Journal of Molecular Biology
Volume 193, Issue 1, 5 January 1987, Pages 171-187
Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 Å resolution☆
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Crystal structures of a dual coenzyme specific glyceraldehyde-3-phosphate dehydrogenase from the enteric pathogen Campylobacter jejuni
2021, Journal of Molecular StructureCitation Excerpt :The crystal structure of CjGAPDH-ADP reveals a second SO42− binding site that interacts with Lys193. This binding site does not match with Pi binding site of formerly published structures [13] where the SO42- ions are coordinated by the Thr208, Ser148 and Gly209 residues (Fig. 4). The superimposition of a subunit of CjGAPDHNAD(P+) and CjGAPDH-ADP complexes shows the local conformational alterations taking place when the coenzyme is substituted by ADP.
Part-of-the-sites binding and reactivity in the homooligomeric enzymes – facts and artifacts
2018, Archives of Biochemistry and Biophysics
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The research was funded by the Medical Research Council of Great Britain. P.C.E.M. was the holder of an SERC studentship.
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On leave from the University of Lódź, Poland.
Copyright © 1987 Published by Elsevier Ltd.