Role of lecithin in D-β-hydroxybutyrate dehydrogenase function

Gazzotti, Paolo; Bock, Hans-Georg O.; Fleischer, Sidney

doi:10.1016/0006-291x(74)90928-0

Cited by 82 publications

(47 citation statements)

References 11 publications

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“…Preparations retaining three or more endogenous (Ptd)2Gro molecules were maximally active in lysolipid. There was no further increase in activity upon addition of (Ptd)2Gro, PtdCho, or PtdEtn in the presence of this 8 16 24 amphiphile. These preparations were activated by exogenous phospholipids when assayed in Tween 80 but this was a nonspecific effect, the activity regenerated being proportional to the amount of lipid bound to the protein in the assay medium (as shown in Fig.…”

mentioning

confidence: 82%

“…In addition to such general effects, there may be specific lipid requirements for certain membrane activities. For example, there is evidence that Na',K' ATPase requires anionic lipids (7) and that hydroxybutyrate dehydrogenase requires phosphatidylcholine (PtdCho) for maximal activity (8).…”

mentioning

confidence: 99%

“…The most efficient method for removing these most tightly bound (Ptd)2Gro molecules proved to be the glycerol gradient procedure in 1% Triton X-100 first described by Robinson (23). When a single gradient step was used, protein could be collected in several fractions with phospholipid content ranging from 8 (Fig. 1).…”

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confidence: 99%

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Diphosphatidylglycerol is required for optimal activity of beef heart cytochrome c oxidase.

Vik¹,

Georgevich²,

Capaldi³

1981

Proc. Natl. Acad. Sci. U.S.A.

160

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Isolated beef heart cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) contains four or five molecules of tightly bound diphosphatidylglycerol per monomer (2-heme complex). This lipid could be removed in part, or wholly, by mixing the enzyme with high concentrations of Triton X-100 and then centrifuging the mixture through a glycerol gradient equilibrated in the same detergent. Cytochrome c oxidase retaining three or more diphosphatidylglycerol molecules per monomer was fully active when assayed in 1-oleoyl lysophosphatidylcholine. Upon removal of one or more of these diphosphatidylglycerols, enzymic activity was lost. Full activation could be obtained by adding diphosphatidylglycerol to the assay mixture along with lysophosphatidylcholine but not by adding phosphatidylcholine or phosphatidylethanolamine. Direct binding experiments, kinetic studies, and previous work using arylazidocytochrome c derivatives [Bisson, R., Jacobs, B. & Capaldi, R. A. (1980) Biochemistry 10, 4173-4178], indicate that diphosphatidylglycerol is involved in binding of substrate cytochrome c to cytochrome c oxidase.

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confidence: 82%

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confidence: 99%

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Diphosphatidylglycerol is required for optimal activity of beef heart cytochrome c oxidase.

Vik¹,

Georgevich²,

Capaldi³

1981

Proc. Natl. Acad. Sci. U.S.A.

160

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“…The catalytic activity of many membrane-bound enzymes is dependent upon the presence of phospholipids (Martonosi et al, 1968;Strobel et al, 1970;Cater et al, 1975;Gazzotti et al, 1975). Similarly, a phospholipid requirement has been suggested for UDP-glucuronyltransferase (EC 2.4.1.17) activity.…”

mentioning

confidence: 98%

Phospholipid-dependence of oestrone UDP-glucuronyltransferase and p-nitrophenol UDP-glucuronyltransferase

Tukey¹,

Billings²,

Autor³

et al. 1979

Biochemical Journal

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Hepatic UDP-glucuronyltransferase activity was resolved into two fractions, one exhibiting oestrone glucuronyltransferase activity and the other exhibiting p-nitrophenol glucuronyltransferase activity. Hydroxyapatite-column chromatography removed greater than 95 % of the phospholipids from both preparations. The partially purified delipidated enzymes were essentially devoid of catalytic activity, but activities were restored by the addition of phospholipids or phosphatidylcholine mixtures containing various saturated and unsaturated fatty acids. Both oestrone andp-nitrophenol glucuronyltransferase activities were reconstituted to similar degrees with the phosphatidylcholine mixtures. When purified phospholipids were tested, phosphatidylcholine and lysophosphatidylcholine were most effective in restoring activity, whereas phosphatidylethanolamine was the least effective. These results further suggest that oestrone and p-nitrophenol UDP-glucuronyltransferases are dependent on phospholipids for their activity.

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“…Previous studies on the interactions of BDH with pospholipids (Gazzoti et al, 1964;McIntyre et al, 1978;Berrez et al, 1984;Kante et al, 1990) have demonstrated that the composition of membrane phospholipids induced structural modifications of BDH. The local environment of the protein may result in an important kinetic change.…”

Section: Discussionmentioning

confidence: 95%

Prehibernation and hibernation effects on the d-3-hydroxybutyrate dehydrogenase of the heavy and light mitochondria from liver jerboa (Jaculus orientalis) and related metabolism

Mountassif¹,

Kabine²,

Latruffe³

et al. 2007

Biochimie

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Kebbaj To cite this version:Driss Mountassif, Mostafa Kabine, Norbert Latruffe, M'Hammed Saïd El Kebbaj. Prehibernation and hibernation effects on the D-3-hydroxybutyrate dehydrogenase of the heavy and light mitochondria from liver jerboa (Jaculus orientalis) and related metabolism.. Biochimie, Elsevier, 2007, 89 (8) Abstract:The D-3-hydroxybutyrate dehydrogenase (BDH) (EC 1.1.1.30) from liver jerboa (Jaculus orientalis), a ketone body converting enzyme in mitochondria, in two populations of mitochondria (heavy and light) has been studied in different jerboa states (euthermic, prehibernatingand hibernating). The results reveal: (1) important variations between states in terms of ketones bodies, glucose and lipid levels; (2) significant differences between the BDH of the two mitochondrial populations in term of protein expression and kinetic properties. These results suggest that BDH leads an important conformational change depending on the physiological state of jerboa. This BDH structural change could be the consequence of the lipid composition modifications in inner mitochondrial membrane leading to changes in BDH catalytic properties.

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Role of lecithin in D-β-hydroxybutyrate dehydrogenase function

Cited by 82 publications

References 11 publications

Diphosphatidylglycerol is required for optimal activity of beef heart cytochrome c oxidase.

Diphosphatidylglycerol is required for optimal activity of beef heart cytochrome c oxidase.

Phospholipid-dependence of oestrone UDP-glucuronyltransferase and p-nitrophenol UDP-glucuronyltransferase

Prehibernation and hibernation effects on the d-3-hydroxybutyrate dehydrogenase of the heavy and light mitochondria from liver jerboa (Jaculus orientalis) and related metabolism

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