Tags

Type your tag names separated by a space and hit enter

Identification and purification of a peroxisomal branched chain fatty acyl-CoA oxidase.
J Biol Chem. 1991 Dec 25; 266(36):24676-83.JB

Abstract

Isoprenoid (branched) fatty acids such as pristanic acid can be degraded via beta-oxidation in peroxisomes. We synthesized 2-methylpalmitoyl-CoA as a model substrate in order to study the first step of the peroxisomal beta-oxidation of branched fatty acids, catalyzed by an acyl-CoA oxidase. 2-Methylpalmitoyl-CoA oxidase activity was found in rat liver homogenates. Subcellular fractionation demonstrated that the oxidase was confined to peroxisomes. 2-Methylpalmitoyl-CoA oxidase was also present in kidney and intestine. It was not induced in liver or in the extrahepatic tissues by treatment of rats with peroxisome proliferators or by feeding diets containing excess isoprenoids. The enzyme was partially purified together with palmitoyl-CoA oxidase and trihydroxycoprostanoyl-CoA oxidase by heat treatment and ammonium sulfate fractionation of liver extracts. The partially purified preparation was chromatographed on various columns. 2-Methylpalmitoyl-CoA oxidase could be separated from the inducible (by peroxisome proliferators) palmitoyl-CoA oxidase and from trihydroxycoprostanoyl-CoA oxidase, but it always coeluted with the noninducible palmitoyl-CoA oxidase, recently described by us (Schepers, L., Van Veldhoven, P. P., Casteels, M., Eyssen, H. J., and Mannaerts, G. P. (1990) J. Biol. Chem. 265, 5242-5246). 2-Methylpalmitoyl-CoA oxidase was purified to near homogeneity in three chromatographic steps (anion exchange, hydroxylapatite, and gel filtration). Its apparent molecular mass is approximately 415 kDa, and it consists of identical subunits of approximately 70 kDa. The enzyme oxidized 2-methylpalmitoyl-CoA twice as rapidly as palmitoyl-CoA and pristanoyl-CoA as rapidly as palmitoyl-CoA, so that it can be considered as a branched fatty acyl-CoA oxidase. Since pristanoyl-CoA is one of its naturally occurring substrates we propose to name this enzyme pristanoyl-CoA oxidase.

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

1761563

Citation

Van Veldhoven, P P., et al. "Identification and Purification of a Peroxisomal Branched Chain Fatty acyl-CoA Oxidase." The Journal of Biological Chemistry, vol. 266, no. 36, 1991, pp. 24676-83.
Van Veldhoven PP, Vanhove G, Vanhoutte F, et al. Identification and purification of a peroxisomal branched chain fatty acyl-CoA oxidase. J Biol Chem. 1991;266(36):24676-83.
Van Veldhoven, P. P., Vanhove, G., Vanhoutte, F., Dacremont, G., Parmentier, G., Eyssen, H. J., & Mannaerts, G. P. (1991). Identification and purification of a peroxisomal branched chain fatty acyl-CoA oxidase. The Journal of Biological Chemistry, 266(36), 24676-83.
Van Veldhoven PP, et al. Identification and Purification of a Peroxisomal Branched Chain Fatty acyl-CoA Oxidase. J Biol Chem. 1991 Dec 25;266(36):24676-83. PubMed PMID: 1761563.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Identification and purification of a peroxisomal branched chain fatty acyl-CoA oxidase. AU - Van Veldhoven,P P, AU - Vanhove,G, AU - Vanhoutte,F, AU - Dacremont,G, AU - Parmentier,G, AU - Eyssen,H J, AU - Mannaerts,G P, PY - 1991/12/25/pubmed PY - 1991/12/25/medline PY - 1991/12/25/entrez SP - 24676 EP - 83 JF - The Journal of biological chemistry JO - J Biol Chem VL - 266 IS - 36 N2 - Isoprenoid (branched) fatty acids such as pristanic acid can be degraded via beta-oxidation in peroxisomes. We synthesized 2-methylpalmitoyl-CoA as a model substrate in order to study the first step of the peroxisomal beta-oxidation of branched fatty acids, catalyzed by an acyl-CoA oxidase. 2-Methylpalmitoyl-CoA oxidase activity was found in rat liver homogenates. Subcellular fractionation demonstrated that the oxidase was confined to peroxisomes. 2-Methylpalmitoyl-CoA oxidase was also present in kidney and intestine. It was not induced in liver or in the extrahepatic tissues by treatment of rats with peroxisome proliferators or by feeding diets containing excess isoprenoids. The enzyme was partially purified together with palmitoyl-CoA oxidase and trihydroxycoprostanoyl-CoA oxidase by heat treatment and ammonium sulfate fractionation of liver extracts. The partially purified preparation was chromatographed on various columns. 2-Methylpalmitoyl-CoA oxidase could be separated from the inducible (by peroxisome proliferators) palmitoyl-CoA oxidase and from trihydroxycoprostanoyl-CoA oxidase, but it always coeluted with the noninducible palmitoyl-CoA oxidase, recently described by us (Schepers, L., Van Veldhoven, P. P., Casteels, M., Eyssen, H. J., and Mannaerts, G. P. (1990) J. Biol. Chem. 265, 5242-5246). 2-Methylpalmitoyl-CoA oxidase was purified to near homogeneity in three chromatographic steps (anion exchange, hydroxylapatite, and gel filtration). Its apparent molecular mass is approximately 415 kDa, and it consists of identical subunits of approximately 70 kDa. The enzyme oxidized 2-methylpalmitoyl-CoA twice as rapidly as palmitoyl-CoA and pristanoyl-CoA as rapidly as palmitoyl-CoA, so that it can be considered as a branched fatty acyl-CoA oxidase. Since pristanoyl-CoA is one of its naturally occurring substrates we propose to name this enzyme pristanoyl-CoA oxidase. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/1761563/Identification_and_purification_of_a_peroxisomal_branched_chain_fatty_acyl_CoA_oxidase_ DB - PRIME DP - Unbound Medicine ER -