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Role and organization of peroxisomal beta-oxidation.
Adv Exp Med Biol. 1999; 466:261-72.AE

Abstract

In mammals, peroxisomes are involved in breakdown of very long chain fatty acids, prostanoids, pristanic acid, dicarboxylic fatty acids, certain xenobiotics and bile acid intermediates. Substrate spectrum and specificity studies of the four different beta-oxidation steps in rat and/or in man demonstrate that these substrates are degraded by separate beta-oxidation systems composed of different enzymes. In both species, the enzymes acting on straight chain fatty acids are palmitoyl-CoA oxidase, an L-specific multifunctional protein (MFP-1) and a dimeric thiolase. In liver, bile acid intermediates undergo one cycle of beta-oxidation catalyzed by trihydroxycoprostanoyl-CoA oxidase (in rat), or branched chain acyl-CoA oxidase (in man), a D-specific multifunctional protein (MFP-2) and SCPX-thiolase. Finally, pristanic acid is degraded in rat tissues by pristanoyl-CoA oxidase, the D-specific multifunctional protein-2 and SCPX-thiolase. Although in man a pristanoyl-CoA oxidase gene is present, so far its product has not been found. Hence, pristanoyl-CoA is believed to be desaturated in human tissues by the branched chain acyl-CoA oxidase. Due to the stereospecificity of the oxidases acting on 2-methyl-branched substrates, an additional enzyme, 2-methylacyl-CoA racemase, is required for the degradation of pristanic acid and the formation of bile acids.

Authors+Show Affiliations

Katholieke Universiteit Leuven, Afdeling Farmakologie, Belgium. Paul.VanVeldhoven@med.kuleuven.ac.beNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

10709653

Citation

Van Veldhoven, P P., and G P. Mannaerts. "Role and Organization of Peroxisomal Beta-oxidation." Advances in Experimental Medicine and Biology, vol. 466, 1999, pp. 261-72.
Van Veldhoven PP, Mannaerts GP. Role and organization of peroxisomal beta-oxidation. Adv Exp Med Biol. 1999;466:261-72.
Van Veldhoven, P. P., & Mannaerts, G. P. (1999). Role and organization of peroxisomal beta-oxidation. Advances in Experimental Medicine and Biology, 466, 261-72.
Van Veldhoven PP, Mannaerts GP. Role and Organization of Peroxisomal Beta-oxidation. Adv Exp Med Biol. 1999;466:261-72. PubMed PMID: 10709653.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Role and organization of peroxisomal beta-oxidation. AU - Van Veldhoven,P P, AU - Mannaerts,G P, PY - 2000/3/10/pubmed PY - 2000/4/15/medline PY - 2000/3/10/entrez SP - 261 EP - 72 JF - Advances in experimental medicine and biology JO - Adv Exp Med Biol VL - 466 N2 - In mammals, peroxisomes are involved in breakdown of very long chain fatty acids, prostanoids, pristanic acid, dicarboxylic fatty acids, certain xenobiotics and bile acid intermediates. Substrate spectrum and specificity studies of the four different beta-oxidation steps in rat and/or in man demonstrate that these substrates are degraded by separate beta-oxidation systems composed of different enzymes. In both species, the enzymes acting on straight chain fatty acids are palmitoyl-CoA oxidase, an L-specific multifunctional protein (MFP-1) and a dimeric thiolase. In liver, bile acid intermediates undergo one cycle of beta-oxidation catalyzed by trihydroxycoprostanoyl-CoA oxidase (in rat), or branched chain acyl-CoA oxidase (in man), a D-specific multifunctional protein (MFP-2) and SCPX-thiolase. Finally, pristanic acid is degraded in rat tissues by pristanoyl-CoA oxidase, the D-specific multifunctional protein-2 and SCPX-thiolase. Although in man a pristanoyl-CoA oxidase gene is present, so far its product has not been found. Hence, pristanoyl-CoA is believed to be desaturated in human tissues by the branched chain acyl-CoA oxidase. Due to the stereospecificity of the oxidases acting on 2-methyl-branched substrates, an additional enzyme, 2-methylacyl-CoA racemase, is required for the degradation of pristanic acid and the formation of bile acids. SN - 0065-2598 UR - https://www.unboundmedicine.com/medline/citation/10709653/Role_and_organization_of_peroxisomal_beta_oxidation_ DB - PRIME DP - Unbound Medicine ER -