Structures of Iron-Dependent Alcohol Dehydrogenase 2 from Zymomonas mobilis ZM4 with and without NAD + Cofactor

The ethanologenic bacterium Zymomonas mobilis ZM4 is of special interest because it has a high ethanol yield. This is made possible by the two alcohol dehydrogenases (ADHs) present in Z. mobilis ZM4 (zmADHs), which shift the equilibrium of the reaction toward the synthesis of ethanol. They are metal...

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Veröffentlicht in:	Journal of molecular biology 2011-04, Vol.407 (3), p.413-424
Hauptverfasser:	Moon, Ji-Hyun, Lee, Hyun-Ju, Park, Suk-Youl, Song, Jung-Mi, Park, Mi-Young, Park, Hye-Mi, Sun, Jiali, Park, Jeong-Hoh, Kim, Bo Yeon, Kim, Jeong-Sun
Format:	Artikel
Sprache:	eng
Schlagworte:	alcohol dehydrogenase Alcohol Dehydrogenase - chemistry Alcohol Dehydrogenase - genetics Alcohol Dehydrogenase - metabolism Amino Acid Sequence Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Catalytic Domain crystal structure Crystallography, X-Ray Ethanol - metabolism Iron - metabolism Kinetics Models, Molecular Molecular Sequence Data NAD NAD - metabolism Protein Folding respiration Zymomonas - enzymology Zymomonas - metabolism Zymomonas mobilis
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