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Sterol carrier protein X (SCPx) is a peroxisomal branched-chain beta-ketothiolase specifically reacting with 3-oxo-pristanoyl-CoA: a new, unique role for SCPx in branched-chain fatty acid metabolism in peroxisomes.
Biochem Biophys Res Commun. 1997 Jul 30; 236(3):565-9.BB

Abstract

One of the most important functions of peroxisomes, at least in humans, is the beta-oxidation of a range of different fatty acids and fatty acid derivatives. Recent studies have shown that the enzymatic machinery required for the beta-oxidations of these substrates, may be much more complex as originally thought. We now report that the conventional peroxisomal thiolase which has so far been thought to catalyze the thiolytic cleavage of the 3-oxoacyl-CoA esters of all fatty acids oxidized in peroxisomes, shows poor reactivity towards the 3-oxoacyl-CoA esters of 2-methyl branched-chain fatty acids such as pristanic acid. Our data further show, that SCPx, a 58 kDa protein with both thiolase and sterol carrier protein activity but unknown function so far, readily reacts with 3-oxopristanoyl-CoA. Taken together, our data show that SCPx plays a central role in branched chain fatty acid beta-oxidation in peroxisomes. This finding has major implications not only for the functional organization of the peroxisomal beta-oxidation system but also for studies dealing with the resolution of the underlying defect in patients with some defect in peroxisomal beta-oxidation.

Authors+Show Affiliations

Department of Clinical Chemistry, Emma Children's Hospital, Academic Medical Centre, University of Amsterdam, The Netherlands. wanders@amc.uva.nlNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

9245689

Citation

Wanders, R J., et al. "Sterol Carrier Protein X (SCPx) Is a Peroxisomal Branched-chain Beta-ketothiolase Specifically Reacting With 3-oxo-pristanoyl-CoA: a New, Unique Role for SCPx in Branched-chain Fatty Acid Metabolism in Peroxisomes." Biochemical and Biophysical Research Communications, vol. 236, no. 3, 1997, pp. 565-9.
Wanders RJ, Denis S, Wouters F, et al. Sterol carrier protein X (SCPx) is a peroxisomal branched-chain beta-ketothiolase specifically reacting with 3-oxo-pristanoyl-CoA: a new, unique role for SCPx in branched-chain fatty acid metabolism in peroxisomes. Biochem Biophys Res Commun. 1997;236(3):565-9.
Wanders, R. J., Denis, S., Wouters, F., Wirtz, K. W., & Seedorf, U. (1997). Sterol carrier protein X (SCPx) is a peroxisomal branched-chain beta-ketothiolase specifically reacting with 3-oxo-pristanoyl-CoA: a new, unique role for SCPx in branched-chain fatty acid metabolism in peroxisomes. Biochemical and Biophysical Research Communications, 236(3), 565-9.
Wanders RJ, et al. Sterol Carrier Protein X (SCPx) Is a Peroxisomal Branched-chain Beta-ketothiolase Specifically Reacting With 3-oxo-pristanoyl-CoA: a New, Unique Role for SCPx in Branched-chain Fatty Acid Metabolism in Peroxisomes. Biochem Biophys Res Commun. 1997 Jul 30;236(3):565-9. PubMed PMID: 9245689.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Sterol carrier protein X (SCPx) is a peroxisomal branched-chain beta-ketothiolase specifically reacting with 3-oxo-pristanoyl-CoA: a new, unique role for SCPx in branched-chain fatty acid metabolism in peroxisomes. AU - Wanders,R J, AU - Denis,S, AU - Wouters,F, AU - Wirtz,K W, AU - Seedorf,U, PY - 1997/7/30/pubmed PY - 1997/7/30/medline PY - 1997/7/30/entrez SP - 565 EP - 9 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 236 IS - 3 N2 - One of the most important functions of peroxisomes, at least in humans, is the beta-oxidation of a range of different fatty acids and fatty acid derivatives. Recent studies have shown that the enzymatic machinery required for the beta-oxidations of these substrates, may be much more complex as originally thought. We now report that the conventional peroxisomal thiolase which has so far been thought to catalyze the thiolytic cleavage of the 3-oxoacyl-CoA esters of all fatty acids oxidized in peroxisomes, shows poor reactivity towards the 3-oxoacyl-CoA esters of 2-methyl branched-chain fatty acids such as pristanic acid. Our data further show, that SCPx, a 58 kDa protein with both thiolase and sterol carrier protein activity but unknown function so far, readily reacts with 3-oxopristanoyl-CoA. Taken together, our data show that SCPx plays a central role in branched chain fatty acid beta-oxidation in peroxisomes. This finding has major implications not only for the functional organization of the peroxisomal beta-oxidation system but also for studies dealing with the resolution of the underlying defect in patients with some defect in peroxisomal beta-oxidation. SN - 0006-291X UR - https://www.unboundmedicine.com/medline/citation/9245689/Sterol_carrier_protein_X__SCPx__is_a_peroxisomal_branched_chain_beta_ketothiolase_specifically_reacting_with_3_oxo_pristanoyl_CoA:_a_new_unique_role_for_SCPx_in_branched_chain_fatty_acid_metabolism_in_peroxisomes_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(97)97007-8 DB - PRIME DP - Unbound Medicine ER -