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由于在产物释放前甲基旋转和烯醇化作用,脱氧核糖5 - 磷酸醛缩酶催化的反应中明显缺乏立体特异性。

An apparent lack of stereospecificity in the reaction catalysed by deoxyribose 5-phosphate aldolase due to methyl-group rotation and enolization before product release.

作者信息

Corina D L, Wilton D C

出版信息

Biochem J. 1976 Sep 1;157(3):573-6. doi: 10.1042/bj1570573.

Abstract

In the reaction catalysed by deoxyribose 5-phosphate aldolase (2-deoxy-D-ribose 5-phosphate acetaldehyde-lyase, EC 4.1.2.4) from Salmonella typhimurium, almost complete equilibration of the methyl-group protons of the product, acetaldehyde, occurs before its release from the enzyme surface. This phenomenon does not allow the stereo-chemical course of the reaction to be determined by using hydrogen-isotope labelling of the methyl group to generate a chiral centre.

摘要

在鼠伤寒沙门氏菌的脱氧核糖5-磷酸醛缩酶(2-脱氧-D-核糖5-磷酸乙醛裂解酶,EC 4.1.2.4)催化的反应中,产物乙醛的甲基质子在从酶表面释放之前几乎完全达到平衡。这种现象使得无法通过对甲基进行氢同位素标记以产生手性中心来确定反应的立体化学过程。

相似文献

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2-deoxyribose-5-phosphate aldolase of Salmonella typhimurium: purification and properties.
Arch Biochem Biophys. 1968 Sep 10;126(3):795-802. doi: 10.1016/0003-9861(68)90473-6.
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2-Deoxyribose 5-phosphate aldolase: genetic analyses of structure.
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