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Literature summary for 2.7.6.3 extracted from

  • Bermingham, A.; Bottomley, J.R.; Primrose, W.U.; Derrick, J.P.
    Equilibrium and kinetic studies of substrate binding to 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase from Escherichia coli (2000), J. Biol. Chem., 275, 17962-17967.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
alpha,beta-methyleneadenosine triphosphate competitive with respect to ATP Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + 6-hydroxymethyl-7,8-dihydropteridine Escherichia coli the product 6-hydroxymethyl-7,8-dihydropterin diphosphate is an intermediate in the pathway for folic acid biosynthesis AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P26281
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 6-hydroxymethyl-7,8-dihydropteridine enzyme binds ATP first, followed by 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine Escherichia coli AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
-
?
ATP + 6-hydroxymethyl-7,8-dihydropteridine the product 6-hydroxymethyl-7,8-dihydropterin diphosphate is an intermediate in the pathway for folic acid biosynthesis Escherichia coli AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
-
?
additional information binding affinity for GTP and GMP, 75fold weaker than for ATP Escherichia coli ?
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?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00031
-
alpha,beta-methyleneadenosine triphosphate
-
Escherichia coli