Picture an enzyme at work
Article Abstract:
Pancreatic lipase is able to increase its catalytic activity when it is mixed with a lipid/water interface. This phenomenon has been termed as interfacial activation. The mechanistic basis for interfacial activation can be understood through knowledge gained from the structure of a human pancreatic lipase-colipase complex in mixed phospholipid/bile salt micelles. Mixed micelles in the crystallization solution forces the protein complex into a series of conformational rearrangement. This results in a binding site for the lipid substrate.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenase
Article Abstract:
Analysis of hydrogen tunnelling as a function of temperature using a thermophilic protein known as ADH-hT makes it possible to investigate how protein mobility influences the contribution of hydrogen tunnelling to the reaction rate. A comparison of the tunnelling behaviour for the thermophilic enzyme across a large temperature range indicates a role for protein mobility in C-H-bond cleavage. This research has significant implications for the catalytic behaviour of enzymes.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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Phosphotransfer hinges in PGK
Article Abstract:
Phosphoglycerate kinase (PKG) is a useful enzyme in both photosynthesis and glycolysis. To understand this small monomeric molecule's function in glycolysis, it is necessary to understand how its two substrates come in contact for the direct phosphotransfer mechanism to operate. Research shows that the two domains, particularly their bound substrates, are brought together in the catalytic cycle by a substantial 'hinge-bending' conformational change.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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