Active site remodeling during the catalytic cycle in metal-dependent fructose-1,6-bisphosphate aldolases

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A conserved glutamate residue exhibits multifunctional catalytic roles in D-fructose-1,6-bisphosphate aldolases.

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Extended amino acid sequences around the active-site lysine residue of class-I fructose 1,6-bisphosphate aldolases from rabbit muscle, sturgeon muscle, trout muscle and ox liver.

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Removal of the growth medium and resuspension of Blastocladiella emersonii vegetative cells in a sporulation medium resulted in an abrupt fall of fructose 2,6-bisphosphate concentration to about 2% of its initial value within 10 min. The concentrations of hexose 6-phosphate and of fructose 1,6-bisphosphate also decreased by, respectively, three and tenfold over the same period. All these values...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 2018

ISSN: 0021-9258

DOI: 10.1074/jbc.ra117.001098