Organism | UniProt | Comment | Textmining |
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Escherichia coli | P30139 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
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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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