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Volume 270, Number 20, Issue of May 19, pp. 12226-12234, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

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Cloning, Expression, Sequence Analysis, and Site-directed Mutagenesis of the Tn5306-encoded N-(Carboxyethyl)ornithine Synthase from Lactococcus lactis K1

Jacob A. Donkersloot , John Thompson

The gene (ceo) encoding N-(carboxyethyl)ornithine synthase (EC 1.5.1.24) has been isolated from the sucrose-nisin transposon Tn5306 of Lactococcus lactis K1, sequenced, and expressed at high level in Escherichia coli. The cloned enzyme has allowed the synthesis of the novel N-carboxypropyl amino acids N-(1-carboxypropyl)-L-ornithine and N-(1-carboxypropyl)-L-lysine. Comparison of the deduced amino acid sequence of N-(1-carboxyethyl)-L-ornithine synthase (M = 35,323) to the functionally analogous octopine and nopaline synthases from crown gall tumors showed surprisingly little similarity. However, N-(1-carboxyethyl)-L-ornithine synthase and yeast saccharopine dehydrogenase exhibit homology at their N and C termini, which suggests that these two proteins constitute a distinct branch of the amino acid dehydrogenase superfamily. A centrally located 9-amino acid segment (GSGNVAQGA) in N-(1-carboxyethyl)-L-ornithine synthase is virtually identical with a sequence present in the -fold of the nucleotide binding domain of several microbial NADPH-dependent glutamate dehydrogenases. A much longer sequence of 80 residues has significant similarity to alanine dehydrogenase. Substitution of arginine 15 of N-(1-carboxyethyl)-L-ornithine synthase by lysine resulted in loss of enzyme activity.

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