Coupling of the i-face and the active site of phospholipase A2 for interfacial activation.

Interfacial enzymes bind to organized interfaces where they access their substrates. As an example of interfacial activation, phospholipase A2 has an observed rate of hydrolysis of the sn-2-acyl chain of phospholipids at bilayer and micellar interfaces that is more than 1,000 times larger than with monodisperse phospholipids. The major challenge for the study of interfacial enzymes is to correlate the elementary steps of the interfacial function of the enzyme with the structure of the enzyme at the interface. Having kinetically resolved the steps of the interfacial turnover cycle, here we outline our recent (mostly since 2000) approaches to address remaining issues of interfacial activation and also the protocols that are likely to provide insights into the distinguishing structural features of the interface-activated enzyme.

NATURVETENSKAP Biologi Biokemi och molekylärbiologi hsv//swe
NATURAL SCIENCES Biological Sciences Biochemistry and Molecular Biology hsv//eng
Animals
Binding Sites
Enzyme Activation/physiology
Hydrolysis
Kinetics
Models; Molecular
Pancreas/enzymology
Phospholipases A/*chemistry
Phospholipids/chemistry
Surface Properties
Swine

Berg, Otto G.Uppsala universitet,Molekylär evolution(Swepub:uu)obe15246 (författare)
Uppsala universitetMolekylär evolution (creator_code:org_t)

Ingår i:Current opinion in chemical biology: Elsevier BV10:5, s. 473-4791367-59311879-0402

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