Carbonyl reductase activity of sepiapterin reductase from rat erythrocytes

Sueoka, Terumi; Katoh, Shigeo

doi:10.1016/0304-4165(85)90139-4

Cited by 44 publications

(19 citation statements)

References 30 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

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

146

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“…7) In addition, several cytosolic enzymes that metabolize endogenous substrates exhibit CR activity. These include tetrameric dicarbonyl/L-xylulose reductase, 8) dimeric sepiapterin reductase, 9) dimeric aflatoxin B 1 aldehyde reductase, 10) monomeric 3a-and 17b-hydroxysteroid dehydrogenases 11,12) and monomeric prostaglandin F synthase. 13) While L-xylulose reductase and sepiapterin reductase are members of the SDR family, the other four enzymes belong to the aldo-keto reductase (AKR) superfamily.…”

mentioning

confidence: 99%

Characterization of an Oligomeric Carbonyl Reductase of Dog Liver: Its Identity with Peroxisomal Tetrameric Carbonyl Reductase

Endo

Matsunaga

Nagano

et al. 2007

Biological & Pharmaceutical Bulletin

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“…It is physiologically significant that the rate of activation of these fragments was more remarkable when the natural cofactor, BH 4 was used as the source of the substrate than when the synthesized cofactor, 6M-PH 4 was used (Table 2). Like SPR (Katoh and Sueoka, 1984;Sueoka and Katoh, 1985), DHPR was demonstrated to be a member of the short-chain dehydrogenase/reductase superfamily, based on its NAD(P)H requirement and primary structure (Jornvall et al, 1995). The enzymes of this family generally have a coenzyme-binding domain in their N-terminal region and a unique segment in their C-terminal region, for individual function, containing conserved residues of the essential motif Tyr-X-X-X-Lys.…”

Section: Discussionmentioning

confidence: 99%

Transient Activation of Dihydropteridine Reductase by Ca2+-activated Proteolysis.

Kawai¹,

Fujimoto²,

Okamoto³

et al. 2000

Zoolog Sci

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Carbonyl reductase activity of sepiapterin reductase from rat erythrocytes

Cited by 44 publications

References 30 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

Characterization of an Oligomeric Carbonyl Reductase of Dog Liver: Its Identity with Peroxisomal Tetrameric Carbonyl Reductase

Transient Activation of Dihydropteridine Reductase by Ca2+-activated Proteolysis.

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