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Literature summary for 2.7.6.3 extracted from

  • Yan, H.; Ji, X.
    Role of protein conformational dynamics in the catalysis by 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (2011), Protein Pept. Lett., 18, 328-335.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
R84A the mutation causes little changes in either dissociation constants or kinetic constants of the enzyme-catalyzed reaction except that the rate constant for the chemical step of the forward reaction decreases by a factor of 4 Escherichia coli
W89A the mutation does not have any significant effects on the Kd and the rate constants for the binding of MgATP, but the Kd for 6-hydroxymethyl-7,8-dihydropteridine of the mutant increases by a factor of 6.5. The mutation decreases the rate constant for the chemical step of the forward reaction by a factor of about 23 and the rate constant for the chemical step of the reverse reaction by a factor of about 33 Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ two Mg2+ ions are required for catalysis Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
18000
-
x * 18000, SDS-PAGE Escherichia coli

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
-
Escherichia coli AMP + 6-hydroxymethyl-7,8-dihydropteridine diphosphate
-
?

Subunits

Subunits Comment Organism
? x * 18000, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase
-
Escherichia coli
HPPK
-
Escherichia coli