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J. Biol. Chem., Vol. 265, Issue 22, 12895-12902, Aug, 1990

Nucleotide sequence of Escherichia coli asnB and deduced amino acid sequence of asparagine synthetase B

MA Scofield, WS Lewis and SM Schuster
Department of Chemistry, University of Nebraska, Lincoln 68588.

The Escherichia coli asparagine synthetase B gene (asnB) has been cloned into a temperature-sensitive, low copy plasmid, pOU71, as shown by the complementation of an E. coli asparagine auxotroph, E. coli JE6279. The nucleotide sequence of asnB and the flanking sequences were determined. The proposed coding region for the gene is 1662 nucleotides in length, and the deduced amino acid sequence of the coding region results in a protein that has a molecular weight of 62,666 and contains 554 amino acids. A promoter region is identified based on the transcription start site that was determined by primer extension experiments. Homology studies of the asnB protein sequence with the human asparagine synthetase and E. coli asparagine synthetase A protein show that there is a high degree of homology with only the human asparagine synthetase. A purF type glutamine amide transfer domain was identified upon inspection of the amino-terminal amino acid sequence of the asparagine synthetase B protein.
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