Redesign of the phosphate binding site of L -rhamnulose- 1-phosphate aldolase towards a dihydroxyacetone dependent aldolase

Xavier Garrabou, Jesús Joglar, Teodor Parella, Ramon Crehuet, Jordi Bujons, Pere Clapés

Research output: Contribution to journalArticleResearchpeer-review

35 Citations (Scopus)

Abstract

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 maxapp 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. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Original languageEnglish
Pages (from-to)89-99
JournalAdvanced Synthesis and Catalysis
Volume353
Issue number1
DOIs
Publication statusPublished - 10 Jan 2011

Keywords

  • aldol reaction
  • amino aldehydes
  • enzyme catalysis
  • L -rhamnulose-1-phosphate aldolase
  • mutagenesis

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