Subcellular localization and physiological role of α-methylacyl-CoA racemase

α-Methylacyl-CoA racemase plays an important role in the β-oxidation of branched-chain fatty acids and fatty acid derivatives because it catalyzes the conversion of several (2R)-methyl-branched-chain fatty acyl-CoAs to their (S)-stereoisomers. Only stereoisomers with the 2-methyl group in the (S)-co...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Sacha Ferdinandusse [verfasserIn] Simone Denis [verfasserIn] Lodewijk IJlst [verfasserIn] Georges Dacremont [verfasserIn] Hans R. Waterham [verfasserIn] Ronald J.A. Wanders [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2000

Schlagwörter:	branched-chain fatty acid β-oxidation stereospecificity (2R,6)-dimethylheptanoyl-CoA

Übergeordnetes Werk:	In: Journal of Lipid Research - Elsevier, 2021, 41(2000), 11, Seite 1890-1896
Übergeordnetes Werk:	volume:41 ; year:2000 ; number:11 ; pages:1890-1896

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1016/S0022-2275(20)31983-0

Katalog-ID:	DOAJ068816391

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allfields	10.1016/S0022-2275(20)31983-0 doi (DE-627)DOAJ068816391 (DE-599)DOAJ7f873e2ce35b44028f1eff8a23853ca2 DE-627 ger DE-627 rakwb eng QD415-436 Sacha Ferdinandusse verfasserin aut Subcellular localization and physiological role of α-methylacyl-CoA racemase 2000 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier α-Methylacyl-CoA racemase plays an important role in the β-oxidation of branched-chain fatty acids and fatty acid derivatives because it catalyzes the conversion of several (2R)-methyl-branched-chain fatty acyl-CoAs to their (S)-stereoisomers. Only stereoisomers with the 2-methyl group in the (S)-configuration can be degraded via β-oxidation. Patients with a deficiency of α-methylacyl-CoA racemase accumulate in their plasma pristanic acid and the bile acid intermediates di- and trihydroxycholestanoic acid, which are all substrates of the peroxisomal β-oxidation system. Subcellular fractionation experiments, however, revealed that both in humans and rats α-methylacyl-CoA racemase is bimodally distributed to both the peroxisome and the mitochondrion. Our findings show that the peroxisomal and mitochondrial enzymes are produced from the same gene and that, as a consequence, the bimodal distribution pattern must be the result of differential targeting of the same gene product. In addition, we investigated the physiological role of the enzyme in the mitochondrion. Both in vitro studies with purified heterologously expressed protein and in vivo studies in fibroblasts of patients with an α-methylacyl-CoA racemase deficiency revealed that the mitochondrial enzyme plays a crucial role in the mitochondrial β-oxidation of the breakdown products of pristanic acid by converting (2R,6)-dimethylheptanoyl-CoA to its (S)-stereoisomer.—Ferdinandusse, S., S. Denis, L. IJlst, G. Dacremont, H. R. Waterham, and R. J. A. Wanders. Subcellular localization and physiological role of α-methylacyl-CoA racemase. J. Lipid Res. 2000. 41: 1890–1896. branched-chain fatty acid β-oxidation stereospecificity (2R,6)-dimethylheptanoyl-CoA Biochemistry Simone Denis verfasserin aut Lodewijk IJlst verfasserin aut Georges Dacremont verfasserin aut Hans R. Waterham verfasserin aut Ronald J.A. Wanders verfasserin aut In Journal of Lipid Research Elsevier, 2021 41(2000), 11, Seite 1890-1896 (DE-627)26601593X (DE-600)1466675-3 15397262 nnns volume:41 year:2000 number:11 pages:1890-1896 https://doi.org/10.1016/S0022-2275(20)31983-0 kostenfrei https://doaj.org/article/7f873e2ce35b44028f1eff8a23853ca2 kostenfrei http://www.sciencedirect.com/science/article/pii/S0022227520319830 kostenfrei https://doaj.org/toc/0022-2275 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2006 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 41 2000 11 1890-1896
spelling	10.1016/S0022-2275(20)31983-0 doi (DE-627)DOAJ068816391 (DE-599)DOAJ7f873e2ce35b44028f1eff8a23853ca2 DE-627 ger DE-627 rakwb eng QD415-436 Sacha Ferdinandusse verfasserin aut Subcellular localization and physiological role of α-methylacyl-CoA racemase 2000 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier α-Methylacyl-CoA racemase plays an important role in the β-oxidation of branched-chain fatty acids and fatty acid derivatives because it catalyzes the conversion of several (2R)-methyl-branched-chain fatty acyl-CoAs to their (S)-stereoisomers. Only stereoisomers with the 2-methyl group in the (S)-configuration can be degraded via β-oxidation. Patients with a deficiency of α-methylacyl-CoA racemase accumulate in their plasma pristanic acid and the bile acid intermediates di- and trihydroxycholestanoic acid, which are all substrates of the peroxisomal β-oxidation system. Subcellular fractionation experiments, however, revealed that both in humans and rats α-methylacyl-CoA racemase is bimodally distributed to both the peroxisome and the mitochondrion. Our findings show that the peroxisomal and mitochondrial enzymes are produced from the same gene and that, as a consequence, the bimodal distribution pattern must be the result of differential targeting of the same gene product. In addition, we investigated the physiological role of the enzyme in the mitochondrion. Both in vitro studies with purified heterologously expressed protein and in vivo studies in fibroblasts of patients with an α-methylacyl-CoA racemase deficiency revealed that the mitochondrial enzyme plays a crucial role in the mitochondrial β-oxidation of the breakdown products of pristanic acid by converting (2R,6)-dimethylheptanoyl-CoA to its (S)-stereoisomer.—Ferdinandusse, S., S. Denis, L. IJlst, G. Dacremont, H. R. Waterham, and R. J. A. Wanders. Subcellular localization and physiological role of α-methylacyl-CoA racemase. J. Lipid Res. 2000. 41: 1890–1896. branched-chain fatty acid β-oxidation stereospecificity (2R,6)-dimethylheptanoyl-CoA Biochemistry Simone Denis verfasserin aut Lodewijk IJlst verfasserin aut Georges Dacremont verfasserin aut Hans R. Waterham verfasserin aut Ronald J.A. Wanders verfasserin aut In Journal of Lipid Research Elsevier, 2021 41(2000), 11, Seite 1890-1896 (DE-627)26601593X (DE-600)1466675-3 15397262 nnns volume:41 year:2000 number:11 pages:1890-1896 https://doi.org/10.1016/S0022-2275(20)31983-0 kostenfrei https://doaj.org/article/7f873e2ce35b44028f1eff8a23853ca2 kostenfrei http://www.sciencedirect.com/science/article/pii/S0022227520319830 kostenfrei https://doaj.org/toc/0022-2275 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2006 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 41 2000 11 1890-1896
allfields_unstemmed	10.1016/S0022-2275(20)31983-0 doi (DE-627)DOAJ068816391 (DE-599)DOAJ7f873e2ce35b44028f1eff8a23853ca2 DE-627 ger DE-627 rakwb eng QD415-436 Sacha Ferdinandusse verfasserin aut Subcellular localization and physiological role of α-methylacyl-CoA racemase 2000 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier α-Methylacyl-CoA racemase plays an important role in the β-oxidation of branched-chain fatty acids and fatty acid derivatives because it catalyzes the conversion of several (2R)-methyl-branched-chain fatty acyl-CoAs to their (S)-stereoisomers. Only stereoisomers with the 2-methyl group in the (S)-configuration can be degraded via β-oxidation. Patients with a deficiency of α-methylacyl-CoA racemase accumulate in their plasma pristanic acid and the bile acid intermediates di- and trihydroxycholestanoic acid, which are all substrates of the peroxisomal β-oxidation system. Subcellular fractionation experiments, however, revealed that both in humans and rats α-methylacyl-CoA racemase is bimodally distributed to both the peroxisome and the mitochondrion. Our findings show that the peroxisomal and mitochondrial enzymes are produced from the same gene and that, as a consequence, the bimodal distribution pattern must be the result of differential targeting of the same gene product. In addition, we investigated the physiological role of the enzyme in the mitochondrion. Both in vitro studies with purified heterologously expressed protein and in vivo studies in fibroblasts of patients with an α-methylacyl-CoA racemase deficiency revealed that the mitochondrial enzyme plays a crucial role in the mitochondrial β-oxidation of the breakdown products of pristanic acid by converting (2R,6)-dimethylheptanoyl-CoA to its (S)-stereoisomer.—Ferdinandusse, S., S. Denis, L. IJlst, G. Dacremont, H. R. Waterham, and R. J. A. Wanders. Subcellular localization and physiological role of α-methylacyl-CoA racemase. J. Lipid Res. 2000. 41: 1890–1896. branched-chain fatty acid β-oxidation stereospecificity (2R,6)-dimethylheptanoyl-CoA Biochemistry Simone Denis verfasserin aut Lodewijk IJlst verfasserin aut Georges Dacremont verfasserin aut Hans R. Waterham verfasserin aut Ronald J.A. Wanders verfasserin aut In Journal of Lipid Research Elsevier, 2021 41(2000), 11, Seite 1890-1896 (DE-627)26601593X (DE-600)1466675-3 15397262 nnns volume:41 year:2000 number:11 pages:1890-1896 https://doi.org/10.1016/S0022-2275(20)31983-0 kostenfrei https://doaj.org/article/7f873e2ce35b44028f1eff8a23853ca2 kostenfrei http://www.sciencedirect.com/science/article/pii/S0022227520319830 kostenfrei https://doaj.org/toc/0022-2275 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2006 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 41 2000 11 1890-1896
allfieldsGer	10.1016/S0022-2275(20)31983-0 doi (DE-627)DOAJ068816391 (DE-599)DOAJ7f873e2ce35b44028f1eff8a23853ca2 DE-627 ger DE-627 rakwb eng QD415-436 Sacha Ferdinandusse verfasserin aut Subcellular localization and physiological role of α-methylacyl-CoA racemase 2000 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier α-Methylacyl-CoA racemase plays an important role in the β-oxidation of branched-chain fatty acids and fatty acid derivatives because it catalyzes the conversion of several (2R)-methyl-branched-chain fatty acyl-CoAs to their (S)-stereoisomers. Only stereoisomers with the 2-methyl group in the (S)-configuration can be degraded via β-oxidation. Patients with a deficiency of α-methylacyl-CoA racemase accumulate in their plasma pristanic acid and the bile acid intermediates di- and trihydroxycholestanoic acid, which are all substrates of the peroxisomal β-oxidation system. Subcellular fractionation experiments, however, revealed that both in humans and rats α-methylacyl-CoA racemase is bimodally distributed to both the peroxisome and the mitochondrion. Our findings show that the peroxisomal and mitochondrial enzymes are produced from the same gene and that, as a consequence, the bimodal distribution pattern must be the result of differential targeting of the same gene product. In addition, we investigated the physiological role of the enzyme in the mitochondrion. Both in vitro studies with purified heterologously expressed protein and in vivo studies in fibroblasts of patients with an α-methylacyl-CoA racemase deficiency revealed that the mitochondrial enzyme plays a crucial role in the mitochondrial β-oxidation of the breakdown products of pristanic acid by converting (2R,6)-dimethylheptanoyl-CoA to its (S)-stereoisomer.—Ferdinandusse, S., S. Denis, L. IJlst, G. Dacremont, H. R. Waterham, and R. J. A. Wanders. Subcellular localization and physiological role of α-methylacyl-CoA racemase. J. Lipid Res. 2000. 41: 1890–1896. branched-chain fatty acid β-oxidation stereospecificity (2R,6)-dimethylheptanoyl-CoA Biochemistry Simone Denis verfasserin aut Lodewijk IJlst verfasserin aut Georges Dacremont verfasserin aut Hans R. Waterham verfasserin aut Ronald J.A. Wanders verfasserin aut In Journal of Lipid Research Elsevier, 2021 41(2000), 11, Seite 1890-1896 (DE-627)26601593X (DE-600)1466675-3 15397262 nnns volume:41 year:2000 number:11 pages:1890-1896 https://doi.org/10.1016/S0022-2275(20)31983-0 kostenfrei https://doaj.org/article/7f873e2ce35b44028f1eff8a23853ca2 kostenfrei http://www.sciencedirect.com/science/article/pii/S0022227520319830 kostenfrei https://doaj.org/toc/0022-2275 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2006 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 41 2000 11 1890-1896
allfieldsSound	10.1016/S0022-2275(20)31983-0 doi (DE-627)DOAJ068816391 (DE-599)DOAJ7f873e2ce35b44028f1eff8a23853ca2 DE-627 ger DE-627 rakwb eng QD415-436 Sacha Ferdinandusse verfasserin aut Subcellular localization and physiological role of α-methylacyl-CoA racemase 2000 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier α-Methylacyl-CoA racemase plays an important role in the β-oxidation of branched-chain fatty acids and fatty acid derivatives because it catalyzes the conversion of several (2R)-methyl-branched-chain fatty acyl-CoAs to their (S)-stereoisomers. Only stereoisomers with the 2-methyl group in the (S)-configuration can be degraded via β-oxidation. Patients with a deficiency of α-methylacyl-CoA racemase accumulate in their plasma pristanic acid and the bile acid intermediates di- and trihydroxycholestanoic acid, which are all substrates of the peroxisomal β-oxidation system. Subcellular fractionation experiments, however, revealed that both in humans and rats α-methylacyl-CoA racemase is bimodally distributed to both the peroxisome and the mitochondrion. Our findings show that the peroxisomal and mitochondrial enzymes are produced from the same gene and that, as a consequence, the bimodal distribution pattern must be the result of differential targeting of the same gene product. In addition, we investigated the physiological role of the enzyme in the mitochondrion. Both in vitro studies with purified heterologously expressed protein and in vivo studies in fibroblasts of patients with an α-methylacyl-CoA racemase deficiency revealed that the mitochondrial enzyme plays a crucial role in the mitochondrial β-oxidation of the breakdown products of pristanic acid by converting (2R,6)-dimethylheptanoyl-CoA to its (S)-stereoisomer.—Ferdinandusse, S., S. Denis, L. IJlst, G. Dacremont, H. R. Waterham, and R. J. A. Wanders. Subcellular localization and physiological role of α-methylacyl-CoA racemase. J. Lipid Res. 2000. 41: 1890–1896. branched-chain fatty acid β-oxidation stereospecificity (2R,6)-dimethylheptanoyl-CoA Biochemistry Simone Denis verfasserin aut Lodewijk IJlst verfasserin aut Georges Dacremont verfasserin aut Hans R. Waterham verfasserin aut Ronald J.A. Wanders verfasserin aut In Journal of Lipid Research Elsevier, 2021 41(2000), 11, Seite 1890-1896 (DE-627)26601593X (DE-600)1466675-3 15397262 nnns volume:41 year:2000 number:11 pages:1890-1896 https://doi.org/10.1016/S0022-2275(20)31983-0 kostenfrei https://doaj.org/article/7f873e2ce35b44028f1eff8a23853ca2 kostenfrei http://www.sciencedirect.com/science/article/pii/S0022227520319830 kostenfrei https://doaj.org/toc/0022-2275 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2006 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 41 2000 11 1890-1896
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topic_facet	branched-chain fatty acid β-oxidation stereospecificity (2R,6)-dimethylheptanoyl-CoA Biochemistry
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callnumber-first	Q - Science
author	Sacha Ferdinandusse
spellingShingle	Sacha Ferdinandusse misc QD415-436 misc branched-chain fatty acid β-oxidation misc stereospecificity misc (2R,6)-dimethylheptanoyl-CoA misc Biochemistry Subcellular localization and physiological role of α-methylacyl-CoA racemase
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topic_title	QD415-436 Subcellular localization and physiological role of α-methylacyl-CoA racemase branched-chain fatty acid β-oxidation stereospecificity (2R,6)-dimethylheptanoyl-CoA
topic	misc QD415-436 misc branched-chain fatty acid β-oxidation misc stereospecificity misc (2R,6)-dimethylheptanoyl-CoA misc Biochemistry
topic_unstemmed	misc QD415-436 misc branched-chain fatty acid β-oxidation misc stereospecificity misc (2R,6)-dimethylheptanoyl-CoA misc Biochemistry
topic_browse	misc QD415-436 misc branched-chain fatty acid β-oxidation misc stereospecificity misc (2R,6)-dimethylheptanoyl-CoA misc Biochemistry
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title	Subcellular localization and physiological role of α-methylacyl-CoA racemase
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title_full	Subcellular localization and physiological role of α-methylacyl-CoA racemase
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title_sort	subcellular localization and physiological role of α-methylacyl-coa racemase
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title_auth	Subcellular localization and physiological role of α-methylacyl-CoA racemase
abstract	α-Methylacyl-CoA racemase plays an important role in the β-oxidation of branched-chain fatty acids and fatty acid derivatives because it catalyzes the conversion of several (2R)-methyl-branched-chain fatty acyl-CoAs to their (S)-stereoisomers. Only stereoisomers with the 2-methyl group in the (S)-configuration can be degraded via β-oxidation. Patients with a deficiency of α-methylacyl-CoA racemase accumulate in their plasma pristanic acid and the bile acid intermediates di- and trihydroxycholestanoic acid, which are all substrates of the peroxisomal β-oxidation system. Subcellular fractionation experiments, however, revealed that both in humans and rats α-methylacyl-CoA racemase is bimodally distributed to both the peroxisome and the mitochondrion. Our findings show that the peroxisomal and mitochondrial enzymes are produced from the same gene and that, as a consequence, the bimodal distribution pattern must be the result of differential targeting of the same gene product. In addition, we investigated the physiological role of the enzyme in the mitochondrion. Both in vitro studies with purified heterologously expressed protein and in vivo studies in fibroblasts of patients with an α-methylacyl-CoA racemase deficiency revealed that the mitochondrial enzyme plays a crucial role in the mitochondrial β-oxidation of the breakdown products of pristanic acid by converting (2R,6)-dimethylheptanoyl-CoA to its (S)-stereoisomer.—Ferdinandusse, S., S. Denis, L. IJlst, G. Dacremont, H. R. Waterham, and R. J. A. Wanders. Subcellular localization and physiological role of α-methylacyl-CoA racemase. J. Lipid Res. 2000. 41: 1890–1896.
abstractGer	α-Methylacyl-CoA racemase plays an important role in the β-oxidation of branched-chain fatty acids and fatty acid derivatives because it catalyzes the conversion of several (2R)-methyl-branched-chain fatty acyl-CoAs to their (S)-stereoisomers. Only stereoisomers with the 2-methyl group in the (S)-configuration can be degraded via β-oxidation. Patients with a deficiency of α-methylacyl-CoA racemase accumulate in their plasma pristanic acid and the bile acid intermediates di- and trihydroxycholestanoic acid, which are all substrates of the peroxisomal β-oxidation system. Subcellular fractionation experiments, however, revealed that both in humans and rats α-methylacyl-CoA racemase is bimodally distributed to both the peroxisome and the mitochondrion. Our findings show that the peroxisomal and mitochondrial enzymes are produced from the same gene and that, as a consequence, the bimodal distribution pattern must be the result of differential targeting of the same gene product. In addition, we investigated the physiological role of the enzyme in the mitochondrion. Both in vitro studies with purified heterologously expressed protein and in vivo studies in fibroblasts of patients with an α-methylacyl-CoA racemase deficiency revealed that the mitochondrial enzyme plays a crucial role in the mitochondrial β-oxidation of the breakdown products of pristanic acid by converting (2R,6)-dimethylheptanoyl-CoA to its (S)-stereoisomer.—Ferdinandusse, S., S. Denis, L. IJlst, G. Dacremont, H. R. Waterham, and R. J. A. Wanders. Subcellular localization and physiological role of α-methylacyl-CoA racemase. J. Lipid Res. 2000. 41: 1890–1896.
abstract_unstemmed	α-Methylacyl-CoA racemase plays an important role in the β-oxidation of branched-chain fatty acids and fatty acid derivatives because it catalyzes the conversion of several (2R)-methyl-branched-chain fatty acyl-CoAs to their (S)-stereoisomers. Only stereoisomers with the 2-methyl group in the (S)-configuration can be degraded via β-oxidation. Patients with a deficiency of α-methylacyl-CoA racemase accumulate in their plasma pristanic acid and the bile acid intermediates di- and trihydroxycholestanoic acid, which are all substrates of the peroxisomal β-oxidation system. Subcellular fractionation experiments, however, revealed that both in humans and rats α-methylacyl-CoA racemase is bimodally distributed to both the peroxisome and the mitochondrion. Our findings show that the peroxisomal and mitochondrial enzymes are produced from the same gene and that, as a consequence, the bimodal distribution pattern must be the result of differential targeting of the same gene product. In addition, we investigated the physiological role of the enzyme in the mitochondrion. Both in vitro studies with purified heterologously expressed protein and in vivo studies in fibroblasts of patients with an α-methylacyl-CoA racemase deficiency revealed that the mitochondrial enzyme plays a crucial role in the mitochondrial β-oxidation of the breakdown products of pristanic acid by converting (2R,6)-dimethylheptanoyl-CoA to its (S)-stereoisomer.—Ferdinandusse, S., S. Denis, L. IJlst, G. Dacremont, H. R. Waterham, and R. J. A. Wanders. Subcellular localization and physiological role of α-methylacyl-CoA racemase. J. Lipid Res. 2000. 41: 1890–1896.
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title_short	Subcellular localization and physiological role of α-methylacyl-CoA racemase
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Only stereoisomers with the 2-methyl group in the (S)-configuration can be degraded via β-oxidation. Patients with a deficiency of α-methylacyl-CoA racemase accumulate in their plasma pristanic acid and the bile acid intermediates di- and trihydroxycholestanoic acid, which are all substrates of the peroxisomal β-oxidation system. Subcellular fractionation experiments, however, revealed that both in humans and rats α-methylacyl-CoA racemase is bimodally distributed to both the peroxisome and the mitochondrion. Our findings show that the peroxisomal and mitochondrial enzymes are produced from the same gene and that, as a consequence, the bimodal distribution pattern must be the result of differential targeting of the same gene product. In addition, we investigated the physiological role of the enzyme in the mitochondrion. Both in vitro studies with purified heterologously expressed protein and in vivo studies in fibroblasts of patients with an α-methylacyl-CoA racemase deficiency revealed that the mitochondrial enzyme plays a crucial role in the mitochondrial β-oxidation of the breakdown products of pristanic acid by converting (2R,6)-dimethylheptanoyl-CoA to its (S)-stereoisomer.—Ferdinandusse, S., S. Denis, L. IJlst, G. Dacremont, H. R. Waterham, and R. J. A. Wanders. Subcellular localization and physiological role of α-methylacyl-CoA racemase. J. Lipid Res. 2000. 41: 1890–1896.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">branched-chain fatty acid β-oxidation</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">stereospecificity</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">(2R,6)-dimethylheptanoyl-CoA</subfield></datafield><datafield tag="653" ind1=" " ind2="0"><subfield code="a">Biochemistry</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Simone Denis</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Lodewijk IJlst</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Georges Dacremont</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="0" ind2=" "><subfield code="a">Hans R. 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