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

BRENDA support

Literature summary for 3.6.1.5 extracted from

  • Tanaka, K.; Nguyen, T.H.; Stacey, G.
    Enzymatic role for soybean ecto-apyrase in nodulation (2011), Plant Signal. Behav., 6, 1034-1036.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.1.5

Cloned(Commentary)

Cloned (Comment) Organism
expression of GS52 in Escherichia coli and in tabacco Glycine soja

Inhibitors

Inhibitors Comment Organism Structure
additional information the activity of the GS52 enzyme is not significantly affected by Nod factor addition Glycine soja

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the catalytic domain of the GS52 ectoapyrase is extracellular and therefore, must act to hydrolyze extracellular nucleotides Glycine soja
-
-

Organism

Organism UniProt Comment Textmining
Glycine soja Q9FVC2 wild soybean
-

Purification (Commentary)

Purification (Comment) Organism
recombinant GS52 from Escherichia coli and tabacco Glycine soja

Source Tissue

Source Tissue Comment Organism Textmining
root
-
 Glycine soja
-

Synonyms

Synonyms Comment Organism
ecto-apyrase
-
 Glycine soja
GS52
-
 Glycine soja
nucleoside triphosphate diphosphohydrolase
-
 Glycine soja

Expression

Organism Comment Expression
Glycine soja expression of the GS52 gene is induced upon Bradyrhizobium japonicum inoculation up

General Information

General Information Comment Organism
malfunction the inactivated, functionally disrupted enzyme is not active in stimulating nodulation Glycine soja
physiological function ecto-apyrase is an extracellular nucleoside triphosphate diphosphohydrolase that modulates the nucleotide concentration in the extracellular matrix. Ecto-apyrase controls the concentration of extracellular nucleotides. GS52 activity stimulates root nodulation, the inactivated enzyme is not effective Glycine soja