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 x 10-5 and 3 x 10-5 M for rat and human liver, respectively). Methylmalonyl CoA was demonstrated to be a competitive inhibitor of malonyl CoA, with K(i) values of 2.4 x 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 |
| State | Published - 1977 |
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ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
Cite this
Comparative effects of methylmalonyl coenzyme A on fatty acid synthetase derived from rat and man. / Frenkel, E. P.; Kitchens, R. L.
In: Proceedings of the Society for Experimental Biology and Medicine, Vol. 156, No. 1, 1977, p. 151-154.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Comparative effects of methylmalonyl coenzyme A on fatty acid synthetase derived from rat and man
AU - Frenkel, E. P.
AU - Kitchens, R. L.
PY - 1977
Y1 - 1977
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 (K(m) = 4 x 10-5 and 3 x 10-5 M for rat and human liver, respectively). Methylmalonyl CoA was demonstrated to be a competitive inhibitor of malonyl CoA, with K(i) values of 2.4 x 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 (K(m) = 4 x 10-5 and 3 x 10-5 M for rat and human liver, respectively). Methylmalonyl CoA was demonstrated to be a competitive inhibitor of malonyl CoA, with K(i) values of 2.4 x 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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UR - http://www.scopus.com/inward/citedby.url?scp=0017572955&partnerID=8YFLogxK
M3 - Article
C2 - 71740
AN - SCOPUS:0017572955
VL - 156
SP - 151
EP - 154
JO - Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N. Y.)
JF - Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N. Y.)
SN - 1535-3702
IS - 1
ER -