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• W1964222798 startingPage "20" @default.
• W1964222798 abstract "Neutral lipases constitute one of the most ubiquitous and diverse families of enzymes. The recently solved crystal structures of three lipases show that enzymatic hydrolysis occurs with the assistance of a catalytic triad, which is structurally reminiscent of serine proteinases. However, these lipases only become active at the oil-water interface through a conformational change that exposes the active centre of the enzyme." @default.
• W1964222798 created "2016-06-24" @default.
• W1964222798 creator A5054600058 @default.
• W1964222798 creator A5055855625 @default.
• W1964222798 date "1993-01-01" @default.
• W1964222798 modified "2023-10-10" @default.
• W1964222798 title "News from the interface: the molecular structures of triacyglyceride lipases" @default.
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• W1964222798 doi "https://doi.org/10.1016/0968-0004(93)90082-x" @default.
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