Literature summary for 2.8.1.10 extracted from

Kriek, M.; Martins, F.; Leonardi, R.; Fairhurst, S.A.; Lowe, D.J.; Roach, P.L.
Thiazole synthase from Escherichia coli: an investigation of the substrates and purified proteins required for activity in vitro (2007), J. Biol. Chem., 282, 17413-17423.

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P30139	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the thiazole-forming activity requires four proteins isolated as heterodimers: ThiGH and ThiFS. Reconstitution of the [4Fe-4S] cluster in ThiH is essential for activity, as is the use of ThiS in the thiocarboxylate form. S-adenosylmethionine binds to the [4Fe-4S] cluster, which becomes more susceptible to reduction to the +1 state. In addition to the proteins, 1-deoxy-xylulose-5-phosphate, tyrosine, S-adenosylmethionine, and a reductant are required. 1 mol equivalent of thiazole phosphate is formed per ThiGH. For each mole of thiazole phosphate formed, 1 equivalent of S-adenosylmethionine and 1 equivalent of tyrosine are utilized, and 1 equivalent of 5-deoxyadenosine is produced. Mechanistic hypothesis suggests that S-adensylmethionine is reductively cleaved to yield a highly reactive 5-deoxyadenosyl radical. This radical abstracts the phenolic hydrogen atom from tyrosine, and the resultant substrate radical cleaves to yield dehydroglycine, which is required by ThiG for the thiazole cyclization reaction	Escherichia coli	?	-	?

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Release 2023.1 (January 2023)