PMID:3026317
| Citation |
Millar, G, Lewendon, A, Hunter, MG and Coggins, JR (1986) The cloning and expression of the aroL gene from Escherichia coli K12. Purification and complete amino acid sequence of shikimate kinase II, the aroL-gene product. Biochem. J. 237:427-37 |
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| Abstract |
The aroL gene encoding the enzyme shikimate kinase II was cloned from Escherichia coli K12. Construction of over-expressing strains permitted for the first time the purification to homogeneity of a monofunctional shikimate kinase. The complete amino acid sequence of shikimate kinase II was determined by a combined nucleotide and direct amino acid sequencing strategy. E. coli shikimate kinase II is a monomeric enzyme containing 173 amino acid residues with a calculated Mr 18,937. The amino acid sequence contains a region homologous with other kinases and ATP-requiring enzymes. Evidence is presented suggesting that the transcriptional start site of the aroL gene is located within a potential operator site. |
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| Keywords |
Amino Acid Sequence; Base Sequence; Cloning, Molecular; DNA, Bacterial/genetics; Escherichia coli/enzymology; Escherichia coli/genetics; Gene Expression Regulation; Genes, Bacterial; Isoenzymes/genetics; Isoenzymes/isolation & purification; Phosphotransferases/genetics; Phosphotransferases/isolation & purification; Phosphotransferases (Alcohol Group Acceptor); Transcription, Genetic |
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