Molecular cloning,expression and tissue distribution of hamster diacetyl reductase. Identity with l-xylulose reductase |
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| Institution: | 1. Laboratory of Biochemistry, Gifu Pharmaceutical University, 5-6-1 Mitahora-higashi, Gifu 502-8585, Japan;2. Taisho Pharmaceutical Co. Ltd., Yoshino-cho, Omiya-shi, Saitama 330-8530, Japan;1. The Wallenberg Laboratory, Department of Molecular and Clinical Medicine, University of Gothenburg, Bruna Stråket 16, 41345 Gothenburg, Sweden;2. Department of Public Health and Clinical Medicine, Umeå Stroke Centre, Umeå University, Umeå, Sweden;3. Department of Pharmacology and Clinical Neuroscience, Umeå University, Umeå, Sweden;4. Karolinska Institute Danderyds Hospital, Department of Clinical Sciences, Stockholm, Sweden;5. Department of Surgical and Perioperative Sciences, Umeå University, Umeå, Sweden;6. Department of Clinical Physiology, Sahlgrenska University Hospital, Gothenburg, Sweden;1. Department of Pharmaceutical, The First Affiliated Hospital of Guangdong Pharmaceutical University, Guangzhou, 510080, China;2. Department of Clinical Pharmacy, Guangdong Pharmaceutical University, Guangzhou, 510080, China;3. School of Traditional Chinese Medicine, Southern Medical University, 1838 North Guangzhou Avenue, Guangzhou, 510515, China;4. The Third Affiliated Hospital of Southern Medical University, Guangzhou, 510630, China |
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| Abstract: | Using rapid amplification of cDNA ends PCR, a cDNA species for diacetyl reductase (EC 1.1.1.5) was isolated from hamster liver. The encoded protein consisted of 244 amino acids, and showed high sequence identity to mouse lung carbonyl reductase and hamster sperm P26h protein, which belong to the short-chain dehydrogenase/reductase family. The enzyme efficiently reduced l-xylulose as well as diacetyl, and slowly oxidized xylitol. The Km values for l-xylulose and xylitol were similar to those reported for l-xylulose reductase (EC 1.1.1.10) of guinea pig liver. The identity of diacetyl reductase with l-xylulose reductase was demonstrated by co-purification of the two enzyme activities from hamster liver and their proportional distribution in other tissues. |
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