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Notes For: 3-ketoacyl-CoA thiolase (FadA) is involved in the degradation of fatty acids via the β-oxidation cycle. It has broad chain-length specificity for substrates, but exhibits its highest activity with medium-chain substrates.
FadA and FadB form a multifunctional enzyme complex |CITS: [334745][6402028][3286611][8454629]| (data from E. coli B in |CITS: [7012144][6350283]|).
Overexpression of FadA and FadB can be utilized for the production of long-chain fatty acids in an engineered reversal of the β-oxidation cycle |CITS: [21832992][23656231]|.
Expression of the enzymes involved in β-oxidation is normally induced by fatty acids of chain length 14 and longer |CITS: [4861587][4886296][18317523]|. Regulation is at the transcriptional level and involves repression by FadR |CITS: [6271734]|.
OldA: oleate degradation A (old-30) |CITS: [4861587][4928881]|
FadA: fatty acid degradation A |CITS: [4563344]|      


Reference(s):  
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[6] Klein K., Steinberg R., Fiethen B., Overath P., 1971, Fatty acid degradation in Escherichia coli. An inducible system for the uptake of fatty acids and further characterization of old mutants., Eur J Biochem 19(3):442-50
[7] Pramanik A., Schulz H., 1983, Multienzyme complexes of fatty acid oxidation from Escherichia coli K12 and from a mutant with a defective L-3-hydroxyacyl coenzyme A dehydrogenase., Biochim Biophys Acta 750(1):41-6
[8] Pauli G, Overath P, 1972, ato Operon: a highly inducible system for acetoacetate and butyrate degradation in Escherichia coli., Eur J Biochem, 29(3):553 10.1111/j.1432-1033.1972.tb02021.x
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