Article
Characterization of ligV essential for catabolism of vanillin by Sphingomonas paucimobilis SYK-6.
Bioscience, biotechnology, and biochemistry - 1 Oct 2007
Masai Eiji, Yamamoto Yuko, Inoue Tomohiko, Takamura Kazuhiro, Hara Hirofumi, Kasai Daisuke, Katayama Yoshihiro, Fukuda Masao
Abstract excerpt
The vanillin dehydrogenase gene (ligV), which conferred the ability to transform vanillin into vanillate on Escherichia coli, was isolated from Sphingomonas paucimobilis SYK-6. The ligV gene consists of a 1,440-bp open reading frame encoding a polypeptide with a molecular mass of 50,301 Da. The deduced amino acid sequence of ligV showed about 50% identity with the known vanillin dehydrogenases of Pseudomonas...
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