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首页> 美国卫生研究院文献>other >Lyso-Phospholipid Micelles Sustain the Stability and Catalytic Activity of Diacylglycerol Kinase in the Absence of Lipids
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Lyso-Phospholipid Micelles Sustain the Stability and Catalytic Activity of Diacylglycerol Kinase in the Absence of Lipids

机译：溶血磷脂胶束延二酰基甘油激酶的稳定性和催化活性脂质的缺失

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There has been a renewal of interest in interactions of membrane proteins with detergents and lipids, sparked both by recent results that illuminate the structural details of these interactions and also by the realization that some experimental membrane protein structures are distorted by detergent-protein interactions. The integral membrane enzyme diacyglycerol kinase (DAGK) has long been thought to require the presence of lipid as an obligate “cofactor” in order to be catalytically viable in micelles. Here, we report that near-optimal catalytic properties are observed for DAGK in micelles composed of lyso-myristoylphosphatidylcholine (LMPC), with significant activity also being observed in micelles composed of lyso-myristoylphosphatidylglycerol and tetradecylphosphocholine. All three of these detergents were also sustained high stability of the enzyme. NMR measurements revealed significant differences in DAGK-detergent interactions involving LMPC micelles versus micelles composed of dodecylphosphocholine. These results highlight the fact that some integral membrane proteins can maintain native-like properties in lipid-free detergent micelles and also suggest that C14-based detergents may be worthy of more widespread use in studies of membrane proteins.

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