Coenzyme preference of Streptococcus pyogenes δ1-pyrroline-5-carboxylate reductase: evidence supporting NADPH as the physiological electron donor

被引：0
|
作者：
Davide Petrollino
Giuseppe Forlani
机构：
[1] Università di Ferrara,Dipartimento di Biologia and Evoluzione
来源：
Amino Acids | 2012年 / 43卷
关键词：
Electron donor; Proline biosynthesis; Substrate ambiguity; Substrate binding;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
The streptococcal enzyme that catalyzes the last step in proline biosynthesis was heterologously expressed and the recombinant protein was purified to electrophoretic homogeneity and characterized thoroughly. As for δ1-pyrroline-5-carboxylate reductases from other sources, it was able to use either NADH or NADPH as the electron donor in vitro. However, with NADH the activity was markedly inhibited by physiological levels of NADP+. Results also strengthen the possibility that an unusual ordered substrate binding occurs, in which the dinucleotide binds last.
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页码：493 / 497
页数：4
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