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Monkey 3-deoxyglucosone reductase: tissue distribution and purification of three multiple forms of the kidney enzyme that are identical with dihydrodiol dehydrogenase, aldehyde reductase, and aldose reductase.
Arch Biochem Biophys. 1993 Dec; 307(2):286-94.AB

Abstract

3-Deoxyglucosone (3DG) is a reactive intermediate in the glucose-mediated cross-linking of proteins. An enzyme catalyzing the reduction of 3DG is thought to prevent the damage to protein by the formation of 3DG. The NADPH-dependent enzyme activity was detected in the extracts of various monkey tissues, among which kidney exhibited the highest specific activity. One dimeric enzyme with subunit M(r) of 39,000 and two monomeric enzymes with M(r) of 38,000 and 34,000 were purified from monkey kidney. The dimeric enzyme exhibited high dihydrodiol dehydrogenase activity and was immunochemically identical to dimeric dihydrodiol dehydrogenase of monkey kidney. The two monomeric enzymes exhibited aldehyde reductase activity, but were clearly distinct from each other in substrate specificity, inhibitor sensitivity, and effect of sulfate ions. One enzyme was immunologically cross-reacted with human liver aldehyde reductase, whereas sequence data of digested peptides from the other enzyme revealed > 97% identity with human placental aldose reductase. Comparison of kinetic constants among the monkey kidney enzymes and aldoketo reductases from several mammalian tissues indicated that dimeric dihydrodiol dehydrogenase and aldose reductase exhibited higher catalytic efficiency for 3DG than did aldehyde reductase, carbonyl reductase, and monomeric dihydrodiol dehydrogenase.

Authors+Show Affiliations

Laboratory of Biochemistry, Gifu Pharmaceutical University, Japan.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

8274014

Citation

Sato, K, et al. "Monkey 3-deoxyglucosone Reductase: Tissue Distribution and Purification of Three Multiple Forms of the Kidney Enzyme That Are Identical With Dihydrodiol Dehydrogenase, Aldehyde Reductase, and Aldose Reductase." Archives of Biochemistry and Biophysics, vol. 307, no. 2, 1993, pp. 286-94.
Sato K, Inazu A, Yamaguchi S, et al. Monkey 3-deoxyglucosone reductase: tissue distribution and purification of three multiple forms of the kidney enzyme that are identical with dihydrodiol dehydrogenase, aldehyde reductase, and aldose reductase. Arch Biochem Biophys. 1993;307(2):286-94.
Sato, K., Inazu, A., Yamaguchi, S., Nakayama, T., Deyashiki, Y., Sawada, H., & Hara, A. (1993). Monkey 3-deoxyglucosone reductase: tissue distribution and purification of three multiple forms of the kidney enzyme that are identical with dihydrodiol dehydrogenase, aldehyde reductase, and aldose reductase. Archives of Biochemistry and Biophysics, 307(2), 286-94.
Sato K, et al. Monkey 3-deoxyglucosone Reductase: Tissue Distribution and Purification of Three Multiple Forms of the Kidney Enzyme That Are Identical With Dihydrodiol Dehydrogenase, Aldehyde Reductase, and Aldose Reductase. Arch Biochem Biophys. 1993;307(2):286-94. PubMed PMID: 8274014.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Monkey 3-deoxyglucosone reductase: tissue distribution and purification of three multiple forms of the kidney enzyme that are identical with dihydrodiol dehydrogenase, aldehyde reductase, and aldose reductase. AU - Sato,K, AU - Inazu,A, AU - Yamaguchi,S, AU - Nakayama,T, AU - Deyashiki,Y, AU - Sawada,H, AU - Hara,A, PY - 1993/12/1/pubmed PY - 1993/12/1/medline PY - 1993/12/1/entrez SP - 286 EP - 94 JF - Archives of biochemistry and biophysics JO - Arch. Biochem. Biophys. VL - 307 IS - 2 N2 - 3-Deoxyglucosone (3DG) is a reactive intermediate in the glucose-mediated cross-linking of proteins. An enzyme catalyzing the reduction of 3DG is thought to prevent the damage to protein by the formation of 3DG. The NADPH-dependent enzyme activity was detected in the extracts of various monkey tissues, among which kidney exhibited the highest specific activity. One dimeric enzyme with subunit M(r) of 39,000 and two monomeric enzymes with M(r) of 38,000 and 34,000 were purified from monkey kidney. The dimeric enzyme exhibited high dihydrodiol dehydrogenase activity and was immunochemically identical to dimeric dihydrodiol dehydrogenase of monkey kidney. The two monomeric enzymes exhibited aldehyde reductase activity, but were clearly distinct from each other in substrate specificity, inhibitor sensitivity, and effect of sulfate ions. One enzyme was immunologically cross-reacted with human liver aldehyde reductase, whereas sequence data of digested peptides from the other enzyme revealed > 97% identity with human placental aldose reductase. Comparison of kinetic constants among the monkey kidney enzymes and aldoketo reductases from several mammalian tissues indicated that dimeric dihydrodiol dehydrogenase and aldose reductase exhibited higher catalytic efficiency for 3DG than did aldehyde reductase, carbonyl reductase, and monomeric dihydrodiol dehydrogenase. SN - 0003-9861 UR - https://www.unboundmedicine.com/medline/citation/8274014/Monkey_3_deoxyglucosone_reductase:_tissue_distribution_and_purification_of_three_multiple_forms_of_the_kidney_enzyme_that_are_identical_with_dihydrodiol_dehydrogenase_aldehyde_reductase_and_aldose_reductase_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0003-9861(83)71591-2 DB - PRIME DP - Unbound Medicine ER -