NADPH ACTIVATES A DECARBOXYLATION REACTION CATALYZED BY LAMB LIVER 6-PHOSPHOGLUCONATE DEHYDROGENASE

被引：23

作者：

HANAU, S ^{[1
]}

DALLOCCHIO, F ^{[1
]}

RIPPA, M ^{[1
]}

机构：

[1] UNIV FERRARA,IST CHIM BIOL,VIA LUIGI BORSARI 46,I-44100 FERRARA,ITALY

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1992年 / 1122卷 / 03期

关键词：

PHOSPHOGLUCONATE DEHYDROGENASE; OXIDATIVE DECARBOXYLATION; ENZYME MECHANISM; PHOSPHODEOXYGLUCONATE; (LAMB LIVER);

D O I：

10.1016/0167-4838(92)90404-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

NADP-dependent lamb liver 6-phosphogluconate deydrogenase catalyses the oxidative decarboxylation of 2-deoxy-6-phospho-gluconate, an analogue of the natural substrate. The first products of the reaction are NADPH and 3-keto-2-deoxy-6-phospho-gluconate. The NADPH, released from the enzyme, binds to the coenzyme site of the same or the other subunit, activating the decarboxylation reaction in which has not a redox role, since it can be substituted by an analogue devoid of enzymatic redox power. These findings are compared to those obtained with other NADP-dependent decarboxylating dehydrogenases.

引用

页码：273 / 277

页数：5

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