Abstract
A one-carbon degradation of long-chain fatty acids, which was found to occur in the brains of rats in vivo, has been investigated in a brain microsomal fraction in vitro. Decarboxylation of the α-hydroxy acid, a possible intermediate product between the substrate and the next shorter acid, in the presence of brain microsomal fraction was enhanced by ATP, NAD, and a dialyzable fraction from the supernatant fraction. The cofactor requirement for the decarboxylation of the α-hydroxy acids provided by the dialyzable fraction can be met by several reducing agents or ferrous ion. The effectiveness of several possible cofactors for the decarboxylation of α-hydroxy acids has been evaluated.
It is concluded that the decarboxylation of the α-hydroxystearic acid may be a reaction with molecular oxygen catalyzed by an oxidase or oxygenase that requires iron in the reduced state for activity. The possibility that the reaction proceeds through an α-keto acid intermediate has been examined in the light of new knowledge of the conditions for decarboxylation. It is concluded that a short-lived keto acid is a possible intermediate. Definitive proof however is lacking because the characteristics of the reaction require that such an intermediate decarboxylate without dissociating from the enzyme.
Similar content being viewed by others
References
Levis, G. M., and J. F. Mead, J. Biol. Chem.239, 77–80 (1964).
Mead, J. F., and G. M. Levis, J. Biol. Chem.238, 1634–1636 (1963).
Muller, A., and I. Binzer, Chem. Ber.72B, 615–619 (1939).
Anker, H. S., J. Biol. Chem.194, 177–182 (1952).
Criegee, R., L. Kraft and B. Rank, Ann.507, 159–197 (1933).
Levis, G. M., Biochim. Biophys. Acta99, 194–197 (1965).
Davies, W. E., A. K. Hajra, S. S. Parmar, N. S. Radin and J. F. Mead, J. Lipid Res.1 270–276, (1968).
Kaufman, S., and B. Levenberg, J. Biol. Chem.234, 2683–2688 (1959).
Stumpf, P. K., Nature194, 1158–1160, (1962).
Hayaishi, O., in “Oxygenases,” ed. O. Hayaishi, Academic Press, New York, 1962.
Yamamoto,et al., in: “Biological and Chemical Aspects of Oxygenases,” K. Bloch and O. Hayaishi, eds., Maruzen, Tokyo, 1968, p. 303.
Nozali, M.,et al., Ibid. “ K. Bloch and O. Hayaishi, eds., Maruzen, Tokyo, 1968, p. 347.
Dixon, M., and E. C. Webb, “The Enzymes,” Academic Press, New York, 1964, p. 407.
Orr, C. W. M., Biochem. Biophys. Res. Comm.23, 854–860 (1968).
Sutton, W.B., J. Biol. Chem.226, 395–405 (1957).
Robinson, J. C., L. Keay, R. Molinari and I. W. Sizer, J. Biol. Chem.237, 2001–2010 (1962).
Charalampous, F. C., J. Biol. Chem.235, 1286–1291 (1960).
Author information
Authors and Affiliations
Additional information
These studies were supported in part by Contract AT (04-1) GEN-12 between the Atomic Energy Commission and the University of California.
Supported in part by Grant He-5306 from the U.S. Public Health Service.
Supported in part by USPHS Research Career Award GM-K6-19, 177 from the Division of General Medical Sciences.
About this article
Cite this article
Macdonald, R.C., Mead, J.F. Thealpha-oxidation system of brain microsomes. Cofactors foralpha-hydroxy acid decarboxylation. Lipids 3, 275–283 (1968). https://doi.org/10.1007/BF02531201
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF02531201