Crystal structure of a mono-and diacylglycerol lipase from Malassezia globosa reveals a novel lid co

来源 :2013年第四届全国“跨学科蛋白质研究”学术讨论会 | 被引量 : 0次 | 上传用户：xxxxkeat

【摘要】

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　　Most lipases contain a lid domain to shield the hydrophobic binding site from the water environment.The lid, mostly in helical form, can undergo a conformat

【作者】

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许婷婷刘璐侯淑琳徐进新杨博王永华刘劲松

【机构】

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中国科学院广州生物医药与健康研究院,广州510530华南理工大学轻工与食品学院,广州510006

【出处】

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2013年第四届全国“跨学科蛋白质研究”学术讨论会

【发表日期】

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2013年10期

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　　Most lipases contain a lid domain to shield the hydrophobic binding site from the water environment.The lid, mostly in helical form, can undergo a conformational change to expose the active cleft during the interfacial activation.

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Crystal structure of a mono-and diacylglycerol lipase from Malassezia globosa reveals a novel lid co

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