PMID:6749498
| Citation |
Valentin-Hansen, P, Boëtius, F, Hammer-Jespersen, K and Svendsen, I (1982) The primary structure of Escherichia coli K12 2-deoxyribose 5-phosphate aldolase. Nucleotide sequence of the deoC gene and the amino acid sequence of the enzyme. Eur. J. Biochem. 125:561-6 |
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| Abstract |
The sequence of the deoC gene of Escherichia coli K12 and the amino acid sequence of the corresponding protein, deoxyriboaldolase, has been established. The protein consists of 259 amino acids with a molecular weight of 27 737. The purified enzyme may exist both as a monomer and as a dimer. On the basis of amino acid composition, molecular weight and catalytic properties, the enzymes from E. coli and Salmonella typhimurium seem to be almost similar. They belong to the class I aldolases, which form Schiff base intermediates. Using data for the S. typhimurium enzyme, the lysine residue involved in the active site in the E. coli enzyme was tentatively identified. |
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| Keywords |
Aldehyde-Lyases/genetics; Amino Acid Sequence; Bacterial Proteins/analysis; Base Sequence; Chromatography, Gel; Escherichia coli/enzymology; Escherichia coli/genetics; Genes, Bacterial; Molecular Weight; Plasmids |
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