Human liver long-chain 3-hydroxyacyl-coenzyme a dehydrogenase is a multifunctional membrane-bound beta-oxidation enzyme of mitochondria

Carpenter, K.; Pollitt, R. J.; Middleton, Bruce

doi:10.1016/0006-291x(92)90501-b

Cited by 138 publications

(78 citation statements)

References 22 publications

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“…Mitochondrial inner membrane protein complex, the trifunctional protein (TFP) consists of 4 a-subunits harboring long chain enoyl-CoA hydratase, long chain 3-hydroxyacylCoA dehydrogenase (LCHAD) activity, and 4 b-subunits carrying long chain 3-ketothiolase activity Carpenter et al 1992a;Carpenter et al 1992b). The TFP a-subunit is encoded by the HADHA gene (OMIM*600890) and the b-subunit by the HADHB gene (OMIM 143450), both of which lie on chromosome 2p23.…”

Section: Introductionmentioning

confidence: 99%

Prevalence of Long-Chain 3-Hydroxyacyl-CoA Dehydrogenase Deficiency in Estonia

et al. 2011

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The aim of our study was to evaluate the prevalence of long chain 3-hydroxyacyl-CoA dehydrogenase deficiency (LCHADD) in the general Estonian population and among patients with symptoms suggestive of fatty acid oxidation (FAO) defects. We collected DNA from a cohort of 1,040 anonymous newborn blood spot samples. We screened these samples for the presence of the common c.1528G>C mutation in the HADHA gene. Based on the clinical suspicion of FAO defects, we screened suspected individuals since 2004 for the common c.1528G>C mutation in the HADHA gene and since 2008 in addition by tandem mass spectrometric analysis of plasma acylcarnitines. Our results showed that the carrier frequency of the c.1528G>C mutation in the Estonian population is high -1:173. During the screening of symptomatic patients, we identified five LCHADD patients in four families. Three patients were retrospectively identified by molecular screening of the HADHA gene.

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Section: Introductionmentioning

confidence: 99%

Prevalence of Long-Chain 3-Hydroxyacyl-CoA Dehydrogenase Deficiency in Estonia

et al. 2011

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“…It has recently been discovered that the LCHAD activity resides in a mitochondrial trifunctional protein. This protein harbors the activities of two other enzymes involved in ~3-oxidation of long-chain fatty acids: enoyl-CoA hydratase and 3-ketoacylCoA thiolase, z, 3 The trifunctional protein has eight subunits: four «-subunits that have LCHAD and long-chain enoylCoA hydratase activity, and four Ô-subunits that have longchain 3-ketoacyl-CoA thiolase activity. 4 Four patients have been described in the literature who have had a combined deficiency with a marked reduction of all three enzyme activities of the trifunctional protein.…”

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confidence: 99%

Long-chain 3-hydroxyacyl–coenzyme A dehydrogenase deficiency with the G1528C mutation: Clinical presentation of thirteen patients

Tyni¹,

Palotie²,

Viinikka³

et al. 1997

The Journal of Pediatrics

132

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“…Recent studies on 3-hydroxydicarboxylic aciduria showed that many but not all of the patients who are characterized by the massive excretion of 3-hydroxydicarboxylic acids have deficient activity of the mitochondrial LCHAD (3)(4)(5)(6)(7)(8)(9)(10)(11)(12). Moreover, LCHAD seems to be associated with a trifunctional enzyme having also enoyl-CoA hydratase and 3-ketoacyl-CoA thiolase activity (13)(14)(15).…”

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confidence: 99%