1986
DOI: 10.1002/9780470123041.ch4
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Succinyl‐CoA Synthetase Structure‐Function Relationships and Other Considerations

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Cited by 22 publications
(17 citation statements)
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“…N -3 PUFA was previously found to regulate the metabolic function of liver effectively by increasing MDH enzyme activity of rat liver [59,72]. SCS catalyzes the reversible reaction of succinyl-CoA to succinate, and is the only mitochondrial enzyme capable of ATP production via substrate level phosphorylation in the absence of oxygen [73]. SCS plays a key role in the citric acid cycle, ketone metabolism and heme synthesis [74].…”
Section: Resultsmentioning
confidence: 99%
“…N -3 PUFA was previously found to regulate the metabolic function of liver effectively by increasing MDH enzyme activity of rat liver [59,72]. SCS catalyzes the reversible reaction of succinyl-CoA to succinate, and is the only mitochondrial enzyme capable of ATP production via substrate level phosphorylation in the absence of oxygen [73]. SCS plays a key role in the citric acid cycle, ketone metabolism and heme synthesis [74].…”
Section: Resultsmentioning
confidence: 99%
“…The molecular mass of the ␣ and ␤ subunits are ϳ30 and ϳ40 kDa, respectively (19), and there are fundamental differences in the quaternary structures of the bacterial and mammalian forms of succinyl-CoA synthetases. The Escherichia coli enzyme functions as an ␣ 2 ␤ 2 tetramer with no activity associated with a heterodimeric form, whereas the enzyme isolated from pig heart functions only as the ␣␤ dimer (20).…”
Section: Dementioning
confidence: 99%
“…Succinyl-CoA synthetases (SucCD; EC 6.2.1.4 or EC 6.2.1.5) occur in prokaryotes and eukaryotes and are widely known for catalyzing the only substrate-level phosphorylation in the citric acid cycle (7,31). Therein, the conversion of succinyl-CoA to succinate yields nucleoside triphosphates during aerobic metabolism.…”
mentioning
confidence: 99%