Stopped-flow studies of human aldose reductase reveal which enzyme form predominates during steady-state turnover in either reaction direction.

Abstract

Progress in the aldo-keto reductase field has been quite rapid since the solution of the 3-dimensional structure of aldose reductase (ALR2) by the French group (Rondeau et al., 1992) and the Baylor group (Wilson et al., 1992), with additional contributions from Washington University School of Medicine with BioCryst Pharmaceuticals (Borhani et al., 1992) and with Dr. Quiocho’s laboratory (Wilson et al., 1993). Most recently, a definitive assignment of the active site constellation of amino acid residues and their likely roles in the catalytic mechanism was established by the collaborative efforts of researchers at Baylor, Brandeis and The Whittier Institute (Harrison et al., 1994; Bohren et al., 1994).KeywordsAldose ReductaseNucleotide BindingProgress CurveAldehyde ReductaseBurst PhaseThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.