Stereoinversion via Alcohol Dehydrogenases Enables Complete Catabolism of ..beta..-1-Type Lignin-Derived Aromatic Isomers

Ryo Kato, Kodai Maekawa, Shota Kobayashi, Shojiro Hishiyama, Rui Katahira, Miki Nambo, Yudai Higuchi, Eugene Kuatsjah, Gregg Beckham, Naofumi Kamimura, Eiji Masai

Research output: Contribution to journalArticlepeer-review


Sphingobium sp. strain SYK-6 is an efficient aromatic catabolic bacterium that can consume all four stereoisomers of 1,2-diguaiacylpropane-1,3-diol (DGPD), which is a ring-opened β-1-type dimer. Recently, LdpA-mediated catabolism of erythro-DGPD was reported in SYK-6, but the catabolic pathway for threo-DGPD was as yet unknown. Here, we elucidated the catabolism of threo-DGPD, which proceeds through conversion to erythro-DGPD. When threo-DGPD was incubated with SYK-6, the Ca hydroxy groups of threo-DGPD (DGPD I and II) were initially oxidized to produce the Ca carbonyl form (DGPDketo I and II). This initial oxidation step is catalyzed by Ca-dehydrogenases, which belong to the short-chain dehydrogenase/reductase (SDR) family and are involved in the catabolism of b-O-4-type dimers. Analysis of seven candidate genes revealed that NAD1-dependent LigD and LigL are mainly involved in the conversion of DGPD I and II, respectively. Next, we found that DGPD-keto I and II were reduced to erythro-DGPD (DGPD III and IV) in the presence of NADPH. Genes involved in this reduction were sought from Ca-dehydrogenase and ldpA-neighboring SDR genes. The gene products of SLG_12690 (ldpC) and SLG_12640 (ldpB) catalyzed the NADPH-dependent conversion of DGPD-keto I to DGPD III and DGPDketo II to DGPD IV, respectively. Mutational analysis further indicated that ldpC and ldpB are predominantly involved in the reduction of DGPD-keto. Together, these results demonstrate that SYK-6 harbors a comprehensive catabolic enzyme system to utilize all four β-1-type stereoisomers through successive oxidation and reduction reactions of the Cα hydroxy group of threo-DGPD with a net stereoinversion using multiple dehydrogenases. IMPORTANCE In many catalytic depolymerization processes of lignin polymers, aryl-ether bonds are selectively cleaved, leaving carbon-carbon bonds between aromatic units intact, including dimers and oligomers with β-1 linkages. Therefore, elucidating the catabolic system of β-1-type lignin-derived compounds will aid in the establishment of biological funneling of heterologous lignin-derived aromatic compounds to value-added products. Here, we found that threo-DGPD was converted by successive stereoselective oxidation and reduction at the Cα position by multiple alcohol dehydrogenases to erythro-DGPD, which is further catabolized. This system is very similar to that developed to obtain enantiopure alcohols from racemic alcohols by artificially combining two enantiocomplementary alcohol dehydrogenases. The results presented here demonstrate that SYK-6 has evolved to catabolize all four stereoisomers of DGPD by incorporating this stereoinversion system into its native β-1-type dimer catabolic system.

Original languageAmerican English
Number of pages19
JournalApplied and Environmental Microbiology
Issue number6
StatePublished - 2023

Bibliographical note

Publisher Copyright:
© 2023 American Society for Microbiology.

NREL Publication Number

  • NREL/JA-2A00-86481


  • alcohol dehydrogenase
  • aromatic compounds
  • catabolism
  • lignin
  • Sphingobium
  • stereoinversion
  • stereospecificity


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