Guinea-pig liver testosterone 17 β-dehydrogenase (NADP+) and aldehyde reductase exhibit benzene dihydrodiol dehydrogenase activity

Hara, Akira; Hayashibara, Masakazu; Nakayama, Toshihiro; Hasebe, Kazuhisa; Usui, Shigeyuki; Sawada, Hideo

doi:10.1042/bj2250177

Cited by 21 publications

(15 citation statements)

References 18 publications

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“…21. LXylulose reductase was purified from male Hartley guinea pig livers (50 g) essentially according to the same procedures employed for the purification of hamster diacetyl reductase.…”

Section: Methodsmentioning

confidence: 99%

“…The recombinant DCXRs were purified from the cell extract according to the procedures for purification of hamster liver diacetyl reductase (21), except that a Matrex Red A (Amicon, Beverly, MA) column was used instead of the Blue-Sepharose column. The adsorbed DCXR was eluted from the Matrex Red A column with buffer containing 0.5 mM NADP ϩ .…”

Section: Methodsmentioning

confidence: 99%

“…Each of the cDNA species contained a stop codon (TGA or TAA), a polyadenylation signal sequence, the poly(A) sequence, and the characteristic sequence around the first ATG codon. The cDNA species for hamster and guinea pig DCXRs could also be isolated by RT-PCR and RACE from the total RNA samples of the livers, because the recombinant DCXRs exhibited the activities of diacetyl reductase and L-xylulose reductase (as described below), which have been purified from the livers of the two animals (21,26).…”

Section: Cloning Of Cdna Species For Rodent and Human Dcxrs-inmentioning

confidence: 99%

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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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“…21. LXylulose reductase was purified from male Hartley guinea pig livers (50 g) essentially according to the same procedures employed for the purification of hamster diacetyl reductase.…”

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Cloning Of Cdna Species For Rodent and Human Dcxrs-inmentioning

confidence: 99%

See 1 more Smart Citation

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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show abstract

“…The immunoprecipitation of reductase activities towards aromatic ketones, isatin and all-trans-retinal in the liver extract by the anti-pig PTCR antibody was performed as described previously. 25) RESULTS AND DISCUSSION Properties of Dog Liver CR From 50 g dog liver, 5.1 mg of CR was purified in a yield of 57%, and it exhibited a specific activity of 35 U/mg with 5 mM 4-benzoylpyridine as the substrate. The specific activity and kinetic constants for valerophenone, n-butyrophenone and 4-benzoylpyridine of this enzyme preparation (Table 2) are essentially identical to those of the dog liver CR reported previously.…”

Section: )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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“…The enzyme exists in multiple forms in mammalian tissues. Most of the enzymes purified from various mammalian tissues are monomeric and have been shown to be identical with 3α-, 17β-and 20α-hydroxysteroid dehydrogenases, aldehyde reductase and\or aldose reductase [5][6][7][8][9][10], which are members of the aldo-keto reductase superfamily [11]. In addition to the monomeric enzymes, dimeric DDs composed of 39 kDa subunits have been isolated from rabbit lens [10], monkey kidney [12,13], pig tissues [14] and dog liver [15].…”

Section: Introductionmentioning

confidence: 99%

Cloning and sequencing of the cDNA species for mammalian dimeric dihydrodiol dehydrogenases

Arimitsu

Aoki

Ishikura

et al. 1999

Biochemical Journal

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Cynomolgus and Japanese monkey kidneys, dog and pig livers and rabbit lens contain dimeric dihydrodiol dehydrogenase (EC 1.3.1.20) associated with high carbonyl reductase activity. Here we have isolated cDNA species for the dimeric enzymes by reverse transcriptase-PCR from human intestine in addition to the above five animal tissues. The amino acid sequences deduced from the monkey, pig and dog cDNA species perfectly matched the partial sequences of peptides digested from the respective enzymes of these animal tissues, and active recombinant proteins were expressed in a bacterial system from the monkey and human cDNA species. Northern blot analysis revealed the existence of a single 1.3 kb mRNA species for the enzyme in these animal tissues. The human enzyme shared 94%, 85%, 84% and 82% amino acid identity with the enzymes of the two monkey strains (their sequences were identical), the dog, the pig and the rabbit respectively. The sequences of the primate enzymes consisted of 335 amino acid residues and lacked one amino acid compared with the other animal enzymes. In contrast with previous reports that other types of dihydrodiol dehydrogenase, carbonyl reductases and enzymes with either activity belong to the aldo-keto reductase family or the short-chain dehydrogenase/reductase family, dimeric dihydrodiol dehydrogenase showed no sequence similarity with the members of the two protein families. The dimeric enzyme aligned with low degrees of identity (14-25%) with several prokaryotic proteins, in which 47 residues are strictly or highly conserved. Thus dimeric dihydrodiol dehydrogenase has a primary structure distinct from the previously known mammalian enzymes and is suggested to constitute a novel protein family with the prokaryotic proteins.

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Guinea-pig liver testosterone 17 β-dehydrogenase (NADP+) and aldehyde reductase exhibit benzene dihydrodiol dehydrogenase activity

Cited by 21 publications

References 18 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

Cloning and sequencing of the cDNA species for mammalian dimeric dihydrodiol dehydrogenases

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