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Literature summary for 1.3.8.17 extracted from

  • Bashiri, G.; Antoney, J.; Jirgis, E.NM.; Shah, M.V.; Ney, B.; Copp, J.; Stuteley, S.M.; Sreebhavan, S.; Palmer, B.; Middleditch, M.; Tokuriki, N.; Greening, C.; Scott, C.; Baker, E.N.; Jackson, C.J.
    A revised biosynthetic pathway for the cofactor F420 in prokaryotes (2019), Nat. Commun., 10, 1558 .
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
apoenzyme and in complex with phosphoenolpyruvate, to 1.99 and 2.18 A resolution, respectively Mycolicibacterium smegmatis

Organism

Organism UniProt Comment Textmining
Mycolicibacterium smegmatis A0QUZ4 cf. EC 2.7.7.105, EC 6.3.2.31, and EC 6.3.2.34
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Mycolicibacterium smegmatis ATCC 700084 A0QUZ4 cf. EC 2.7.7.105, EC 6.3.2.31, and EC 6.3.2.34
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oxidized coenzyme F420-0 + FMN
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 Mycolicibacterium smegmatis dehydro coenzyme F420-0 + FMNH2
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 ?
oxidized coenzyme F420-0 + FMN
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 Mycolicibacterium smegmatis ATCC 700084 dehydro coenzyme F420-0 + FMNH2
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 ?

General Information

General Information Comment Organism
physiological function guanylyltransferase FbiD accepts phosphoenolpyruvate, leading to the formation of intermediate dehydro-F420-0. The C-terminal domain of FbiB then utilizes FMNH2 to reduce dehydro-F420-0, which produces mature F420 species when combined with the gamma-glutamyl ligase activity of the N-terminal domain. FbiB also catalyzes the activities of EC 6.3.2.31, coenzyme F420-0:L-glutamate ligase, and EC 6.3.2.34, coenzyme F420-1:gamma-L-glutamate ligase. Expression of genes FbiABCD is sufficient to produce F420 in Escherichia coli Mycolicibacterium smegmatis