The structure of NADH in the enzyme dTDP-D-glucose dehydratase (RmlB)

Keyphrases

• Nicotinamide 100%
• Hydrides 100%
• Dehydratase 100%
• D-glucose 100%
• Nicotinamide Adenine Dinucleotide (NAD+) 66%
• Single Crystal 33%
• Active Sites 33%
• Conformational Change 33%
• Dihydropyridine 33%
• Hydrogen Bonds (H-bonds) 33%
• Spectroscopic Studies 33%
• Redox Potential 33%
• Amides 33%
• Electron Density 33%
• Native Structure 33%
• Phosphate Group 33%
• Substrate Analog 33%
• Si-face 33%
• Keto 33%
• Tyrosine Residue 33%
• Ab Initio Electronic Structure Calculations 33%
• Oxygen Atom 33%
• Bending Degree 33%
• Xylose 33%
• Internal Hydrogen 33%
• Concave Surface 33%
• Nicotinamide Cofactor 33%
• Enzyme Turnover 33%
• Hydride Donor 33%
• Streptococcus Suis (S. suis) 33%

Biochemistry, Genetics and Molecular Biology

• Dehydratase 100%
• Enzyme 100%
• Nicotinamide 100%
• Coenzyme 50%
• Conformation 25%
• Hydrogen Bond 25%
• Conformational Change 25%
• Active Site 25%
• Substrate Analog 25%
• Tyrosine 25%
• Enzyme Metabolism 25%
• Serotype 25%
• Oxidation Reduction Potential 25%
• Streptococcus suis 25%
• Dihydropyridine 25%
• Xylose 25%

Chemistry

• dTDP-D-glucose 100%
• NADH 100%
• Nicotinamide 80%
• dTDP 60%
• Coenzyme 40%
• Single Crystalline Solid 20%
• Electronic State 20%
• Redox Potential 20%
• Tyrosine Residue 20%
• Carboxamide 20%
• Donor 20%
• Hydrogen Bonding 20%
• Electron Density 20%
• Phosphate Group 20%
• Xylose 20%
• Cofactor 20%
• Dihydropyridine 20%
• Oxygen Atom 20%