2O
-
Glycine max UMP + 2 phosphate
-
?

Subunits

Subunits Comment Organism
More GS52 apyrase structure modeling of apo-form and tertiary complex with the nonhydrolyzable ATP analogue AMPPNP and cofactor Ca2+, overview Glycine max

Synonyms

Synonyms Comment Organism
ecto-apyrase
-
Glycine max
GS52
-
Glycine max

General Information

General Information Comment Organism
evolution GS52 is a member of the NTPDase/apyrase family Glycine max
physiological function important role for the Glycine max ecto-apyrase GS52 in rhizobial root hair infection and root nodule formation Glycine max

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.28
-
ATP pH and temperature not specified in the publication Glycine max
3.02
-
ADP pH and temperature not specified in the publication Glycine max