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Structure of a Class I Tagatose-1,6-bisphosphate Aldolase
TLDR
Structural analysis indicates extensive active site conservation with respect to class I FBP aldolases, including conserved conformational responses to DHAP binding and conserved stereospecific proton transfer at the DHAP C3 carbon mediated by a proximal water molecule.
1 STRUCTURE OF A CLASS I TAGATOSE-1 , 6-BIPHOSPHATE ALDOLASE : STUDY INTO AN APPARENT LOSS OF STEREOSPECIFICITY
Tagatose-1,6-biphosphate (TBP) aldolase from Streptococcus pyogenes is a class I aldolase that exhibits a remarkable lack of chiral discrimination with respect to the configuration of hydroxyl groups
Celebrating crystallography from K to 12 at CIMF, Montreal
If crystallography is well known to many scientists, this is not true for the general public. Aims of the international year of crystallography include the desire to increase public awareness, to
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