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Literature summary for 1.14.14.15 extracted from

  • Chang, C.; Lohman, J.; Cao, H.; Tan, K.; Rudolf, J.; Ma, M.; Xu, W.; Bingman, C.; Yennamalli, R.; Bigelow, L.; Babnigg, G.; Yan, X.; Joachimiak, A.; Phillips, G.; Shen, B.
    Crystal structures of SgcE6 and SgcC, the two-component monooxygenase that catalyzes hydroxylation of a carrier protein-tethered substrate during the biosynthesis of the enediyne antitumor antibiotic C-1027 in Streptomyces globisporus (2016), Biochemistry, 55, 5142-5154 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Streptomyces globisporus Q8GME2 and Q8GMG6 Q8GME2 i.e. flavin reductase subunit SgcE6, Q8GMG6 i.e. chlorophenol-4-monooxygenase subunit SgcC
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

Synonyms Comment Organism
SgcE6
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Streptomyces globisporus