Abstract
Aldose reductase-mediated reaction of glyceraldehyde with enzyme-bound NADP + gives different products depending on the enantiomer used. D-Glyceraldehyde reacts to form a chromophore (336 nm) similar to the covalent NADP-glycolaldehyde adduct characterized previously [Grimshaw et al. 1990 Biochemistry 29, 9936–9946]. L-Glyceraldehyde, however, reacts in a slow steady-state process to form an additional chromophore whose spectral properties (λ max 290 nm, ε ≈ 16,700 M −1cm −1) suggest that hydration of the nicotinamide 5,6-double bond has occurred. Several mechanisms are proposed to explain this unique stereoisomer-dependent change in reaction pathway.
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