Literature summary for 2.7.6.3 extracted from

Hennig, M.; Dale, G.E.; D'Arcy, A.; Danel, F.; Fischer, S.; Gray, C.P.; Jolidon, S.; Muller, F.; Page, M.G.; Pattison, P.; Oefner, C.
The structure and function of the 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase from Haemophilus influenzae (1999), J. Mol. Biol., 287, 211-219.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Haemophilus influenzae

Crystallization (Commentary)

Crystallization (Comment)	Organism
a complex of the purified protein with a substrate analog is crystallized and its structure is solved by multiple anomalous dispersion using phase information obtained from a single crystal of selenomethionine-labeled protein	Haemophilus influenzae

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
18299	-	1 * 18299, calculation from nucleotide sequence	Haemophilus influenzae
20000	-	gel filtration, equilibrium sedimentation, quasi-elastic light scattering	Haemophilus influenzae

Organism

Organism	UniProt	Comment	Textmining
Haemophilus influenzae	-	Brookhaven Protein Data Bank: 1cbk	-

Purification (Commentary)

Purification (Comment)	Organism
-	Haemophilus influenzae

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
monomer	1 * 18299, calculation from nucleotide sequence	Haemophilus influenzae

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Release 2023.1 (January 2023)