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Substrate specificities of rat liver peroxisomal acyl-CoA oxidases: palmitoyl-CoA oxidase (inducible acyl-CoA oxidase), pristanoyl-CoA oxidase (non-inducible acyl-CoA oxidase), and trihydroxycoprostanoyl-CoA oxidase.
J Biol Chem. 1992 Oct 05; 267(28):20065-74.JB

Abstract

Rat liver peroxisomes contain three acyl-CoA oxidases:palmitoyl-CoA oxidase, pristanoyl-CoA oxidase, and trihydroxycoprostanoyl-CoA oxidase. The three oxidases were separated by anion-exchange chromatography of a partially purified oxidase preparation, and the column eluate was analyzed for oxidase activity with different acyl-CoAs. Short chain mono (hexanoyl-) and dicarboxylyl (glutaryl-)-CoAs and prostaglandin E2-CoA were oxidized exclusively by palmitoyl-CoA oxidase. Long chain mono (palmitoyl-) and dicarboxylyl (hexadecanedioyl-)-CoAs were oxidized by palmitoyl-CoA oxidase and pristanoyl-CoA oxidase, the former enzyme catalyzing approximately 70% of the total eluate activity. The very long chain lignoceroyl-CoA was also oxidized by palmitoyl-CoA oxidase and pristanoyl-CoA oxidase, the latter enzyme catalyzing approximately 65% of the total eluate activity. Long chain 2-methyl branched acyl-CoAs (2-methylpalmitoyl-CoA and pristanoyl-CoA) were oxidized for approximately 90% by pristanoyl-CoA oxidase, the remaining activity being catalyzed by trihydroxycoprostanoyl-CoA oxidase. The short chain 2-methylhexanoyl-CoA was oxidized by trihydroxycoprostanoyl-CoA oxidase and pristanoyl-CoA oxidase (approximately 60 and 40%, respectively, of the total eluate activity). Trihydroxycoprostanoyl-CoA was oxidized exclusively by trihydroxycoprostanoyl-CoA oxidase. No oxidase activity was found with isovaleryl-CoA and isobutyryl-CoA. Substrate dependences of palmitoyl-CoA oxidase and pristanoyl-CoA oxidase were very similar when assayed with the same (common) substrate. Since the two oxidases were purified to a similar extent and with a similar yield, the contribution of each enzyme to substrate oxidation in the column eluate probably reflects its contribution in the intact liver.

Authors+Show Affiliations

Afdeling Farmacologie, Katholieke Universiteit Leuven, Belgium.No 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

1400324

Citation

Van Veldhoven, P P., et al. "Substrate Specificities of Rat Liver Peroxisomal acyl-CoA Oxidases: palmitoyl-CoA Oxidase (inducible acyl-CoA Oxidase), pristanoyl-CoA Oxidase (non-inducible acyl-CoA Oxidase), and trihydroxycoprostanoyl-CoA Oxidase." The Journal of Biological Chemistry, vol. 267, no. 28, 1992, pp. 20065-74.
Van Veldhoven PP, Vanhove G, Assselberghs S, et al. Substrate specificities of rat liver peroxisomal acyl-CoA oxidases: palmitoyl-CoA oxidase (inducible acyl-CoA oxidase), pristanoyl-CoA oxidase (non-inducible acyl-CoA oxidase), and trihydroxycoprostanoyl-CoA oxidase. J Biol Chem. 1992;267(28):20065-74.
Van Veldhoven, P. P., Vanhove, G., Assselberghs, S., Eyssen, H. J., & Mannaerts, G. P. (1992). Substrate specificities of rat liver peroxisomal acyl-CoA oxidases: palmitoyl-CoA oxidase (inducible acyl-CoA oxidase), pristanoyl-CoA oxidase (non-inducible acyl-CoA oxidase), and trihydroxycoprostanoyl-CoA oxidase. The Journal of Biological Chemistry, 267(28), 20065-74.
Van Veldhoven PP, et al. Substrate Specificities of Rat Liver Peroxisomal acyl-CoA Oxidases: palmitoyl-CoA Oxidase (inducible acyl-CoA Oxidase), pristanoyl-CoA Oxidase (non-inducible acyl-CoA Oxidase), and trihydroxycoprostanoyl-CoA Oxidase. J Biol Chem. 1992 Oct 5;267(28):20065-74. PubMed PMID: 1400324.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Substrate specificities of rat liver peroxisomal acyl-CoA oxidases: palmitoyl-CoA oxidase (inducible acyl-CoA oxidase), pristanoyl-CoA oxidase (non-inducible acyl-CoA oxidase), and trihydroxycoprostanoyl-CoA oxidase. AU - Van Veldhoven,P P, AU - Vanhove,G, AU - Assselberghs,S, AU - Eyssen,H J, AU - Mannaerts,G P, PY - 1992/10/5/pubmed PY - 1992/10/5/medline PY - 1992/10/5/entrez SP - 20065 EP - 74 JF - The Journal of biological chemistry JO - J Biol Chem VL - 267 IS - 28 N2 - Rat liver peroxisomes contain three acyl-CoA oxidases:palmitoyl-CoA oxidase, pristanoyl-CoA oxidase, and trihydroxycoprostanoyl-CoA oxidase. The three oxidases were separated by anion-exchange chromatography of a partially purified oxidase preparation, and the column eluate was analyzed for oxidase activity with different acyl-CoAs. Short chain mono (hexanoyl-) and dicarboxylyl (glutaryl-)-CoAs and prostaglandin E2-CoA were oxidized exclusively by palmitoyl-CoA oxidase. Long chain mono (palmitoyl-) and dicarboxylyl (hexadecanedioyl-)-CoAs were oxidized by palmitoyl-CoA oxidase and pristanoyl-CoA oxidase, the former enzyme catalyzing approximately 70% of the total eluate activity. The very long chain lignoceroyl-CoA was also oxidized by palmitoyl-CoA oxidase and pristanoyl-CoA oxidase, the latter enzyme catalyzing approximately 65% of the total eluate activity. Long chain 2-methyl branched acyl-CoAs (2-methylpalmitoyl-CoA and pristanoyl-CoA) were oxidized for approximately 90% by pristanoyl-CoA oxidase, the remaining activity being catalyzed by trihydroxycoprostanoyl-CoA oxidase. The short chain 2-methylhexanoyl-CoA was oxidized by trihydroxycoprostanoyl-CoA oxidase and pristanoyl-CoA oxidase (approximately 60 and 40%, respectively, of the total eluate activity). Trihydroxycoprostanoyl-CoA was oxidized exclusively by trihydroxycoprostanoyl-CoA oxidase. No oxidase activity was found with isovaleryl-CoA and isobutyryl-CoA. Substrate dependences of palmitoyl-CoA oxidase and pristanoyl-CoA oxidase were very similar when assayed with the same (common) substrate. Since the two oxidases were purified to a similar extent and with a similar yield, the contribution of each enzyme to substrate oxidation in the column eluate probably reflects its contribution in the intact liver. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/1400324/Substrate_specificities_of_rat_liver_peroxisomal_acyl_CoA_oxidases:_palmitoyl_CoA_oxidase__inducible_acyl_CoA_oxidase__pristanoyl_CoA_oxidase__non_inducible_acyl_CoA_oxidase__and_trihydroxycoprostanoyl_CoA_oxidase_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0021-9258(19)88666-0 DB - PRIME DP - Unbound Medicine ER -