The catalytic triad of the neutral lipase from Humicola lanuginosa is buried by a short helix
under aqueous conditions rendering the enzyme inactive. Upon adsorption to a lipid …

The already known X-ray structures of lipases provide little evidence about initial, discrete
structural steps occurring in the first phases of their activation in the presence of lipids …

Neutral lipases constitue one of the most ubiquitous and diverse families of enzymes. The
recently solved crystal structures of three lipases show that enzymatic hydrolysis occurs with …

We have investigated the binding properties of and dynamics in Humicola lanuginosa lipase
(Hll) and the inactive mutant S146A (active Ser146 substituted with Ala) using fluorescence …

Background: Lipases, a family of enzymes which catalyze the hydrolysis of triglycerides, are
widely distributed in many organisms. True lipases are distinguished from esterases by the …

Publisher Summary This chapter focuses on the current progress in crystallographic studies
of neutral lipases and the impact of these studies have on understanding of the structure …

Lipases that break down triglycerides to monoglycerides and glycerol are characterised by
low or no activity in water; in the presence of an oil/water interface, however, their activity …

The importance of Glu87 and Trp89 in the lid of Humicola lanuginosa lipase for the
hydrolytic activity at the water/lipid interface was investigated by site-directed mutagenesis. It …

After purification from the crude commercial preparation, the 3D structure of the synthetically
valuable lipase from Pseudomonas stutzeri (LipC) is described through homology …

Lipase from Pseudomonas aeruginosa is a M r, 29 kDa protein with a single functional
disulfide bond as shown by a shift in electrophoretic mobility after treatment with …