Isolation and Characterization of Multiforms of Aldehyde Reductase in Chicken Kidney

Hara, Akira; Deyashiki, Yoshihiro; Nakayama, Toshihiro; Sawada, Hideo

doi:10.1111/j.1432-1033.1983.tb07449.x

Cited by 21 publications

(12 citation statements)

References 46 publications

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“…Dicarbonyl compounds are substrates for monomeric aldoketo reductases (10,11,39) and carbonyl reductase (40), as well as dimeric dihydrodiol dehydrogenase (11) and sepiapterine reductase (41), in addition to tetrameric diacetyl reductase (21,42,43) purified from animal tissues. Of these enzymes, diacetyl reductase resembles DCXR with respect to the tetrameric structure, pH optimum, and substrate specificity, including the kinetic constants for various carbonyl compounds.…”

Section: Discussionmentioning

confidence: 99%

Molecular Characterization of Mammalian Dicarbonyl/l-Xylulose Reductase and Its Localization in Kidney

Nakagawa¹,

Ishikura²,

Asami³

et al. 2002

Journal of Biological Chemistry

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146

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In this report, we first cloned a cDNA for a protein that is highly expressed in mouse kidney and then isolated its counterparts in human, rat hamster, and guinea pig by polymerase chain reaction-based cloning. The cDNAs of the five species encoded polypeptides of 244 amino acids, which shared more than 85% identity with each other and showed high identity with a human sperm 34-kDa protein, P34H, as well as a murine lungspecific carbonyl reductase of the short-chain dehydrogenase/reductase superfamily. In particular, the human protein is identical to P34H, except for one amino acid substitution. The purified recombinant proteins of the five species were about 100-kDa homotetramers with NADPH-linked reductase activity for ␣-dicarbonyl compounds, catalyzed the oxidoreduction between xylitol and L-xylulose, and were inhibited competitively by nbutyric acid. Therefore, the proteins are designated as dicarbonyl/L-xylulose reductases (DCXRs). The substrate specificity and kinetic constants of DCXRs for dicarbonyl compounds and sugars are similar to those of mammalian diacetyl reductase and L-xylulose reductase, respectively, and the identity of the DCXRs with these two enzymes was demonstrated by their co-purification from hamster and guinea pig livers and by protein sequencing of the hepatic enzymes. Both DCXR and its mRNA are highly expressed in kidney and liver of human and rodent tissues, and the protein was localized primarily to the inner membranes of the proximal renal tubules in murine kidneys. The results imply that P34H and diacetyl reductase (EC 1.1.1.5) are identical to Lxylulose reductase (EC 1.1.1.10), which is involved in the uronate cycle of glucose metabolism, and the unique localization of the enzyme in kidney suggests that it has a role other than in general carbohydrate metabolism.

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Section: Discussionmentioning

confidence: 99%

Molecular Characterization of Mammalian Dicarbonyl/l-Xylulose Reductase and Its Localization in Kidney

Nakagawa¹,

Ishikura²,

Asami³

et al. 2002

Journal of Biological Chemistry

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146

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“…These include the regulation of the pro-inflammatory response via the reduction of aldehyde phospholipids [1], the synthesis of metabolically vital compounds such as prostaglandins [2,3] and the modulation and modification of steroids in vivo [4 -7], which include progesterone signalling in breast mammary cells [8]. Members of the AKR superfamily are composed of approximately 315 -330 residues, which generally form monomeric proteins with a molecular weight of 36 kDa [9,10]. While ALR1 prefers the reduction of aromatic rather than aliphatic aldehydes [11], both ALR1 and ALR2 catalyse the NADPHdependent reduction of aldehydes, xenobiotic aldehydes, ketones, trioses and triose phosphates [9, 10, 12 -15].…”

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confidence: 99%

Selectivity determinants of the aldose and aldehyde reductase inhibitor-binding sites

El‐Kabbani

Podjarny

2007

Cell. Mol. Life Sci.

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Aldose reductase and aldehyde reductase belong to the aldo-keto reductase superfamily of enzymes whose members are responsible for a wide variety of biological functions. Aldose reductase has been identified as the first enzyme involved in the polyol pathway of glucose metabolism which converts glucose into sorbitol. Glucose over-utilization through the polyol pathway has been linked to tissue-based pathologies associated with diabetes complications, which make the development of a potent aldose reductase inhibitor an obvious and attractive strategy to prevent or delay the onset and progression of the complications. Structural studies of aldose reductase and the homologous aldehyde reductase in complex with inhibitor were carried out to explain the difference in the potency of enzyme inhibition. The aim of this review is to provide a comprehensive summary of previous studies to aid the development of aldose reductase inhibitors that may have less toxicity problems than the currently available ones.

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“…Beef liver was prepared as a 33% homogenate in 10 mM sodium phosphate buffer (PH 8.0) containing 1 mM EDTA and 155 mM KC1 and fractionated by the method of Hara et al [13]. Lactate dehydrogenase, cytochrome c reductase and glutamate dehydrogenase were used as marker enzymes.…”

Section: Subcellular Localization Of Enzyme Activitiesmentioning

confidence: 99%

Characterization of an enzyme which catalyzes isomerization and epimerization of d‐erythrose 4‐phosphate

Terada

Mukae

Ohashi

et al. 1985

European Journal of Biochemistry

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The enzyme which catalyzes the conversion of D-erythrose 4-phosphate to D-erythrulose 4-phosphate and D-threose 4-phosphate has been purified to homogeneity from a crude extract of beef liver. Analysis of the purified enzyme by Sephadex G-100 gel filtration and sodium dodecyl sulfate/polyacrylamide gel electrophoresis revealed it to be a dimer of relative molecular mass 43000. From the gas chromatography/mass spectrometry analyses of the enzymatic reaction products, it appeared that about 90% of the total amount of tetrose 4-phosphate was present as D-erythrulose 4-phosphate after equilibration. The purified enzyme, which is tentatively called 'erythrose-4-phosphate isomerase' had no significant isomerase activities on D-glyceraldehyde 3-phosphate, D-ribose 5-phosphate, D-glucose 6-phosphate and D-fructose 6-phosphate, but a strong ~-ribulose-5-phosphate 3-epimerase activity was co-purified with the erythrose-4-phosphate isomerase activity through every step in the isolation. Both the erythrose-4-phosphate isomerase and ~-ribulose-5-phosphate 3-epimerase activities were inactivated at the same rate at the elevated temperature, and also inhibited to the same extent by various inhibitors. It is likey, that both activities are catalyzed by the single enzyme protein.We have reported previously the purification and properties of D-erythrulose reductase (EC 1.1.1.1 62) [I, 21 and aldehyde reductase (EC 1.1.1.2) [3], which catalyze the reduction of D-erythrulose and D-erythrose respectively. These enzymes were considered to be important with respect to the tetrose metabolism. In the continuing efforts from this laboratory to understand how the naturally occurring tetritols, such as erythritol and threitol excreted in urine, are synthesized we recently found an enzyme catalyzing both isomerization and epimerization of D-erythrose 4-phosphate (Ery4P) to D-erythrulose 4-phosphate and D-threose 4-phosphate in beef liver [4]. This enzyme could be described as erythrose-4-phosphate (Ery4P) isomerase since it was able to catalyze the isomerization of Ery4P to the major product, D-erythrulose 4-phosphate. Since other mammalian enzymes catalyzing such a reaction have not been reported until now, this enzyme has been the subject of extensive research by our laboratory.In the present report we describe the characterization of a highly purified enzyme having both the Ery4P isomerase and epimerase activities from beef liver, and discuss the mechanism

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Isolation and Characterization of Multiforms of Aldehyde Reductase in Chicken Kidney

Cited by 21 publications

References 46 publications

Molecular Characterization of Mammalian Dicarbonyl/l-Xylulose Reductase and Its Localization in Kidney

Molecular Characterization of Mammalian Dicarbonyl/l-Xylulose Reductase and Its Localization in Kidney

Selectivity determinants of the aldose and aldehyde reductase inhibitor-binding sites

Characterization of an enzyme which catalyzes isomerization and epimerization of d‐erythrose 4‐phosphate

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