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D-fructose 6-phosphate
D-glucose 6-phosphate
D-fructose 6-phosphate
D-mannose 6-phosphate
D-galactose
D-tagatose
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D-glucose 6-phosphate
D-fructose 6-phosphate
D-Mannose 6-phosphate
D-Fructose 6-phosphate
fructose 6-phosphate
D-glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
Glucose 6-phosphate
Fructose 6-phosphate
L-talose
L-tagatose
best aldose substrate
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malonic dialdehyde
methylglyoxal
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additional information
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
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the enzyme is involved in the modified Embden-Meyerhof pathway
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
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the enzyme is involved in the modified Embden-Meyerhof pathway
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
Cassia coluteoides
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
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r
D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-glucose 6-phosphate
the isomerization occurrs by a cis-enediol intermediate involving C-1 pro-R hydrogen of D-fructose 6-phosphate. The presence of metal electrophile to activate the carbonyl group is required not only for the hydride shift mechanism but also for the operation of an enediol process
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D-fructose 6-phosphate
D-glucose 6-phosphate
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D-fructose 6-phosphate
D-mannose 6-phosphate
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D-fructose 6-phosphate
D-mannose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
Cassia coluteoides
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
multistep catalytic mechanism is proposed: first the enzyme catalyzes ring opening to yield the open chain form of the substrate. Then isomerization proceeds via proton transfer between C2 and C1 of a cis-enediol(ate) intermediate to yield the open chain form of the product. His388 promotes ring opening by protonating the ring oxygen. Glu216 helps to position His388, and a water molecule that is held in position by Lys518 and Thr214 accepts a proton from the hydroxyl group at C2
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D-glucose 6-phosphate
D-fructose 6-phosphate
the active site residues Lys58 and His388 might be involved in catalytic mechanism
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D-glucose 6-phosphate
D-fructose 6-phosphate
in the cytoplasm, it catalyzes the second step in glycolysis. Outside the cell, it serves as a nerve growth factor and cytokine
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
in hydride shift mechanism of catalysis Fe2+ is responsible for proton transfer between O1 and O2, and the hydride shift between C1 and C2 is favored by a markedly hydrophobic environment in the active site. The absence of any obvious enzymatic machinery for catalyzing ring opening of the sugar substrates suggests that the pyrococcal enzyme has a preference for straight chain substrates. The metabolism in extreme thermophiles may use sugars in both ring and straight chain forms. At the extreme temperatures in which Pyrococcus furiosus exists, the equilibrium would increasingly favor the open chain forms
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
the glucose 6-phosphate molecule is bound in an extended conformation in the active site of PGI, substrate binding structure, overview
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D-glucose 6-phosphate
D-fructose 6-phosphate
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D-glucose 6-phosphate
D-fructose 6-phosphate
the glucose 6-phosphate molecule is bound in an extended conformation in the active site of PGI, substrate binding structure, overview
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D-Mannose 6-phosphate
D-Fructose 6-phosphate
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D-Mannose 6-phosphate
D-Fructose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Glucose 6-phosphate
Fructose 6-phosphate
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Glucose 6-phosphate
Fructose 6-phosphate
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Glucose 6-phosphate
Fructose 6-phosphate
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Glucose 6-phosphate
Fructose 6-phosphate
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Glucose 6-phosphate
Fructose 6-phosphate
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Glucose 6-phosphate
Fructose 6-phosphate
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Glucose 6-phosphate
Fructose 6-phosphate
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Glucose 6-phosphate
Fructose 6-phosphate
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Glucose 6-phosphate
Fructose 6-phosphate
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Glucose 6-phosphate
Fructose 6-phosphate
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Glucose 6-phosphate
Fructose 6-phosphate
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Glucose 6-phosphate
Fructose 6-phosphate
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Glucose 6-phosphate
Fructose 6-phosphate
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Glucose 6-phosphate
Fructose 6-phosphate
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Glucose 6-phosphate
Fructose 6-phosphate
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Glucose 6-phosphate
Fructose 6-phosphate
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Glucose 6-phosphate
Fructose 6-phosphate
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Glucose 6-phosphate
Fructose 6-phosphate
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Glucose 6-phosphate
Fructose 6-phosphate
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Glucose 6-phosphate
Fructose 6-phosphate
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Glucose 6-phosphate
Fructose 6-phosphate
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additional information
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the multifunctional protein GPI shows specific and competitive inhibitory activity toward a myofibril-bound serine proteinase, MBSP, from Carassius auratus with a Ki of 320 nM, inhibition kinetics, while no inhibitory activity is identified toward other serine proteinases, such as white croaker MBSP and crucian carp trypsin, overview
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additional information
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the formation of phosphoglucose isomerase is under respiratory control, during anaerobiosis the enzyme is derepressed parallely with other glycolytic enzymes
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additional information
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the formation of phosphoglucose isomerase is under respiratory control, during anaerobiosis the enzyme is derepressed parallely with other glycolytic enzymes
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additional information
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the enzyme has cell-motility-stimulating activity on mouse colon cancer cells
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additional information
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the enzyme has cell-motility-stimulating activity on mouse colon cancer cells
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additional information
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the enzyme plays a central role in both the glycolysis and the gluconeogenesis pathways
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additional information
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the enzyme plays a central role in both the glycolysis and the gluconeogenesis pathways
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additional information
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PGI/AMF stimulates beta-catenin expression and is involved in E-cadherin and beta-catenin expression regulation, overview
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additional information
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the enzyme can also act as an autocrine motility factor, neuroleukin, and maturation factor
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additional information
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the enzyme can also act as an autocrine motility factor, neuroleukin, and maturation factor
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additional information
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the enzyme plays important roles in glycolysis and gluconeogenesis
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additional information
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the enzyme plays important roles in glycolysis and gluconeogenesis
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additional information
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the enzyme is part of the glycolytic pathway
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additional information
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glucose-6-phosphate isomerase catalyzes the interconversion between two different aldoses and ketose for pentoses and hexoses via two isomerization reactions. Activity order as follows: aldose substrates with hydroxyl groups oriented in the same direction at C2, C3, and C4 better than C2 and C4 better than C2 and C3 better than C3 and C4. L-Talose and D-ribulose exhibit the most preferred substrates among the aldoses and ketoses, respectively, substrate specificity, overview
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additional information
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glucose-6-phosphate isomerase catalyzes the interconversion between two different aldoses and ketose for pentoses and hexoses via two isomerization reactions. Activity order as follows: aldose substrates with hydroxyl groups oriented in the same direction at C2, C3, and C4 better than C2 and C4 better than C2 and C3 better than C3 and C4. L-Talose and D-ribulose exhibit the most preferred substrates among the aldoses and ketoses, respectively, substrate specificity, overview
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additional information
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enzyme does not convert mannose 6-phosphate to fructose 6-phosphate
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additional information
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enzyme does not convert mannose 6-phosphate to fructose 6-phosphate
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additional information
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glycolytic enzyme
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additional information
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enzyme of the oxidative pentose phosphate cycle
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additional information
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the isomerization occurs by a cis-enediol intermediate involving the C-1 pro-R hydrogen atom of fructose 6-phosphate. The presence of a metal electrophile to activate the carbonyl group is required not only for the hydride shift mechanism but also for the operation of an enediol process
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additional information
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the isomerization occurs by a cis-enediol intermediate involving the C-1 pro-R hydrogen atom of fructose 6-phosphate. The presence of a metal electrophile to activate the carbonyl group is required not only for the hydride shift mechanism but also for the operation of an enediol process
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additional information
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probable role of the enzyme in starch biosynthesis in amyloplasts
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additional information
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glycolytic enzyme
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additional information
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glycolytic enzyme
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