Enantiospecific change in products for aldose reductase-mediated reaction of glyceraldehyde with bound NADP+.
Enantiospecific change in products for aldose reductase-mediated reaction of glyceraldehyde with bound NADP+.
复制标题
醛糖还原酶介导的甘油醛与结合的 NADP 反应产物的对映特异性变化。
DOI：
10.1016/0006-291x(91)91656-w
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发表时间：
1991
影响因子：
3.1
通讯作者：
Grimshaw,CE
中科院分区：
文献类型：
--
作者：
Grimshaw,CE
醛糖还原酶介导的甘油醛与酶结合的NADP+的反应根据所使用的对映体而产生不同的产物。D-甘油醛反应形成与之前表征的共价NADP-乙醇醛加合物类似的发色团（336 nm）[Grimshaw等人。1990 Biochemistry 29，9936-9946]。然而，在缓慢的稳态过程中反应形成额外的发色团，其光谱特性（λ max 290 nm，ε ≈ 16，700 M-1cm-1）表明烟酰胺5，6-双键已经发生水合作用。提出了几种机制来解释这种独特的立体异构体依赖的反应途径的变化。
Aldose reductase-mediated reaction of glyceraldehyde with enzyme-bound NADP+gives different products depending on the enantiomer used.D-Glyceraldehyde reacts to form a chromophore (336 nm) similar to the covalent NADP-glycolaldehyde adduct characterized previously [Grimshaw et al. 1990Biochemistry 29, 9936–9946].L-Glyceraldehyde, however, reacts in a slow steady-state process to form an additional chromophore whose spectral properties (λmax290 nm, ε ≈ 16,700 M−1cm−1) suggest that hydration of the nicotinamide 5,6-double bond has occurred. Several mechanisms are proposed to explain this unique stereoisomer-dependent change in reaction pathway.