Crystal structure of a trapped phosphoenzyme during a catalytic reaction.
The crystal structure of the fructose-2,6-bisphosphatase domain trapped during the reaction reveal a phosphorylated His 258, and a water molecule immobilized by the product, fructose-6-phosphate. The geometry suggests that the dephosphorylation step requires prior removal of the product for an 'associative in-line' phosphoryl transfer to the catalytic water.
Lee
Y H
YH
Olson
T W
TW
Ogata
C M
CM
Levitt
D G
DG
Banaszak
L J
LJ
Lange
A J
AJ
D000818:Animals; D002384:Catalysis; D018360:Crystallography, X-Ray; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005635:Fructosediphosphates / Q000737:chemistry* / Q000378:metabolism; D005636:Fructosephosphates / Q000494:pharmacology; D008099:Liver / Q000201:enzymology; D008958:Models, Molecular; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D025481:Phosphofructokinase-2; D010750:Phosphoproteins / Q000737:chemistry* / Q000378:metabolism; D010744:Phosphoric Monoester Hydrolases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D051381:Rats
D004791:Enzyme Inhibitors; D005635:Fructosediphosphates; D005636:Fructosephosphates; D010750:Phosphoproteins; C027618:fructose-6-phosphate; C027652:fructose 2,6-diphosphate; D025481:Phosphofructokinase-2; D010744:Phosphoric Monoester Hydrolases