Literature summary for 2.7.7.73 extracted from

Lehmann, C.; Begley, T.P.; Ealick, S.E.
Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis (2006), Biochemistry, 45, 11-19.

Search for more literature for 2.7.7.73

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL834(DE3) cells	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with ThiS, hanging drop vapor diffusion method, using 7-8% polyethylene glycol 400, 35 mM calcium chloride, and 100 mM Tris-HCl (pH 7.0-7.3)	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	ThiF contains a Zn-sulfur center	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
27000	-	2 * 27000, calculated from amino acid sequence	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
Hi-Trap QFF 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 the adenylation of the carboxy terminus of ThiS and the subsequent displacement of AMP catalyzed by ThiI-persulfide to give a ThiS-ThiI acyl disulfide	Escherichia coli	diphosphate + adenylyl-[sulfur-carrier protein ThiS]	-	?

Subunits

Subunits	Comment	Organism
homodimer	2 * 27000, calculated from amino acid sequence	Escherichia coli

Synonyms

Synonyms	Comment	Organism
ThiF	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Escherichia coli

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Release 2023.1 (January 2023)