Journal
ADVANCED SYNTHESIS & CATALYSIS
Volume 353, Issue 1, Pages 89-99Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/adsc.201000719
Keywords
aldol reaction; amino aldehydes; enzyme catalysis; L-rhamnulose-1-phosphate aldolase; muta-genesis
Categories
Funding
- Spanish MICINN [CTQ2009-07359, CTQ2009-08328]
- Generalitat de Catalunya [2009 SGR 00281]
- ESF COST [CM0701]
- CSIC
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available