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

Identification and characterisation of a new human glucose-6-phosphatase isoform
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DOI:
10.1016/s0014-5793(03)00903-7
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发表时间:
2003-09-11
期刊:
影响因子:
3.5
通讯作者:
Burchell, A
Burchell, A
中科院分区:
生物学3区
文献类型:
--
作者:
Guionie, O;Clottes, E;Burchell, A

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肝内质网葡萄糖-6-磷酸酶催化亚基(G6 PC 1)在糖原合成和糖原分解过程中催化葡萄糖-6-磷酸水解。葡萄糖-6-磷酸酶活性最高的是肝脏和肾脏;在其他组织中有许多葡萄糖-6-磷酸水解的报道。我们从人脑中克隆了一个新的G6 PC亚型(G6 PC 3),它由一个六外显子基因(染色体17 q21)编码。G6 PC 3蛋白能够在转染的中国仓鼠卵巢细胞中水解葡萄糖6-磷酸。葡萄糖6-磷酸水解的最适pH较低,K.相对于G6 PC 1。与肝酶相比,G6 PC 3优先水解其他底物,包括pNPP和2-脱氧葡萄糖-6-磷酸。(C)2003年欧洲生物化学学会联合会。Elsevier B. V.出版,保留所有权利。
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 K. higher relative to G6PC1. G6PC3 preferentially hydrolyzed other substrates including pNPP and 2-deoxy-glucose-6-phosphate compared to the liver enzyme. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.