Koenzim F420

Koenzim F420 (8-hidroksi-5-deazaflavin) je koenzim koji učestvuje u redoks reakcijama u metanogenima,^[1] u mnogim aktinobakterijama, i sporadično u drugim bakterijskim rodovima. On je flavinski derivat. Koenzim je supstrat za koenzim F420 hidrogenazu,^[2] 5,10-metilentetrahidrometanopterin reduktazu i metilentetrahidrometanopterin dehidrogenazu.^[3]^[4]

Posebno bogat prirodni izvor F420 je Mycobacterium smegmatis, u kojoj nekoliko desetina enzima koristi F420 umesto srodnog kofaktora FMN koji koriste homologni enzimi većine drugih vrsta.^[5]

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Reference

^ Deppenmeier U (2002). „Redox-driven proton translocation in methanogenic Archaea”. Cell. Mol. Life Sci. 59 (9): 1513—33. PMID 12440773. doi:10.1007/s00018-002-8526-3.
^ Fox JA, Livingston DJ, Orme-Johnson WH, Walsh CT (1987). „8-Hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum: 1. Purification and characterization”. Biochemistry. 26 (14): 4219–27. PMID 3663585. doi:10.1021/bi00388a007.
^ Hagemeier CH, Shima S, Thauer RK, Bourenkov G, Bartunik HD, Ermler U (2003). „Coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase (Mtd) from Methanopyrus kandleri: a methanogenic enzyme with an unusual quarternary [sic] structure”. J. Mol. Biol. 332 (5): 1047—57. PMID 14499608. doi:10.1016/S0022-2836(03)00949-5.
^ GD; Geerts, WJ; Keltjens, JT; Van Der Drift, C; Vogels, GD (1991). „Purification and properties of 5,10-methylenetetrahydromethanopterin dehydrogenase and 5,10-methylenetetrahydromethanopterin reductase, two coenzyme F420-dependent enzymes, from Methanosarcina barkeri”. Biochim. Biophys. Acta. 1079 (3): 293–302. PMID 1911853. doi:10.1016/0167-4838(91)90072-8.
^ Selengut JD, Haft DH (2010). „Unexpected abundance of coenzyme F(420)-dependent enzymes in Mycobacterium tuberculosis and other actinobacteria.”. J Bacteriol. 192 (21): 5788–98. PMC 2953692 . PMID 20675471. doi:10.1128/JB.00425-10.

Spoljašnje veze

KEGG entry for F420

[1] Deppenmeier U (2002). „Redox-driven proton translocation in methanogenic Archaea”. Cell. Mol. Life Sci. 59 (9): 1513—33. PMID 12440773. doi:10.1007/s00018-002-8526-3.

[2] Fox JA, Livingston DJ, Orme-Johnson WH, Walsh CT (1987). „8-Hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum: 1. Purification and characterization”. Biochemistry. 26 (14): 4219–27. PMID 3663585. doi:10.1021/bi00388a007.

[3] Hagemeier CH, Shima S, Thauer RK, Bourenkov G, Bartunik HD, Ermler U (2003). „Coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase (Mtd) from Methanopyrus kandleri: a methanogenic enzyme with an unusual quarternary [sic] structure”. J. Mol. Biol. 332 (5): 1047—57. PMID 14499608. doi:10.1016/S0022-2836(03)00949-5.

[4] GD; Geerts, WJ; Keltjens, JT; Van Der Drift, C; Vogels, GD (1991). „Purification and properties of 5,10-methylenetetrahydromethanopterin dehydrogenase and 5,10-methylenetetrahydromethanopterin reductase, two coenzyme F420-dependent enzymes, from Methanosarcina barkeri”. Biochim. Biophys. Acta. 1079 (3): 293–302. PMID 1911853. doi:10.1016/0167-4838(91)90072-8.

[5] Selengut JD, Haft DH (2010). „Unexpected abundance of coenzyme F(420)-dependent enzymes in Mycobacterium tuberculosis and other actinobacteria.”. J Bacteriol. 192 (21): 5788–98. PMC 2953692 . PMID 20675471. doi:10.1128/JB.00425-10.

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