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TitleA synthetic cell-free pathway for biocatalytic upgrading of one-carbon substrates.
Journal, issue, pagesbioRxiv, Year 2024
Publish dateAug 8, 2024
AuthorsGrant M Landwehr / Bastian Vogeli / Cong Tian / Bharti Singal / Anika Gupta / Rebeca Lion / Edward H Sargent / Ashty S Karim / Michael C Jewett /
PubMed AbstractBiotechnological processes hold tremendous potential for the efficient and sustainable conversion of one-carbon (C1) substrates into complex multi-carbon products. However, the development of robust ...Biotechnological processes hold tremendous potential for the efficient and sustainable conversion of one-carbon (C1) substrates into complex multi-carbon products. However, the development of robust and versatile biocatalytic systems for this purpose remains a significant challenge. In this study, we report a hybrid electrochemical-biochemical cell-free system for the conversion of C1 substrates into the universal biological building block acetyl-CoA. The synthetic reductive formate pathway (ReForm) consists of five core enzymes catalyzing non-natural reactions that were established through a cell-free enzyme engineering platform. We demonstrate that ReForm works in a plug-and-play manner to accept diverse C1 substrates including CO equivalents. We anticipate that ReForm will facilitate efforts to build and improve synthetic C1 utilization pathways for a formate-based bioeconomy.
External linksbioRxiv / PubMed:39149402 / PubMed Central
MethodsEM (single particle)
Resolution2.18 - 2.3 Å
Structure data

45461

9cd3

EMDB-45461, PDB-9cd3:
Cryo-EM structure of Candidatus Saccharibacterium phosphoketolase complexed with thiamine diphosphate
Method: EM (single particle) / Resolution: 2.18 Å

45462

9cd4

EMDB-45462, PDB-9cd4:
Cryo-EM structure of Candidatus Saccharibacterium phosphoketolase complexed with 2-acetyl-thiamine diphosphate
Method: EM (single particle) / Resolution: 2.3 Å

Chemicals

ChemComp-TPP:
THIAMINE DIPHOSPHATE

ChemComp-HTL:
2-ACETYL-THIAMINE DIPHOSPHATE

Source
  • candidatus saccharibacteria bacterium (bacteria)
KeywordsLYASE / acetyl-phosphate synthase / glycolaldehyde dehydration / carbohydrate metabolic process / aldehyde-lyase activity

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