Characterizing and predicting carboxylic acid reductase activity for diversifying bioaldehyde production

Matthew Moura*, Dante Pertusi, Stephen Lenzini, Namita Bhan, Linda J. Broadbelt, Keith E.J. Tyo

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

Chemicals with aldehyde moieties are useful in the synthesis of polymerization reagents, pharmaceuticals, pesticides, flavors, and fragrances because of their high reactivity. However, chemical synthesis of aldehydes from carboxylic acids has unfavorable thermodynamics and limited specificity. Enzymatically catalyzed reductive bioaldehyde synthesis is an attractive route that overcomes unfavorable thermodynamics by ATP hydrolysis in ambient, aqueous conditions. Carboxylic acid reductases (Cars) are particularly attractive, as only one enzyme is required. We sought to increase the knowledge base of permitted substrates for four Cars. Additionally, the Lys2 enzyme family was found to be mechanistically the same as Cars and two isozymes were also tested. Our results show that Cars prefer molecules where the carboxylic acid is the only polar/charged group. Using this data and other published data, we develop a support vector classifier (SVC) for predicting Car reactivity and make predictions on all carboxylic acid metabolites in iAF1260 and Model SEED. Biotechnol.

Original languageEnglish (US)
Pages (from-to)944-952
Number of pages9
JournalBiotechnology and Bioengineering
Volume113
Issue number5
DOIs
StatePublished - May 1 2016

Keywords

  • Carboxylic acid reductase
  • Enzyme promiscuity
  • Reductive aldehyde synthesis
  • Support vector machines

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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