Topic
Aldose
About: Aldose is a research topic. Over the lifetime, 1270 publications have been published within this topic receiving 27197 citations. The topic is also known as: aldoses.
Papers published on a yearly basis
Papers
More filters
TL;DR: The affinity of ALR2 for glucose suggests that glucose can be a substrate under hyperglycemic conditions and ALR1 shows broad specificity for aldehydes but does not efficiently catalyze the reduction of glucose due to poor binding.
67 citations
TL;DR: Molecular modeling and inhibitory activity measurements suggest that the difference in the interaction between the side chain of Trp220 and fidarestat may contribute to the different in the binding of the inhibitor to the enzymes.
Abstract: Structure determination of porcine aldehyde reductase holoenzyme in complex with the potent aldose reductase inhibitor fidarestat was carried out to explain the difference in the potency of the inhibitor for aldose and aldehyde reductases. The hydrogen bonds between the active-site residues Tyr50, His113, and Trp114 and fidarestat are conserved in the two enzymes. In aldose reductase, Leu300 forms a hydrogen bond through its main-chain nitrogen atom with the exocyclic amide group of the inhibitor, which when replaced with a Pro in aldehyde reductase, cannot form a hydrogen bond, thus causing a loss in binding energy. Furthermore, in aldehyde reductase, the side chain of Trp220 occupies a disordered split conformation that is not observed in aldose reductase. Molecular modeling and inhibitory activity measurements suggest that the difference in the interaction between the side chain of Trp220 and fidarestat may contribute to the difference in the binding of the inhibitor to the enzymes.
67 citations
TL;DR: Two aldose reductases, immunologically and electrophoretically identical to the muscle enzymes, were found in rabbit lens and also detected in the skeletal muscle of male rats and pigs and in pig and bovine lens.
67 citations
TL;DR: It is proposed that aldose and aldehyde reductase participate in the conversion of the corticosteroid ketol side chain to the glycol side chain via an aldol intermediate by the 'long loop' pathway proposed by Monder and Bradlow.
Abstract: In this paper we describe the reduction of corticosteroid metabolites containing the 17β-aldol side chain (isocorticosteroids) by aldose and aldehyde reductase from human tissues. Aldose reductase catalyzed the reduction of the aldehydes derived from cortisol and corticosterone at about the same rate, whereas aldehyde reductase preferentially acted on the aldehydes derived from 17-deoxycorticosteroids. At comparable rates of reduction the Michaelis constants for the best steroid aldehydes were one order of magnitude lower than for the hitherto best substrates. We propose that aldose and aldehyde reductase participate in the conversion of the corticosteroid ketol side chain to the glycol side chain via an aldol intermediate by the ‘long loop’ pathway proposed by Monder and Bradlow [(1977) J. Steroid Biochem. 8, 897–908].
66 citations
66 citations