Horst Schulz

Professor Emeritus

Biochemistry

Tel. (212) 650-8323
Fax: (212) 650-8322
E-mail: hoschu[at]sci.ccny.cuny.edu

M.S., Ph.D. Technical University Berlin

Research

Beta Oxidation of Fatty Acids

Fatty acids are degraded by ß-oxidation in both mitochondria and peroxisomes of animal cells. Although the two organelle-specific processes are well-established, important questions about the pathways and their cooperation, the enzymes and their supramolecular organizations, and the regulation of these processes remain unanswered. It is the long-term goal of this research group to resolve these questions with the aim of providing a comprehensive and detailed view of this vital area of mammalian metabolism. The focus of our current research effort is the ß-oxidation of unsaturated and polyunsaturated fatty acids with an emphasis on reactions and reaction sequences that involve preexisting double bonds. Our experimental approaches include (1) metabolic studies with cellular extracts, isolated mitochondria, peroxisomes, and isolated cells and (2) investigations of ß-oxidation enzymes that require their purifications, their molecular cloning and mutagenesis to carry out metabolic and mechanistic studies of these enzymes. Simultaneously an investigation continues that assesses the impact of the supramolecular organization of ß-oxidation enzymes on the regulation of this process in mitochondria. These studies are expected to provide a better understanding of the dynamics of fatty acid oxidation in normal and diseased mammals.

Recent Publications

Ren, Y. and Schulz, H. 2003 Metabolic Functions of the Two Pathways of Oleate ß-Oxidation. Double Bond Metabolism During the ß-Oxidation of Oleic Acid in Rat Heart Mitochondria. J. Biol. Chem. 278, 111-116.

Hubbard, P.A., Liang, X., Schulz, H. and Kim, J.-J.P. 2003. The Crystal Structure and Catalytic Mechanism of E. coli 2,4-Dienoyl-CoA Reductase. J. Biol. Chem. 278, 37553-37560.

Ren, Y., Aguirre, J., Ntamack, A.G., Chu, C. and Schulz, H. 2004. An Alternative Pathway of Oleate ß-Oxidation in Escherichia coli Involving Hydrolysis of a Dead-end Intermediate by a Thioesterase. J. Biol. Chem. 279, 11042-11050.

Schulz, H. 2004. Fatty Acid Oxidation. In Encyclopedia of Biological Chemistry (W.J. Lennarz, W. J., and Lane, M.D., eds.) Elsevier, Oxford, Vol. 2, pp. 90-94.

Yu, W., Liang, X., Ensenauer, R.E., Vockley, J., Sweetman, L. and Schulz, H. 2004. Leaky ß-Oxidation of a trans Fatty Acid: Incomplete ß-Oxidation of Elaidic Acid Is Due to the Accumulation of 5-trans-Tetradecenoyl-CoA and Its Hydrolysis and Conversion to Tetradecenoylcarnitine in the Matrix of Rat Mitochondria. J. Biol. Chem. 279, 52160-52167.

Hubbard, P.A., Yu, W., Schulz, H. and Kim, J.-J. 2005. Domain Swapping in the Low-Similarity Isomerase/Hydratase Superfamily: The Crystal Structure of Rat Mitochondrial ³,²-Enoyl-CoA Isomerase. Protein Sci. 14, 1545-1555.

Yang, S.-Y., He, X.-Y. and Schulz, H. 2005. 3-Hydroxyacyl-CoA Dehydrogenase and Short Chain 3-Hydroxyacyl-CoA Dehydrogenase in Human Health and Disease. FEBS J. 274, 4874-4883.

Schulz, H. 2008. Oxidation of Fatty Acids in Eukaryotes. In Biochemistry of Lipids, Lipoproteins and Membranes (Vance, D. E., and Vance, J., eds.) Elsevier, Amsterdam, 5th Edn. pp. 131-154.

Tu, X., Hubbard, P.A., Kim, J.-J., and Schulz, H. 2008. Two Distinct Proton Donors at the Active Site of E. coli 2,4-Dienoyl-CoA Reductase Are Responsible for the Formation of Different Products. Biochemistry, 47, 1167-1175.

Nie, L., Ren, Y., and Schulz, H. 2008. Identification and Characterization of E. coli Thioesterase III That Functions in Fatty Acid ß-Oxidation. Biochemistry, 47, 7744-7751.

Nie, L., Ren, Y., Janakiraman, A., Smith, S., and Schulz, H. 2008. A Novel Paradigm of Fatty Acid ß-Oxidation Exemplified by the Thioesterase-dependent Partial Degradation of Conjugated Linoleic Acid That Fully Supports Growth of Escherichia coli. Biochemistry, 47, 9618-9626.

Ntamack, A.G., Karpichev, I.V., Gould, S.J., Small, G.M., and Schulz, H. 2009. Oleate ß-Oxidation in Yeast Involves Thioesterase but Not Yor180c That Is Not a Dienoyl-CoA Isomerase. Biochim. Biophys. Acta, 1791, 371-378.