Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation
Article Abstract:
The conformational changes that phosphoglycerate kinase (PGK) undergo during catalysis were examined by analyzing the 2.8 A crystal structure of a ternary complex of PGK from Trypanosoma brucie. PGK is a vital monomeric enzyme in glycolysis as it speeds up the transfer of a phosphoryl-group from 1,3-bis-phosphoglycerate to adenosine diphosphate to form 3-phosphoglycerate and adenosine triphosphate. Results show that PGK is a hinge-bending enzyme and that substrate-induced effects combine synergistically to generate major catalytic conformational changes.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Release of gelatinase A during platelet activation mediates aggregation
Article Abstract:
A blood platelet aggregation pathway that involves the proenzyme gelatinase A as an active agent has been discovered. The pathway, like those mediated by endoperoxides/thromboxane A2 and ADP1-3, promotes platelet aggregation after vascular injury or in various medical conditions such as thrombosis and metastasis. The research indicates that the presence of Gelatinase A stimulates physiological and pathological activity in platelets. They may be used in the future as anti-thrombotic agents.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
User Contributions:
Comment about this article or add new information about this topic:
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