[HTML][HTML] Identification and characterisation of a new human glucose-6-phosphatase isoform

O Guionie, E Clottes, K Stafford, A Burchell - FEBS letters, 2003 - Elsevier
O Guionie, E Clottes, K Stafford, A Burchell
FEBS letters, 2003Elsevier
The liver endoplasmic reticulum glucose-6-phosphatase catalytic subunit (G6PC1) catalyses
glucose 6-phosphate hydrolysis during gluconeogenesis and glycogenolysis. The highest
glucose-6-phosphatase activities are found in the liver and the kidney; there have been
many reports of glucose 6-phosphate hydrolysis in other tissues. We cloned a new G6Pase
isoform (G6PC3) from human brain encoded by a six-exon gene (chromosome 17q21).
G6PC3 protein was able to hydrolyse glucose 6-phosphate in transfected Chinese hamster …
The liver endoplasmic reticulum glucose-6-phosphatase catalytic subunit (G6PC1) catalyses glucose 6-phosphate hydrolysis during gluconeogenesis and glycogenolysis. The highest glucose-6-phosphatase activities are found in the liver and the kidney; there have been many reports of glucose 6-phosphate hydrolysis in other tissues. We cloned a new G6Pase isoform (G6PC3) from human brain encoded by a six-exon gene (chromosome 17q21). G6PC3 protein was able to hydrolyse glucose 6-phosphate in transfected Chinese hamster ovary cells. The optimal pH for glucose 6-phosphate hydrolysis was lower and the Km higher relative to G6PC1. G6PC3 preferentially hydrolyzed other substrates including pNPP and 2-deoxy-glucose-6-phosphate compared to the liver enzyme.
Elsevier