High impact information on ALR1

• The tertiary structure of aldehyde reductase is similar to that of aldose reductase and consists of an alpha/beta-barrel with the active site located at the carboxy terminus of the strands of the barrel [1].
• Aldehyde reductase, a member of the aldo-keto reductase superfamily, catalyzes the NADPH-dependent reduction of a variety of aldehydes to their corresponding alcohols [1].
• A specific aldehyde reductase was also purified to homogeneity from brain mitochondria preparations [2].
• Pig kidney aldehyde reductase is inactivated by 2,3-butanedione, phenylglyoxal, methylglyoxal, and 1,2-cyclohexanedione [3].
• A functional arginine residue in NADPH-dependent aldehyde reductase from pig kidney [3].

Biological context of ALR1

• Kinetics and mechanism of action of aldehyde reductase from pig kidney [4].
• Despite its capacity to reduce ketones, ALR3 is primarily an aldehyde reductase, but clues as to its physiological role in brain cannot be discerned from its substrate specificity [5].

Anatomical context of ALR1

• Aldehyde reductase was purified from pig kidney cortex to homogeneity by a new procedure [6].

Associations of ALR1 with chemical compounds

• Sheep liver ALR1 was inhibited by the ionized forms of alrestatin, sorbinil, valproate, 2-ethylhexanoate and phenobarbitone, indicating the presence of an anion-binding site similar to that described for the pig liver enzyme, which interacts with inhibitors and substrates containing a carboxy group [7].
• ALR1 and ALR2 are immunologically nonrelated, and little immunologic relatedness exists between aldehyde reductases, particularly ALR1, from different species [8].
• Unlike aldose reductase, the N epsilon 2 of the imidazole ring of His 113 in aldehyde reductase interacts, through a hydrogen bond, with the amide group of the nicotinamide ring of NADPH [1].
• Some physical and chemical properties of the monomeric NADP+-dependent aldehyde reductase (previously called TPN-L-hexonate dehydrogenase or D-glucuronate reductase) from pig kidney have been examined [9].
• In the reduction of D-glyceraldehyde, catalyzed by aldehyde reductase, the pro-4R "A" hydrogen of NADPH attacks the re face of the carbonyl group [9].

Physical interactions of ALR1

• Structure of aldehyde reductase holoenzyme in complex with the potent aldose reductase inhibitor fidarestat: implications for inhibitor binding and selectivity [10].

Other interactions of ALR1

• Both ALR1 and ALR2 may be involved in the reduction of isocorticosteroids [5].

Analytical, diagnostic and therapeutic context of ALR1

• The mutant binds cofactor (both oxidized and reduced) more tightly than the wild-type enzyme but shows a complete lack of binding of the aldehyde reductase inhibitor barbitone, as determined by fluorescence titrations [11].

References