Studies on the regulation of the human E1 subunit of the 2-oxoglutarate dehydrogenase complex, including the identification of a novel calcium-binding site
Abstract
The regulation of the 2-oxoglutarate dehydrogenase complex is central to intramitochondrial energy metabolism. In the present study, the active full-length E1 subunit of the human complex has been expressed and shown to be regulated by Ca2+, adenine nucleotides and NADH, with NADH exerting a major influence on the K0.5 value for Ca2+. We investigated two potential Ca2+-binding sites on E1, which we term site 1 (D114ADLD) and site 2 (E139SDLD). Comparison of sequences from vertebrates with those from Ca2+-insensitive non-vertebrate complexes suggest that site 1 may be the more important. Consistent with this view, a mutated form of E1, D114A, shows a 6-fold decrease in sensitivity for Ca2+, whereas variant ∆site1 (in which the sequence of site 1 is replaced by A114AALA) exhibits an almost complete loss of Ca2+ activation. Variant ∆site2 (in which the sequence is replaced with A139SALA) shows no measurable change in Ca2+ sensitivity. We conclude that site 1, but not site 2, forms part of a regulatory Ca2+-binding site, which is distinct from other previously described Ca2+-binding sites.
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As a result of the OGDH splice switch, a stretch of 34 amino acids in OGDH1 containing a Ca2+-binding motif is replaced by 45 amino acids specific to OGDHneu.
“a stretch of 34 amino acids in OGDH1, containing a Ca2+-binding motif (Armstrong et al., 2014), is replaced by 45 amino acids specific to OGDHneu”
From Metabolic reprogramming during neuronal differentiation from aerobic glycolysis to neuronal oxidative phosphorylation (2016) · cites this paper as Armstrong et al., 2014
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- Authors
- Armstrong, C. T., Anderson, J. L. R., & Denton, R. M.
- Affiliations
- University of Bristol (GB)
- ORCID
- Anderson, J. L. Ross
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2014-03-28
- Volume
- 459
- Issue
- 2
- Pages
- 369-381
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W2105671007
- Cited by
- 44
- References
- 56
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 2 · 2023: 4 · 2022: 7 · 2021: 8 · 2020: 4 · 2019: 3 · 2018: 1 · 2017: 1 · 2016: 7 · 2014: 1
- FWCI
- 1.33
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical Journal (publishedVersion)
- PubMed (publishedVersion)
- Explore Bristol Research (publishedVersion)
- Bristol Research (University of Bristol) (submittedVersion)
- Funders
- University of Bristol
- Biotechnology and Biological Sciences Research Council (BB1014063/1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Biochemical Acid Research Studies
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Keywords
- 2-oxoglutarate dehydrogenase, calcium binding sites, calcium regulation, adenine nucleotides, site-directed mutagenesis
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Calcium, Humans, Ketoglutarate Dehydrogenase Complex, Ketoglutaric Acids, Kinetics, Molecular Sequence Data, Myocardium, Protein Binding, Species Specificity, Swine, Molecular Structure, Gene Expression Regulation, Enzymologic, Protein Subunits
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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