Complete amino acid sequence of chicken liver acyl carrier protein derived from the fatty acid synthase.
The acyl carrier protein domain of the chicken liver fatty acid synthase has been isolated after tryptic treatment of the synthase. The isolated domain functions as an acceptor of acetyl and malonyl moieties in the synthase-catalyzed transfer of these groups from their coenzyme A esters and therefore indicates that the acyl carrier protein domain exists in the complex as a discrete entity. The amino acid sequence of the acyl carrier protein was derived from analyses of peptide fragments produced by cyanogen bromide cleavage and trypsin and Staphylococcus aureus V8 protease digestions of the molecule. The isolated acyl carrier protein domain consists of 89 amino acid residues and has a calculated molecular weight of 10,127. The protein contains the phosphopantetheine group attached to the serine residue at position 38. The isolated acyl carrier protein peptide shows some sequence homology with the acyl carrier protein of Escherichia coli, particularly in the vicinity of the site of phosphopantetheine attachment, and shows extensive sequence homology with the acyl carrier protein from the uropygial gland of goose.
Huang
W Y
WY
Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, Texas 77030.
Stoops
J K
JK
Wakil
S J
SJ
D000213:Acyl Carrier Protein / Q000032:analysis*; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis*; D000818:Animals; D002645:Chickens; D004926:Escherichia coli / Q000201:enzymology; D064429:Fatty Acid Synthases / Q000032:analysis*; D008099:Liver / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis; D013045:Species Specificity; D014357:Trypsin
D000213:Acyl Carrier Protein; D000596:Amino Acids; D010446:Peptide Fragments; D064429:Fatty Acid Synthases; D014357:Trypsin