Crystallization (Comment) | Organism |
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structures of both flavin reductase subunit SgcE6, and chlorophenol-4-monooxygenase subunit SgcC, t 1.66 and 2.63 A resolution, respectively. A flexible loop near the active site of SgcE6 plays a role in FAD binding | Streptomyces globisporus |
Organism | UniProt | Comment | Textmining |
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Streptomyces globisporus | Q8GME2 and Q8GMG6 | Q8GME2 i.e. flavin reductase subunit SgcE6, Q8GMG6 i.e. chlorophenol-4-monooxygenase subunit SgcC | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
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additional information | subunit SgcE6 is responsible for the production of FADH2. FADH2 diffuses to SgcC, where Arg119 activates an O2 molecule to form a C-4a-hydroperoxyflavin intermediate. SgcC2 interacts with SgcC and guides the (S)-3-chloro-beta-tyrosyl moiety into the active site. It is activated by conserved general base His161, which results in electrophilic attack of the hydroxy group of the C-4a-hydroperoxyflavin intermediate, introducing a hydroxy group at the C-5 position of the (S)-3-chloro-beta-tyrosyl moiety. The hydroxyflavin (FADHO-) abstracts a proton from the C-5 atom of the intermediate, resulting in the formation of the rearomatizated (S)-3-chloro-5-hydroxy-beta-tyrosyl-S-SgcC2, which then dissociates from SgcC. Finally, the hydroxyflavin (FADHOH) undergoes dehydration to form FAD, which is released and recycled by SgcE6 | Streptomyces globisporus | ? | - |
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Synonyms | Comment | Organism |
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SgcE6 | - |
Streptomyces globisporus |