NADPH ACTIVATES A DECARBOXYLATION REACTION CATALYZED BY LAMB LIVER 6-PHOSPHOGLUCONATE DEHYDROGENASE
NADPH ACTIVATES A DECARBOXYLATION REACTION CATALYZED BY LAMB LIVER 6-PHOSPHOGLUCONATE DEHYDROGENASE
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DOI：
10.1016/0167-4838(92)90404-2
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发表时间：
1992-08-21
期刊：
影响因子：
--
通讯作者：
RIPPA, M
中科院分区：
文献类型：
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作者：
HANAU, S;DALLOCCHIO, F;RIPPA, M
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.
