Molecular analysis of the Corynebacterium glutamicum transketolase gene
1999
Ikeda, M. (Kyowa Hakko Kogyo Co. Ltd., Hofu, Yamaguchi (Japan). Hofu Plant) | Kamada, N. | Takano, Y. | Nakano, T.
Transketolase is important in production of the aromatic amino acids in Corynebacterium glutamicum. The complete nucleotide sequence of the C. glutamicum transketolase gene has been identified. The DNA-derived protein sequence is highly similar to the transketolase of Mycobacterium tuberculosis, taxonomically related to C. glutamicum. The alignment of the N-terminus regions between both transketolases showed TTG to be the most probable start codon. Potential ribosomal binding and promoter regions were situated upstream from the TTG. The deduced amino acid sequence consists of 700 residues with a calculated molecular mass of 75 kDa, and contains all amino acid residues involved in cofactor and substrate binding in the well-characterized yeast transketolase sequence
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