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.
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.
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004269:DNA, Bacterial / Q000235:genetics; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D005786:Gene Expression Regulation; D005798:Genes, Bacterial; D007527:Isoenzymes / Q000235:genetics* / Q000302:isolation & purification; D010770:Phosphotransferases / Q000235:genetics* / Q000302:isolation & purification; D017853:Phosphotransferases (Alcohol Group Acceptor); D014158:Transcription, Genetic
D004269:DNA, Bacterial; D007527:Isoenzymes; D010770:Phosphotransferases; D017853:Phosphotransferases (Alcohol Group Acceptor); C022642:shikimate kinase