A GMC Oxidoreductase GmcA Is Required for Symbiotic Nitrogen Fixation in Rhizobium leguminosarum bv. viciae

Zou, Qian; Luo, Sha; Wu, Hetao; He, Donglan; Li, Xiaohua; Cheng, Guyue

doi:10.3389/fmicb.2020.00394

Cited by 3 publications

(1 citation statement)

References 53 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The GMC oxidoreductase superfamily harbors diverse enzymes with the function of catalyzing a wide variety of redox reactions such as the oxidation of an alcohol moiety to the corresponding aldehyde and the two-step oxidation of an alcohol moiety to the corresponding carboxylic acid [ 34 ]. For example, the choline dehydrogenase catalyzes the two-step oxidation of choline to glycine betaine [ 35 ]. In the current study, we found that capO presented a reverse-U expression pattern in Sphingomonas sp.…”

Section: Resultsmentioning

confidence: 99%

Deciphering chloramphenicol biotransformation mechanisms and microbial interactions via integrated multi-omics and cultivation-dependent approaches

Zhang

Klümper

et al. 2022

Microbiome

View full text Add to dashboard Cite

Background As a widely used broad-spectrum antibiotic, chloramphenicol is prone to be released into environments, thus resulting in the disturbance of ecosystem stability as well as the emergence of antibiotic resistance genes. Microbes play a vital role in the decomposition of chloramphenicol in the environment, and the biotransformation processes are especially dependent on synergistic interactions and metabolite exchanges among microbes. Herein, the comprehensive chloramphenicol biotransformation pathway, key metabolic enzymes, and interspecies interactions in an activated sludge-enriched consortium were elucidated using integrated multi-omics and cultivation-based approaches. Results The initial biotransformation steps were the oxidization at the C1-OH and C3-OH groups, the isomerization at C2, and the acetylation at C3-OH of chloramphenicol. Among them, the isomerization is an entirely new biotransformation pathway of chloramphenicol discovered for the first time. Furthermore, we identified a novel glucose-methanol-choline oxidoreductase responsible for the oxidization of the C3-OH group in Sphingomonas sp. and Caballeronia sp. Moreover, the subsequent biotransformation steps, corresponding catalyzing enzymes, and the microbial players responsible for each step were deciphered. Synergistic interactions between Sphingomonas sp. and Caballeronia sp. or Cupriavidus sp. significantly promoted chloramphenicol mineralization, and the substrate exchange interaction network occurred actively among key microbes. Conclusion This study provides desirable strain and enzyme resources for enhanced bioremediation of chloramphenicol-contaminated hotspot sites such as pharmaceutical wastewater and livestock and poultry wastewater. The in-depth understanding of the chloramphenicol biotransformation mechanisms and microbial interactions will not only guide the bioremediation of organic pollutants but also provide valuable knowledge for environmental microbiology and biotechnological exploitation.

show abstract

Section: Resultsmentioning

confidence: 99%