Journal of Molecular Biology
Regular ArticleEntropy in Bi-substrate Enzymes: Proposed Role of an Alternate Site in Chaperoning Substrate into, and Products out of, Thymidylate Synthase
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Cited by (23)
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2004, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Interestingly, the adenine ring of AMPCPP occupies a binding pocket similar to that in which the anthraniloyl group of 2′d3′ANT-ATP binds. Such alternate binding of substrate analogs in crystal soaking is not uncommon and has been found in crystal structures of other enzymes such as thymidylate synthase from Lactobacillus casei[28]. As described above, the triphosphate portions of AMPCPP and 3′dATP are similar in their binding to the catalytic site of EF3, while the adenosines of these two non-cyclizable ATP analogs differ drastically in their binding to EF3.
Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase
2003, Journal of Biological ChemistryCitation Excerpt :Ligand-induced flexibility in loop 355 in an early complex of the SHMT reaction may be coupled to limited disorder of the pteridine-binding groups of the active site and to multiple conformations of the tetrahydropyrazine ring that are necessary to realize productive binding of a single conformer in a subsequent reaction step. A pre-binding folate site has also been proposed for a folate-soaked complex of thymidylate synthase (55). Two studies have previously used chemical modification to locate the folate-binding site on SHMT.
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