期刊
ADVANCED SYNTHESIS & CATALYSIS
卷 353, 期 1, 页码 89-99出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/adsc.201000719
关键词
aldol reaction; amino aldehydes; enzyme catalysis; L-rhamnulose-1-phosphate aldolase; muta-genesis
资金
- Spanish MICINN [CTQ2009-07359, CTQ2009-08328]
- Generalitat de Catalunya [2009 SGR 00281]
- ESF COST [CM0701]
- CSIC
The aldol addition of unphosphorylated dihydroxyacetone (DHA) to aldehydes catalyzed by L-rhamnulose-1-phosphate aldolase (RhuA), a dihydroxyacetone phosphate-dependent aldolase, is reported. Moreover, a single point mutation in the phosphate binding site of the RhuA wild type, that is, substitution of aspartate for asparagine at position N29, increased by 3-fold the V-max(app) of aldol addition reactions of DHA to other aldehyde acceptors rather than the natural L-lactaldehyde. The RhuA N29D mutant modified the optimum enzyme design for the natural substrate and changed its catalytic properties making the aldolase more versatile to other aldol additions of DHA.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据