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Title: Cloning and expression of the sarcosine oxidase gene from Bacillus sp. NS-129 in Escherichia coli. Author: Koyama Y, Yamamoto-Otake H, Suzuki M, Nakano E. Journal: Agric Biol Chem; 1991 May; 55(5):1259-63. PubMed ID: 1368683. Abstract: The gene coding for a thermostable sarcosine oxidase (EC 1.5.3.1) was isolated from Bacillus sp. NS-129. The primary structure of sarcosine oxidase deduced from the nucleotide sequence was a protein composed of 387 amino acids with molecular weight 42,955. When the sarcosine oxidase was overproduced to about 35% of soluble protein in E. coli under the control of a lac promoter, the sarcosine oxidase activity of the crude extract was increased 3-fold by the addition of FAD. This indicates that most of the enzyme is accumulated in an active form, a flavinless aporotein, in the cell.[Abstract] [Full Text] [Related] [New Search]