Purification and characterization of 4-N-trimethylamino-1-butanol dehydrogenase of Pseudomonas sp. 13CM

…, S Morimoto, H Murakami, T Ichiyanagi…

Index: Hassan, Maizom; Morimoto, Sachiko; Murakami, Hiroyuki; Ichiyanagi, Tsuyoshi; Mori, Nobuhiro Bioscience, Biotechnology and Biochemistry, 2007 , vol. 71, # 6 p. 1439 - 1446

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Citation Number: 11

Abstract

A new enzyme, NAD+-dependent 4-N-trimethylamino-1-butanol dehydrogenase from Pseudomonas sp. 13CM, was purified 526-fold to apparent homogeneity in 5 chromatographic steps. The enzyme had a molecular mass of 45 kDa and appeared to be a monomer enzyme. The isoeletric point was found to be 4.8. The optimum temperature was 50° C, and the optimum pHs for the oxidation and reduction reactions were 9.5 and 6.0 ...