Literature summary for 2.7.6.3 extracted from

Li, Y.; Wu, Y.; Blaszczyk, J.; Ji, X.; Yan, H.
Catalytic roles of arginine residues 82 and 92 of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase: site-directed mutagenesis and biochemical studies (2003), Biochemistry, 42, 1581-1588.

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Protein Variants

Protein Variants	Comment	Organism
R82A	mutation causes a decrease in the rate constant for the chemical step by a factor of 380, no significant change in the binding energy or kinetics of either substrate	Escherichia coli
R92A	mutation causes a decrease in the rate constant for the chemical step by a factor of 35000. The mutation causes no significant change in the binding energy or binding kinetics of MgATP2-. It does not cause a significant change in the binding energy of 6-hydroxymethyl-7,8-dihydropterin either but causes a decrease in the association rate constant for the binding of 6-hydroxymethyl-7,8-dihydropterin by a factor of 1.4 and a decrease in the dissociation rate constant by a factor of 10	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	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	-	Escherichia coli

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Release 2023.1 (January 2023)