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The CoA esters of 2-methyl-branched chain fatty acids and of the bile acid intermediates di- and trihydroxycoprostanic acids are oxidized by one single peroxisomal branched chain acyl-CoA oxidase in human liver and kidney.
J Biol Chem. 1993 May 15; 268(14):10335-44.JB

Abstract

Rat liver peroxisomes contain three acyl-CoA oxidases: palmitoyl-CoA oxidase, which oxidizes the CoA esters of straight chain fatty acids and prostaglandins; pristanoyl-CoA oxidase, which oxidizes the CoA esters of 2-methyl-branched fatty acids (e.g. pristanic acid); and trihydroxycoprostanoyl-CoA oxidase, which oxidizes the CoA esters of the bile acid intermediates di- and trihydroxycoprostanic acids (Van Veldhoven, P. P., Vanhove, G., Asselberghs, S., Eyssen, H. J., and Mannaerts, G. P. (1992) J. Biol. Chem. 267, 20065-20074). In the present report we demonstrate that human liver peroxisomes contain only two acyl-CoA oxidases: palmitoyl-CoA oxidase, which oxidizes the CoA esters of straight chain fatty acids and prostaglandins, and a novel branched chain acyl-CoA oxidase, which oxidizes the CoA esters of 2-methyl-branched fatty acids as well as those of the bile acid intermediates (which also possess a 2-methyl substitution in their side chains). The branched chain acyl-CoA oxidase was purified to near homogeneity by means of column chromatography. It appeared to be a 70-kDa monomeric protein that did not cross-react with antisera raised against rat palmitoyl-CoA oxidase and pristanoyl-CoA oxidase. No indication was found for the presence of a separate trihydroxycoprostanoyl-CoA oxidase in human liver. The branched chain acyl-CoA oxidase was present also in human kidney, suggesting that it is expressed in other extrahepatic tissues as well. Our results explain a number of clinical-chemical observations made in certain cases of peroxisomal beta-oxidation disorders.

Authors+Show Affiliations

Katholieke Universiteit Leuven, Afdeling Farmacologie, Belgium.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

8387517

Citation

Vanhove, G F., et al. "The CoA Esters of 2-methyl-branched Chain Fatty Acids and of the Bile Acid Intermediates Di- and Trihydroxycoprostanic Acids Are Oxidized By One Single Peroxisomal Branched Chain acyl-CoA Oxidase in Human Liver and Kidney." The Journal of Biological Chemistry, vol. 268, no. 14, 1993, pp. 10335-44.
Vanhove GF, Van Veldhoven PP, Fransen M, et al. The CoA esters of 2-methyl-branched chain fatty acids and of the bile acid intermediates di- and trihydroxycoprostanic acids are oxidized by one single peroxisomal branched chain acyl-CoA oxidase in human liver and kidney. J Biol Chem. 1993;268(14):10335-44.
Vanhove, G. F., Van Veldhoven, P. P., Fransen, M., Denis, S., Eyssen, H. J., Wanders, R. J., & Mannaerts, G. P. (1993). The CoA esters of 2-methyl-branched chain fatty acids and of the bile acid intermediates di- and trihydroxycoprostanic acids are oxidized by one single peroxisomal branched chain acyl-CoA oxidase in human liver and kidney. The Journal of Biological Chemistry, 268(14), 10335-44.
Vanhove GF, et al. The CoA Esters of 2-methyl-branched Chain Fatty Acids and of the Bile Acid Intermediates Di- and Trihydroxycoprostanic Acids Are Oxidized By One Single Peroxisomal Branched Chain acyl-CoA Oxidase in Human Liver and Kidney. J Biol Chem. 1993 May 15;268(14):10335-44. PubMed PMID: 8387517.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The CoA esters of 2-methyl-branched chain fatty acids and of the bile acid intermediates di- and trihydroxycoprostanic acids are oxidized by one single peroxisomal branched chain acyl-CoA oxidase in human liver and kidney. AU - Vanhove,G F, AU - Van Veldhoven,P P, AU - Fransen,M, AU - Denis,S, AU - Eyssen,H J, AU - Wanders,R J, AU - Mannaerts,G P, PY - 1993/5/15/pubmed PY - 1993/5/15/medline PY - 1993/5/15/entrez SP - 10335 EP - 44 JF - The Journal of biological chemistry JO - J Biol Chem VL - 268 IS - 14 N2 - Rat liver peroxisomes contain three acyl-CoA oxidases: palmitoyl-CoA oxidase, which oxidizes the CoA esters of straight chain fatty acids and prostaglandins; pristanoyl-CoA oxidase, which oxidizes the CoA esters of 2-methyl-branched fatty acids (e.g. pristanic acid); and trihydroxycoprostanoyl-CoA oxidase, which oxidizes the CoA esters of the bile acid intermediates di- and trihydroxycoprostanic acids (Van Veldhoven, P. P., Vanhove, G., Asselberghs, S., Eyssen, H. J., and Mannaerts, G. P. (1992) J. Biol. Chem. 267, 20065-20074). In the present report we demonstrate that human liver peroxisomes contain only two acyl-CoA oxidases: palmitoyl-CoA oxidase, which oxidizes the CoA esters of straight chain fatty acids and prostaglandins, and a novel branched chain acyl-CoA oxidase, which oxidizes the CoA esters of 2-methyl-branched fatty acids as well as those of the bile acid intermediates (which also possess a 2-methyl substitution in their side chains). The branched chain acyl-CoA oxidase was purified to near homogeneity by means of column chromatography. It appeared to be a 70-kDa monomeric protein that did not cross-react with antisera raised against rat palmitoyl-CoA oxidase and pristanoyl-CoA oxidase. No indication was found for the presence of a separate trihydroxycoprostanoyl-CoA oxidase in human liver. The branched chain acyl-CoA oxidase was present also in human kidney, suggesting that it is expressed in other extrahepatic tissues as well. Our results explain a number of clinical-chemical observations made in certain cases of peroxisomal beta-oxidation disorders. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/8387517/The_CoA_esters_of_2_methyl_branched_chain_fatty_acids_and_of_the_bile_acid_intermediates_di__and_trihydroxycoprostanic_acids_are_oxidized_by_one_single_peroxisomal_branched_chain_acyl_CoA_oxidase_in_human_liver_and_kidney_ L2 - https://metacyc.org/gene?orgid=META&id=HS09732 DB - PRIME DP - Unbound Medicine ER -