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Literature summary extracted from

  • Haft, D.H.; Pierce, P.G.; Mayclin, S.J.; Sullivan, A.; Gardberg, A.S.; Abendroth, J.; Begley, D.W.; Phan, I.Q.; Staker, B.L.; Myler, P.J.; Marathias, V.M.; Lorimer, D.D.; Edwards, T.E.
    Mycofactocin-associated mycobacterial dehydrogenases with non-exchangeable NAD cofactors (2017), Sci. Rep., 7, 41074.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.243 to 1.95 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover Mycolicibacterium thermoresistibile
1.1.1.275 to 1.55 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover Mycobacterium avium
1.1.1.275 to 1.85 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover Mycobacterium avium subsp. paratuberculosis
1.1.1.275 to 1.95 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover Mycobacterium avium
1.1.1.275 to 2.0 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover Mycobacterium avium
1.1.1.275 to 2.15 A resolution. STD-NMR demonstrates binding of the potential substrate carveol, the potential product carvone, the inhibitor tricyclazol, and external redox partner 2,6-dichloroindophenol. The enzyme appears to contain a non-exchangeable NAD cofactor and may rely on an external redox partner, rather than cofactor exchange, for multiple turnover Mycobacterium avium

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.243 Mycolicibacterium thermoresistibile E1C9L4
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-
1.1.1.275 Mycobacterium avium A0A0H2ZTN5
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-
1.1.1.275 Mycobacterium avium A0A0H2ZU39
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1.1.1.275 Mycobacterium avium A0A0H2ZV91
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1.1.1.275 Mycobacterium avium A0A0H2ZWY3
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1.1.1.275 Mycobacterium avium A0A0H2ZYS9
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1.1.1.275 Mycobacterium avium 104 A0A0H2ZTN5
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1.1.1.275 Mycobacterium avium 104 A0A0H2ZU39
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1.1.1.275 Mycobacterium avium 104 A0A0H2ZV91
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1.1.1.275 Mycobacterium avium 104 A0A0H2ZWY3
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1.1.1.275 Mycobacterium avium 104 A0A0H2ZYS9
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1.1.1.275 Mycobacterium avium subsp. paratuberculosis Q73SC8
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1.1.1.275 Mycobacterium avium subsp. paratuberculosis ATCC BAA-968 Q73SC8
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-

Synonyms

EC Number Synonyms Comment Organism
1.1.1.243 A0R518 homolog
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 Mycolicibacterium thermoresistibile
1.1.1.243 MythA.01326.c
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 Mycolicibacterium thermoresistibile
1.1.1.275 MAP_4146
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 Mycobacterium avium subsp. paratuberculosis
1.1.1.275 MAV_0896
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 Mycobacterium avium
1.1.1.275 MAV_1393
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 Mycobacterium avium
1.1.1.275 MAV_1810
-
 Mycobacterium avium
1.1.1.275 MAV_2598
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 Mycobacterium avium
1.1.1.275 MAV_2983
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 Mycobacterium avium