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Cited by 82Metabolism and Genetic DisordersMitochondrial Function and PathologyEnzyme Structure and Function

The mitochondrial trifunctional protein: centre of a β-oxidation metabolon?

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Eaton, S., Bursby, T., Middleton, B., Pourfarzam, M., Mills, K., Johnson, A. W., Bartlecc, K.·2000·Biochemical Society Transactions
DOI 10.1042/bst0280177
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Abstract

The trifunctional enzyme comprises three consecutive steps in the mitochondrial β-oxidation of long-chain acyl-CoA esters: 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase and 3-ketoacyl-CoA thiolase. Deficiencies in either 3-hydroxyacyl-CoA dehydrogenase activity, or all three activities, are important causes of human disease. The dehydrogenase and thiolase have a requirement for NAD+ and CoA respectively, whose levels are conserved within the mitochondrion and thus provide possible means for control and regulation of β-oxidation. Using analysis of the intact CoA ester intermediates produced by the complex, we have examined the sensitivity of the complex to NAD+/NADH and acetyl-CoA. We consider the evidence for channelling within the trifunctional protein and propose a model for a β-oxidation ‘metabolon’.

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  • HADHB encodes the β-subunit of the mitochondrial trifunctional protein that carries out the last three steps of β-oxidation.

    “The gene HADHB encodes for the ␤-subunit of the mitochondrial trifunctional protein that carries out the last three steps of ␤-oxidation (30).”

    From Expression of miR-33 from an SREBP2 Intron Inhibits Cholesterol Export and Fatty Acid Oxidation* (2010) · cites this paper as [30]

  • Several genes involved in fatty acid β-oxidation have predicted targets for miR-33, including CROT, CPT1a, HADHB, and AMPKα.

    “As shown in Fig. S2 (red box), several genes involved in fatty acid β-oxidation have predicted targets for miR-33, including CROT, CPT1a, HADHB and AMPKα (17–20).”

    From miR-33a/b contribute to the regulation of fatty acid metabolism and insulin signaling (2011) · cites this paper as [18]

  • CPT1a mediates the transport of long fatty acids across the mitochondrial membrane by binding them to carnitine and is the rate-limiting enzyme that regulates fatty acid oxidation.

    “CPT1a is a mitochondrial enzyme that mediates the transport of long fatty acids across the membrane by binding them to carnitine, and it is the rate-limiting enzyme that regulates fatty acid oxidation (17–20).”

    From miR-33a/b contribute to the regulation of fatty acid metabolism and insulin signaling (2011) · cites this paper as [18]

  • CROT catalyzes the reversible transfer of fatty acyl between CoA and carnitine and provides a crucial step in the transport of medium and long-chain acyl-CoA out of the peroxisome to the cytosol and mitochondria.

    “CROT, a carnitine acyltransferase that catalyzes the reversible transfer of fatty acyl between CoA and carnitine, provides a crucial step in the transport of medium and long-chain acyl-CoA out of the mammalian peroxisome to the cytosol and mitochondria (17–20).”

    From miR-33a/b contribute to the regulation of fatty acid metabolism and insulin signaling (2011) · cites this paper as [18]

  • AMPKα stimulates hepatic fatty acid oxidation and ketogenesis.

    “AMPKα stimulates hepatic fatty acid oxidation and ketogenesis (17–20).”

    From miR-33a/b contribute to the regulation of fatty acid metabolism and insulin signaling (2011) · cites this paper as [18]

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Authors
Eaton, S., Bursby, T., Middleton, B., Pourfarzam, M., Mills, K., Johnson, A. W., & Bartlecc, K.
Affiliations
  • Unit of Paediatric Surgery, Institute of Child Health, 30 Guilford Street, London WCIN IEH, U.K.
  • Royal Victoria Infirmary (GB)
  • University of Nottingham (GB)
Corresponding author
  • Eaton, S.
  • Mills, K.
ORCID
Venue
Biochemical Society Transactions
Publisher
Portland Press Ltd.
Published
2000-02-01
Volume
28
Issue
2
Pages
177-182
ISSN
  • 0300-5127 (ISSN-L)
  • 1470-8752
DOI
10.1042/bst0280177
OpenAlex
W163773482
Cited by
82
References
0
Citations by year
2026: 3 · 2025: 1 · 2024: 4 · 2023: 5 · 2022: 5 · 2021: 2 · 2020: 3 · 2019: 5 · 2018: 2 · 2017: 4 · 2016: 2 · 2015: 2 · 2014: 3 · 2013: 4 · 2012: 3
FWCI
1.64
Type
journal article
Language
en
Open access
Locations
  • Biochemical Society Transactions (publishedVersion)
  • PubMed (publishedVersion)
  • UCL Discovery (University College London) (submittedVersion)
  • Newcastle University ePrints (Newcastle Univesity)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords
mitochondrial trifunctional protein, fatty acid beta-oxidation, metabolon, 3-hydroxyacyl-CoA dehydrogenase, 3-ketoacyl-CoA thiolase, long-chain acyl-CoA, NAD+/NADH ratio, acetyl-CoA, substrate channeling, enzyme regulation, inborn errors of metabolism
MeSH terms
Amino Acid Sequence, Catalysis, Humans, Models, Biological, Molecular Sequence Data, Multienzyme Complexes, Mutation, Oxygen, Protein Structure, Tertiary, Mitochondrial Trifunctional Protein

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