T
Toshihiro Nakayama
Researcher at Gifu Pharmaceutical University
Publications - 68
Citations - 1455
Toshihiro Nakayama is an academic researcher from Gifu Pharmaceutical University. The author has contributed to research in topics: Enzyme & Dehydrogenase. The author has an hindex of 22, co-authored 68 publications receiving 1446 citations.
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Journal ArticleDOI
Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder.
Yoshihiro Deyashiki,Akihito Ogasawara,Toshihiro Nakayama,Masayuki Nakanishi,Yoshiyuki Miyabe,Kumiko Sato,Akira Hara +6 more
TL;DR: A computer-based comparison of the c DNAs of the isoenzymes with the DNA sequence database revealed that the nucleotide and amino acid sequences of DD2 and DD4 are virtually identical with those of human bile-acid binder and human chlordecone reductase cDNAs respectively.
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Purification and properties of multiple forms of dihydrodiol dehydrogenase from human liver.
TL;DR: Five basic enzymes purified from human liver oxidized alicyclic alcohols as well as the dihydrodiols using both NADP+ and NAD+ as cofactors, but showed differences in specificity for hydroxysteroids and inhibitor sensitivity.
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Reductases for carbonyl compounds in human liver.
TL;DR: Comparison of kinetic constants for aldehydes among the enzymes indicated that alcohol dehydrogenase is the best reductase with the highest affinity and Kcat values.
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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.
Kumiko Sato,Ayako Inazu,Shiho Yamaguchi,Toshihiro Nakayama,Yoshihiro Deyashiki,Hideo Sawada,Akira Hara +6 more
TL;DR: In this article, the NADPH-dependent enzyme activity was detected in the extracts of various monkey tissues, among which kidney exhibited the highest specific activity and was immunochemically identical to dimeric dihydrodiol dehydrogenase of monkey kidney.
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Structural and functional comparison of two human liver dihydrodiol dehydrogenases associated with 3 alpha-hydroxysteroid dehydrogenase activity.
Yoshihiro Deyashiki,Hiroyuki Taniguchi,Tetsuya Amano,Toshihiro Nakayama,Akira Hara,Hideo Sawada +5 more
TL;DR: Two monomeric dihydrodiol dehydrogenases with pI values of 5.4 and 7.6 were co-purified with androsterone dehydrogenase activity to homogeneity from human liver.