Identification of a D-galacturonate reductase efficiently using NADH as a cofactor

Kaisa E. Peltonen, Peter Richard (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

Abstract

D-galacturonate reductases are catalysing the reversible reduction of D-galacturonate to L-galactonate using NAD(P)H as a cofactor. The enzymes are part of two different pathways. One pathway is the fungal pathway for the catabolism of the main compound of pectin, D-galacturonate. The other pathway is a a pathway in plants for L-ascorbic acid synthesis. The previously described naturally occurring enzymes preferably use NADPH as a cofactor. Although certain D-galacturonate reductases, such as the reductases from Aspergillus niger or Euglena gracilis also accept NADH, their activity is significantly higher with NADPH. We identified in E. gracilis a gene, called gaa1, coding for a D-galacturonate reductase with similar activities with NADH and NADPH. It is potentially useful for the metabolic engineering of microbes to make use of pectin rich biomass.
Original languageEnglish
Article numbere00744
Pages (from-to)e00744
JournalBiotechnology Reports
Volume35
DOIs
Publication statusPublished - Sep 2022
MoE publication typeA1 Journal article-refereed

Keywords

  • Cofactor
  • D-galacturonic acid
  • EC 1.1.1.365
  • Saccharomyces cerevisiae

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