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Literature summary for 1.1.1.21 extracted from

  • Blakeley, M.P.; Ruiz, F.; Cachau, R.; Hazemann, I.; Meilleur, F.; Mitschler, A.; Ginell, S.; Afonine, P.; Ventura, O.N.; Cousido-Siah, A.; Haertlein, M.; Joachimiak, A.; Myles, D.; Podjarny, A.
    Quantum model of catalysis based on a mobile proton revealed by subatomic x-ray and neutron diffraction studies of h-aldose reductase (2008), Proc. Natl. Acad. Sci. USA, 105, 1844-1848.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
single-crystal x-ray data, neutron Laue data analysis and quantum mechanical modeling of aldose reductase. Quantum model of catalysis Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P15121
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Reaction

Reaction Comment Organism Reaction ID
alditol + NAD(P)+ = aldose + NAD(P)H + H+ after the hydride donation step, the positive charge in the nicotinamide head stabilizes the neutral bridge between residues D43 and L77, allowing the relaxation of the tyrosine geometry toward the substrate head and the subsequent proton donation. After this last step, Y48 recoils to a locked geometry where the D43-L77 salt bridge is formed again and completes a tight four-charge sandwich involving the D(-), L(+), Y(-), and nicotinamide(+) head Homo sapiens