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Enzymatic Characterization of Salmonella typhimurium Mannitol Dehydrogenase Expressed in Escherichia coli
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  • Journal title : The Korean Journal of Microbiology
  • Volume 48, Issue 2,  2012, pp.156-162
  • Publisher : The Microbiological Society of Korea
  • DOI : 10.7845/kjm.2012.48.2.156
 Title & Authors
Enzymatic Characterization of Salmonella typhimurium Mannitol Dehydrogenase Expressed in Escherichia coli
Jang, Myoung-Uoon; Park, Jung-Mi; Kim, Min-Jeong; Kang, Jung-Hyun; Lee, So-Won; Kim, Tae-Jip;
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A mannitol dehydrogenase (StMDH) gene was cloned from Salmonella typhimurium LT2 (KCTC 2421) and overexpressed in Escherichia coli. It has a 1,467 bp open reading frame encoding 488 amino acids with deduced molecular mass of 54 kDa, which shares approximately 36% of amino acid identity with known long-chain dehydrogenase/reductatse (LDR) family enzymes. The recombinant StMDH showed the highest activity at , and pH 5.0 and 10.0 for D-fructose reduction and D-mannitol oxidation, respectively. On the contrary, it has no activity on glucose, galactose, xylose, and arabinose. StMDH can catalyze the oxidative/reductive reactions between D-fructose and D-mannitol only in the presence of /NADH as coenzymes. These results indicate that StMDH is a typical /NADH-dependent mannitol dehydrogenase (E.C.
Salmonella typhimurium LT2;mannitol dehydrogenase;/NADH-dependent activity;
 Cited by
Sinorhizobium meliloti 유래 Mannitol Dehydrogenase 유전자의 클로닝 및 대장균 내 발현과 효소특성 규명,장명운;박정미;김민정;이소원;강정현;김태집;

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