Primary Information |
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| BoMiProt ID | Bomi272 |
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| Protein Name | Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial |
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| Organism | Bos taurus |
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| Uniprot ID | P31039 |
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| Milk Fraction | Whey, Exosome |
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| Ref Sequence ID | NP_776603.1 |
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| Aminoacid Length | 665 |
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| Molecular Weight | 72944 |
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| FASTA Sequence |
Download |
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| Gene Name | SDHA |
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| Gene ID | 281480 |
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| Protein Existence Status | Reviewed: Experimental evidence at protein level |
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Secondary Information |
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| Protein Function | part of both the citric acid cycle and respiratory electron
transfer chain. Within the citric acid cycle, SDH oxidizes succinate to fumarate; catalyse the reaction succinate + Q ⇌ fumarate + QH2, which serves as a vital link between the tricarboxylic acid cycle and oxidative phosphorylation |
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| Biochemical Properties | Mammalian succinate dehydrogenase exists in unactivated and activated states; Transition of the unactivated enzyme to the activated form appears to be a conformation change initiated by combination of the protein with substrates or competitive inhibitors and results in a many-fold increase in catalytic activity; activation requires a very high energy ; does not proceed at observable rates at 15˚, the deactivation is rapid even at temperatures near 0˚; A modest degree of activation occurs in particulate and soluble preparations also without added activating agents at 38˚ |
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| PTMs | phosphorylated and
acetylated |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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| Predicted Disorder Regions | 480-490,611-612 |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | Reversible acetylation at multiple Lys residues in mouse was shown to attenuate catalytic activity of the enzyme; The Sdh1 subunit is phosphorylated in mammalian cells and, like acetylation, this modification appears to attenuate activity |
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| Bibliography | 1. Cimen, H. et al. (2010) ‘Regulation of Succinate Dehydrogenase Activity by SIRT3 in Mammalian Mitochondria’, Biochemistry, 49(2), pp. 304–311. doi: 10.1021/bi901627u.
2. TOMITSUKA, E., KITA, K. and ESUMI, H. (2009) ‘Regulation of succinate-ubiquinone reductase and fumarate reductase activities in human complex II by phosphorylation of its flavoprotein subunit’, Proceedings of the Japan Academy, Series B, 85(7), pp. 258–265. doi: 10.2183/pjab.85.258. |
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