Evidence for repetitive structure of the large acyl-carrier protein subunit of Escherichia coli citrate lyase.
The amino acid composition of the unusually large acyl-carrier protein subunit of citrate lyase from Escherichia coli is characteristic of a protein with a highly repetitive structure. Peptide mapping studies provide further evidence of repetitive sequences within the subunit. Only a single Pauly-positive spot is detected in the tryptic peptide map although the subunit contains 8 histidine residues. The 4 prosthetic groups covalently bound to the subunit are recovered in a single tryptic fragment in almost quantitative yield. These structural features of the large acyl-carrier protein subunit probably reflect internal gene duplications.
D001275:ATP Citrate (pro-S)-Lyase / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology*; D046911:Macromolecular Substances; D010446:Peptide Fragments / Q000032:analysis; D014357:Trypsin
D000596:Amino Acids; D046911:Macromolecular Substances; D010446:Peptide Fragments; D001275:ATP Citrate (pro-S)-Lyase; D014357:Trypsin