Derewenda_1993_Trends.Biochem.Sci_18_20

Reference

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

Related information

Citations formats

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