Comparative Effects of Methylmalonyl Coenzyme A on Fatty Acid Synthetase Derived From Rat and Man

E. P. Frenkel; R. L. Kitchens

doi:10.3181/00379727-156-39895

Comparative Effects of Methylmalonyl Coenzyme A on Fatty Acid Synthetase Derived From Rat and Man

E. P. Frenkel, R. L. Kitchens

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Abstract

The effect of methylmalonyl CoA on fatty acid synthetase activity was compared on enzyme derived from rats and man. Partially purified fatty acid synthetase from both sources was shown to be strikingly similar. Enzyme from both sources catalyzed propionyl CoA equally well (approximately 90% the rate of acetyl CoA at equimolar concentrations), giving rise to odd-chain fatty acids. Neither enzyme catalyzed methylmalonyl CoA in measurable activities over a wide range of concentrations. Michaelis constants for malonyl CoA were essentially the same (K_m = 4 × 10^-5 and 3 × 10^-5 M for rat and human liver, respectively). Methylmalonyl CoA was demon-strated to be a competitive inhibitor of malonyl CoA, with K_i values of 2.4 × 10^-5 M for the enzyme from both sources. Human liver fatty acid synthetase was immunoreactive with antiserum prepared against purified rat liver fatty acid synthetase.

Original language	English (US)
Pages (from-to)	151-154
Number of pages	4
Journal	Proceedings of the Society for Experimental Biology and Medicine
Volume	156
Issue number	1
DOIs	https://doi.org/10.3181/00379727-156-39895
State	Published - Oct 1977

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

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title = "Comparative Effects of Methylmalonyl Coenzyme A on Fatty Acid Synthetase Derived From Rat and Man",

abstract = "The effect of methylmalonyl CoA on fatty acid synthetase activity was compared on enzyme derived from rats and man. Partially purified fatty acid synthetase from both sources was shown to be strikingly similar. Enzyme from both sources catalyzed propionyl CoA equally well (approximately 90% the rate of acetyl CoA at equimolar concentrations), giving rise to odd-chain fatty acids. Neither enzyme catalyzed methylmalonyl CoA in measurable activities over a wide range of concentrations. Michaelis constants for malonyl CoA were essentially the same (Km = 4 × 10-5 and 3 × 10-5 M for rat and human liver, respectively). Methylmalonyl CoA was demon-strated to be a competitive inhibitor of malonyl CoA, with Ki values of 2.4 × 10-5 M for the enzyme from both sources. Human liver fatty acid synthetase was immunoreactive with antiserum prepared against purified rat liver fatty acid synthetase.",

author = "Frenkel, {E. P.} and Kitchens, {R. L.}",

note = "Funding Information: This work was supported by the Veterans Administration Medical Information System 1450, Southwestern Medical Foundation and the Heddens-Good Foundation. 2 ",

year = "1977",

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doi = "10.3181/00379727-156-39895",

language = "English (US)",

volume = "156",

pages = "151--154",

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AU - Frenkel, E. P.

AU - Kitchens, R. L.

N1 - Funding Information: This work was supported by the Veterans Administration Medical Information System 1450, Southwestern Medical Foundation and the Heddens-Good Foundation. 2

PY - 1977/10

Y1 - 1977/10

N2 - The effect of methylmalonyl CoA on fatty acid synthetase activity was compared on enzyme derived from rats and man. Partially purified fatty acid synthetase from both sources was shown to be strikingly similar. Enzyme from both sources catalyzed propionyl CoA equally well (approximately 90% the rate of acetyl CoA at equimolar concentrations), giving rise to odd-chain fatty acids. Neither enzyme catalyzed methylmalonyl CoA in measurable activities over a wide range of concentrations. Michaelis constants for malonyl CoA were essentially the same (Km = 4 × 10-5 and 3 × 10-5 M for rat and human liver, respectively). Methylmalonyl CoA was demon-strated to be a competitive inhibitor of malonyl CoA, with Ki values of 2.4 × 10-5 M for the enzyme from both sources. Human liver fatty acid synthetase was immunoreactive with antiserum prepared against purified rat liver fatty acid synthetase.

AB - The effect of methylmalonyl CoA on fatty acid synthetase activity was compared on enzyme derived from rats and man. Partially purified fatty acid synthetase from both sources was shown to be strikingly similar. Enzyme from both sources catalyzed propionyl CoA equally well (approximately 90% the rate of acetyl CoA at equimolar concentrations), giving rise to odd-chain fatty acids. Neither enzyme catalyzed methylmalonyl CoA in measurable activities over a wide range of concentrations. Michaelis constants for malonyl CoA were essentially the same (Km = 4 × 10-5 and 3 × 10-5 M for rat and human liver, respectively). Methylmalonyl CoA was demon-strated to be a competitive inhibitor of malonyl CoA, with Ki values of 2.4 × 10-5 M for the enzyme from both sources. Human liver fatty acid synthetase was immunoreactive with antiserum prepared against purified rat liver fatty acid synthetase.

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Comparative Effects of Methylmalonyl Coenzyme A on Fatty Acid Synthetase Derived From Rat and Man

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