| Title : News from the interface: the molecular structures of triacylglyceride lipases - Derewenda_1993_Trends.Biochem.Sci_18_20 |
| Author(s) : Derewenda ZS , Sharp AM |
| Ref : Trends in Biochemical Sciences , 18 :20 , 1993 |
|
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. |
| PubMedSearch : Derewenda_1993_Trends.Biochem.Sci_18_20 |
| PubMedID: 8438232 |
Derewenda ZS, Sharp AM (1993)
News from the interface: the molecular structures of triacylglyceride lipases
Trends in Biochemical Sciences
18 :20
Derewenda ZS, Sharp AM (1993)
Trends in Biochemical Sciences
18 :20