Literature summary for 2.7.1.50 extracted from

Campobasso, N.; Mathews, II; Begley, T.P.; Ealick, S.E.
Crystal structure of 4-methyl-5-beta-hydroxyethylthiazole kinase from Bacillus subtilis at 1.5 A resolution (2000), Biochemistry, 39, 7868-7877.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystallization by vapor diffusion equilibration, crystal structure at 1.5 A resolution	Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole	Bacillus subtilis	the enzyme is a salvage enzyme in the thiamin biosynthetic pathway and enables the cell to use recycled 4-methyl-5-beta-hydroxyethylthiazole as an alternative to its synthesis from 1-deoxy-D-xylulose-5-phosphate, cysteine, and tyrosine	ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole	-	?

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	P39593	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole	phosphate transfer occurs by an inline mechanism	Bacillus subtilis	ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole	-	?
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole	the enzyme is a salvage enzyme in the thiamin biosynthetic pathway and enables the cell to use recycled 4-methyl-5-beta-hydroxyethylthiazole as an alternative to its synthesis from 1-deoxy-D-xylulose-5-phosphate, cysteine, and tyrosine	Bacillus subtilis	ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole	-	?

Subunits

Subunits	Comment	Organism
More	as determined from crystallization data the enzyme is a trimer of identical subunits, the active site is formed at the interface between two subunits within the trimer	Bacillus subtilis

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Release 2023.1 (January 2023)