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Literature summary for 2.7.6.3 extracted from

  • Li, Y.; Gong, Y.; Shi, G.; Blaszczyk, J.; Ji, X.; Yan, H.
    Chemical transformation is not rate-limiting in the reaction catalyzed by Escherichia coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (2002), Biochemistry, 41, 8777-8783.
    View publication on PubMed

Application

Application Comment Organism
medicine because the enzyme is essential for microorganisms but is absent from human and animals, the enzyme is an excellent target for developing antimicrobial agent Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required for binding of nucleotides and for the binding of 6-hydroxymethyl-7,8-dihydropteridine Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 6-hydroxymethyl-7,8-dihydropteridine
-
Escherichia coli AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
-
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