A metal‐mediated hydride shift mechanism for xylose isomerase based on the 1.6 Å Streptomycs rubiginosus structure with xylitol and D‐xylose

Keyphrases

• Xylitol 100%
• Divalent Cations 100%
• Shifting Method 100%
• Xylose Isomerase 100%
• Hydride Shift 100%
• Ring Opening 66%
• OH Groups 66%
• Isomerase 66%
• Manganese Chloride 66%
• Hydrogen Bonds (H-bonds) 66%
• Recombinant 33%
• Lysine 33%
• Glutamate 33%
• Streptomyces 33%
• Isomerization 33%
• Xylose 33%
• Aspartate 33%
• Active Sites 33%
• Biochemical Properties 33%
• Helix 33%
• Histidine Residue 33%
• Hydrophobic Residues 33%
• Histidine 33%
• Chemical Modification 33%
• Activity Profile 33%
• Bond Distance 33%
• Hydroxyl 33%
• Detailed Mechanism 33%
• Ring-opening Reaction 33%
• Extended Conformation 33%
• Catalytic Base 33%
• Active Pocket 33%
• Ring Closure 33%
• Amino Acid Side Chains 33%
• Solvent Exchange 33%
• Replacement Method 33%
• Extended Form 33%
• Multiple Isomorphous Replacement 33%
• Ring-closing 33%
• Manganese Ion 33%

Biochemistry, Genetics and Molecular Biology

• Ring Opening 100%
• Xylose Isomerase 100%
• Xylitol 100%
• Active Site 66%
• Isomerase 66%
• Histidine 66%
• Conformation 33%
• Amino Acids 33%
• Crystal Structure 33%
• Hydrogen Bond 33%
• Enzyme 33%
• Isomerization 33%
• Streptomyces 33%
• Aspartic Acid 33%
• Lysine 33%
• Xylose 33%
• Glutamic Acid 33%