Literature DB >> 31756465

Penicillium camemberti galacturonate reductase: C-1 oxidation/reduction of uronic acids and substrate inhibition mitigation by aldonic acids.

Kurt Wagschal1, Douglas B Jordan2, William M Hart-Cooper3, Victor J Chan3.   

Abstract

The enzyme galacturonate oxidoreductase PcGOR from Penicillium camemberti reduces the C-1 carbon of D-glucuronate and C-4 epimer D-galacturonate to their corresponding aldonic acids, important reactions in both pectin catabolism and ascorbate biosynthesis. PcGOR was active on both glucuronic acid and galacturonic acid, with similar substrate specificities (kcat/Km) using the preferred co-substrate NADPH. Substrate acceptance extended to lactone congeners, and D-glucurono-3,6-lactone was converted to L-gulono-1,4-lactone, an immediate precursor of ascorbate. Reaction with glucuronate showed only minor substrate inhibition, and the product L-gulonate and L-gulono-1,4-lactone were both found to be competitive inhibitors with Ki in the low mM range. In contrast, reaction with C-4 epimer galacturonate displayed marked substrate inhibition. Moreover, the product L-galactonate and L-galactono-1,4-lactone were observed to mitigate substrate inhibition by galacturonate, with the lactone having a greater effect than the acid. Published by Elsevier B.V.

Entities:  

Keywords:  Aldaric acid; Aldonic acid; Food waste; Galacturonate reductase; Substrate inhibition

Year:  2019        PMID: 31756465     DOI: 10.1016/j.ijbiomac.2019.10.239

Source DB:  PubMed          Journal:  Int J Biol Macromol        ISSN: 0141-8130            Impact factor:   6.953


  1 in total

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

Authors:  Kaisa E Peltonen; Peter Richard
Journal:  Biotechnol Rep (Amst)       Date:  2022-06-02
  1 in total

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