Structure and quantum chemical analysis of NAD+-dependent isocitrate dehydrogenase: hydride transfer and co-factor specificity.

Structure and quantum chemical analysis of NAD+-dependent isocitrate dehydrogenase: hydride transfer and co-factor specificity. Research Abstract Details 

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Structure and quantum chemical analysis of NAD+-dependent isocitrate dehydrogenase: hydride transfer and co-factor specificity. Abstract Text:

Katsumi Imada,Takashi Tamura,Ryo Takenaka,Issei Kobayashi,Keiichi Namba,Kenji Inagaki,Katsumi Imada,Takashi Tamura,Ryo Takenaka,Issei Kobayashi,Keiichi Namba,Kenji Inagaki,Katsumi Imada,Takashi Tamura,Ryo Takenaka,Issei Kobayashi,Keiichi Namba,Kenji Inagaki,

The crystal structure of Acidithiobacillus thiooxidans isocitrate dehydrogenase complexed with NAD+ and citrate has been solved to a resolution of 1.9 A. The protein fold of this NAD+-dependent enzyme shares a high similarity with those of NADP+-dependent bacterial ICDHs. The NAD+ and the citrate are clearly identified in the active site cleft with a well-defined electron density. Asp-357 is the direct cofactor-specificity determinant that interacts with 2'-OH and 3'-OH of the adenosine ribose. The adenosine ribose takes a C2'-endo puckering conformation as previously reported for an NAD+-specific isopropylmalate dehydrogenase. The nicotinamide moiety of NAD+ has the amide NH2 group oriented in cis conformation with respect to the C4 carbon of the nicotinamide ring, slanted toward the bound citrate molecule with a dihedral angle of -21 degrees . The semi-empirical molecular orbital calculation suggests that the pro-R hydrogen atom at C4 of NADH would bear the largest negative charge when the amide NH2 group is in such conformation, suggesting that the amide group has a catalytically significant role in stabilizing the transition state as NADH is being formed during the hydride transfer catalysis.

Structure and quantum chemical analysis of NAD+-dependent isocitrate dehydrogenase: hydride transfer and co-factor specificity. Publishing Authors By Initials

K Imada,T Tamura,R Takenaka,I Kobayashi,K Namba,K Inagaki,K Imada,T Tamura,R Takenaka,I Kobayashi,K Namba,K Inagaki,K Imada,T Tamura,R Takenaka,I Kobayashi,K Namba,K Inagaki,

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Structure and quantum chemical analysis of NAD+-dependent isocitrate dehydrogenase: hydride transfer and co-factor specificity. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Proteins

VOLUME: 70

Page Numbers: 63-71

Journal Abbreviation: Proteins

ISSN: 1097-0134

DAY: 1

MONTH: Jan

YEAR: 2008

Structure and quantum chemical analysis of NAD+-dependent isocitrate dehydrogenase: hydride transfer and co-factor specificity. Information

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LANGUAGE: eng

NlmUniqueID: 8700181

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Grant and Affiliation Information for Structure and quantum chemical analysis of NAD+-dependent isocitrate dehydrogenase: hydride transfer and co-factor specificity.

AFFILIATION: Department of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan. kimada@fbs.osaka-u.ac.jp

Country: United States

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MEDLINETA: Proteins

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