酵母氨酸脱氢酶反应中氢转移的立体特异性

Stereospecificity of hydrogen transfer in the saccharopine dehydrogenase reaction.

作者信息

Fujioka M, Takata Y

出版信息

Biochim Biophys Acta. 1979 Sep 12;570(1):210-2. doi: 10.1016/0005-2744(79)90215-8.

Abstract

The stereospecificity of hydrogen transfer in the synthesis of saccharopine from alpha-ketoglutarate and L-lysine catalyzed by saccharopine dehydrogenase (N5-(1,3-dicarboxypropyl)-L-lysine: NAD oxidoreductase (L-lysine-forming), EC 1.5.1.7) was examined by using [4A-3H]- and [4B-3H]NADH. The enzyme showed the A-stereospecificity. The NMR analysis of the saccharopine prepared with [4"A-2H]NADH revealed that the label was incorporated into the C-2 of the glutaryl moiety.

摘要

通过使用[4A-³H]-和[4B-³H]NADH，研究了由saccharopine脱氢酶（N5-(1,3-二羧丙基)-L-赖氨酸：NAD氧化还原酶（形成L-赖氨酸），EC 1.5.1.7）催化从α-酮戊二酸和L-赖氨酸合成saccharopine过程中氢转移的立体特异性。该酶表现出A-立体特异性。用[4"A-²H]NADH制备的saccharopine的NMR分析表明，该标记掺入了戊二酰部分的C-2位。