A small, discrete acyl carrier protein is involved in de novo fatty acid biosynthesis in Streptomyces erythraeus.
A heat-stable factor, required for de novo synthesis of fatty acids in the erythromycin-producing organism Streptomyces erythraeus, has been purified to homogeneity and identified as an acyl carrier protein (ACP). We conclude that, contrary to previous belief, fatty acid synthase in S. erythraeus more closely resembles the dissociable complex of E. coli than the tightly associated, multifunctional enzyme complex found in the related actinomycete Mycobacterium smegmatis.
Hale
R S
RS
Department of Biochemistry, University of Cambridge, England.
Jordan
K N
KN
Leadlay
P F
PF
D000213:Acyl Carrier Protein / Q000235:genetics / Q000302:isolation & purification / Q000502:physiology*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics / Q000302:isolation & purification / Q000502:physiology*; D004926:Escherichia coli / Q000235:genetics; D005227:Fatty Acids / Q000096:biosynthesis*; D006358:Hot Temperature; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D013302:Streptomyces / Q000235:genetics / Q000378:metabolism*
D000213:Acyl Carrier Protein; D001426:Bacterial Proteins; D005227:Fatty Acids