Photolabelling of D‐β‐hydroxybutyrate apodehydrogenase with azidoaryl phospholipids

Kebbaj, M'Hammed Saïd El; Berrez, Jean-Marc; Lakhlifi, Tahar; Morpain, Claude; Latruffe, Norbert

doi:10.1016/0014-5793(85)81178-9

Cited by 12 publications

(4 citation statements)

References 27 publications

(4 reference statements)

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“…Dufourcq et al [16] have concluded that the sensitivity of cytochrome b5 to the phase transition is a consequence of the protein penetration in the hydrophobic core of the bilayer. In agreement with these conclusions, we previously demonstrated [15], using photolabelling of D-/J-hydroxybutyrate dehydrogenase with synthetic azidoaryl-phospholipids, that a portion ofthe enzyme polypeptide chain directly interacts with the hydrophobic moiety of phospholipids.…”

Section: Discussionsupporting

confidence: 77%

See 1 more Smart Citation

Interactions between apo-(d-β-hydroxybutyrate dehydrogenase) and phospholipids studied by intrinsic and extrinsic fluorescence

Kebbaj¹,

Latruffe²,

Monsigny³

et al. 1986

Biochemical Journal

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Interactions of D-beta-hydroxybutyrate dehydrogenase with phospholipids were investigated by both intrinsic- and extrinsic-fluorescence approaches. The intrinsic fluorescence, mainly caused by tryptophan residues, increased upon re-activation in the presence of phospholipids bearing a positive charge, i.e. phosphatidylcholine, but decreased in the presence of non-re-activating phospholipids with a negative charge. This indicates either that the environment of tryptophan residues is affected by charges rather than by hydrophobic chains of phospholipids, or that the enzyme undergoes different conformational changes depending on the nature of the phospholipids. On the other hand, the graph of the temperature-dependence of the fluorescence intensities of the enzyme embedded in dimyristoylphosphatidylcholine liposomes exhibits a break around 21 degrees C. This indicates either that at least one tryptophan residue is closely in contact with the hydrophobic chains of phospholipids or that there is a change in the environment of tryptophan residues owing to the physical state of the phospholipids. The addition of D-beta-hydroxybutyrate apo-dehydrogenase to phospholipid liposomes containing diphenylhexatriene (a fluorescent probe) increased the diphenylhexatriene fluorescence polarization. Moreover, there was a partial fluorescence energy transfer from tryptophan to diphenylhexatriene. These results strongly favour the possibility that there is a portion of the enzyme polypeptide chain inserted into the phospholipid hydrophobic region. All these results demonstrate that D-beta-hydroxybutyrate apo-dehydrogenase interacts with both polar and hydrophobic parts of phospholipids and leads to small, but essential, conformational changes of the enzyme.

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Section: Discussionsupporting

confidence: 77%

“…n.m.r. [11], specific chemical modifications of essential amino acid residues [12,13], controlled proteolysis [14], apoenzyme insertion into phospholipid monolayers [5] and interactions of the apo-dehydrogenase with photoactivable phospholipids [15].…”

Section: Introductionmentioning

confidence: 99%

Interactions between apo-(d-β-hydroxybutyrate dehydrogenase) and phospholipids studied by intrinsic and extrinsic fluorescence

Kebbaj¹,

Latruffe²,

Monsigny³

et al. 1986

Biochemical Journal

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“…T h e optical rotation of compound 13 is very close to that given in the literature (6, 7 (20)(21)(22)(23)(24)(25).…”

Section: I-0-hexndecyl-2-0-benzyl-sn-glycerol(l3)supporting

confidence: 85%

Synthesis and characterization of chemical intermediates of acyl or alkyl phospholipids

Nasser¹,

Morpain²,

Laude³

et al. 1992

Can. J. Chem.

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. Can. J. Chem. 70, 2319 (1992). Precursors of phospholipids or ether lipids were synthesized from ~-m a n n i t~l , i.e., 1-0-myristoyl-2-0-benzyl-sn-glycerol 11 and 1-0-hexadecyl-2-0-benzyl-sn-glycerol 13. The chemical pathways involved sequential protection reactions using allyl, triphenylmethyl, or benzyl groups via 3-0-allyl-sn-glycerol. Eleven intermediates were isolated and for the first time characterized with their spectrometric (especially 'H nmr) and physical parameters and yield. This work allowed preparation of chemically defined membrane phospholipids from compound 11 as well as ether lipids from compound 13 with cell mediator activities bearing different probes such as photoactivatable, fluorescent, or radioactive groups.

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“…The phospholipid composition of heavy and light mitoplasts at different jerboa states were significantly different especially concerning phosphatidylcholine, an activator of BDH (El Kebbaj et al, 1985;Loeb-Hennard and Mc Intyre, 2000), phosphatidylethanolamine and cardiolipin (table 4). 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.…”

Section: Discussionmentioning

confidence: 98%

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

Mountassif¹,

Kabine²,

Latruffe³

et al. 2007

Comparative Biochemistry and Physiology Part B: Biochemistry an

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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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Photolabelling of D‐β‐hydroxybutyrate apodehydrogenase with azidoaryl phospholipids

Cited by 12 publications

References 27 publications

Interactions between apo-(d-β-hydroxybutyrate dehydrogenase) and phospholipids studied by intrinsic and extrinsic fluorescence

Interactions between apo-(d-β-hydroxybutyrate dehydrogenase) and phospholipids studied by intrinsic and extrinsic fluorescence

Synthesis and characterization of chemical intermediates of acyl or alkyl phospholipids

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

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