Literature summary for 1.1.1.243 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.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Organism

Organism	UniProt	Comment	Textmining
Mycolicibacterium thermoresistibile	E1C9L4	-	-

Synonyms

Synonyms	Comment	Organism
A0R518 homolog	-	Mycolicibacterium thermoresistibile
MythA.01326.c	-	Mycolicibacterium thermoresistibile

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Release 2023.1 (January 2023)