Literature summary for 2.7.7.73 extracted from

Duda, D.M.; Walden, H.; Sfondouris, J.; Schulman, B.A.
Structural analysis of Escherichia coli ThiF (2005), J. Mol. Biol., 349, 774-786.

Search for more literature for 2.7.7.73

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21(DE3) cells	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
ThiF alone and in complex with ATP, hanging drop vapor diffusion method, using 14% (w/v) ammonium acetate, 50 mM MES (pH 6.5), 5 mM dithiothreitol, at 25°C	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required for activity	Escherichia coli
Zn2+	each monomer of ThiF binds one zinc atom	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P30138	-	-

Purification (Commentary)

Purification (Comment)	Organism
glutathione affinity column chromatography, Resource Q column chromatography, and Superdex 200 gel filtration	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + [sulfur-carrier protein ThiS]	ThiF catalyzes adenylation of the C terminus of ThiS	Escherichia coli	diphosphate + adenylyl-[sulfur-carrier protein ThiS]	-	?
additional information	ThiF shows no activity with GTP, CTP or TTP as cosubstrates	Escherichia coli	?	-	?

Subunits

Subunits	Comment	Organism
homodimer	x-ray crystallography	Escherichia coli

Synonyms

Synonyms	Comment	Organism
ThiF	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
ATP	ThiF shows strong preference for ATP over GTP, CTP or TTP	Escherichia coli

General Information

General Information	Comment	Organism
metabolism	ThiF is an enzyme in the biosynthetic cascade for generating the essential cofactor thiamin diphosphate	Escherichia coli

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Release 2023.1 (January 2023)