醛糖还原酶介导的甘油醛与结合的烟酰胺腺嘌呤二核苷酸磷酸（NADP⁺）反应产物的对映体特异性变化。

Enantiospecific change in products for aldose reductase-mediated reaction of glyceraldehyde with bound NADP+.

作者信息

Grimshaw C E

机构信息

Lutcher Brown Department of Biochemistry, Whittier Institute for Diabetes and Endocrinology, La Jolla, CA 92037.

出版信息

Biochem Biophys Res Commun. 1991 Mar 29;175(3):943-8. doi: 10.1016/0006-291x(91)91656-w.

DOI:10.1016/0006-291x(91)91656-w

PMID:1902671

Abstract

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. (1990) Biochemistry 29, 9936-9946]. L-Glyceraldehyde, however, reacts in a slow steady-state process to form an additional chromophore whose spectral properties (lambda max 290 nm, epsilon approximately 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.

摘要

醛糖还原酶介导的甘油醛与酶结合的NADP⁺的反应会根据所使用的对映体产生不同的产物。D-甘油醛反应形成一种发色团（336nm），类似于先前表征的共价NADP-乙醇醛加合物[Grimshaw等人（1990年）《生物化学》29卷，9936 - 9946页]。然而，L-甘油醛以缓慢的稳态过程反应形成另一种发色团，其光谱特性（最大吸收波长290nm，摩尔吸光系数约为16,700 M⁻¹cm⁻¹）表明烟酰胺5,6-双键发生了水合作用。提出了几种机制来解释反应途径中这种独特的立体异构体依赖性变化。