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8RIP

Beta-keto acid cleavage enzyme from Paracoccus denitrificans with bound malonate and Coenzyme A

Summary for 8RIP
Entry DOI10.2210/pdb8rip/pdb
Descriptor3-keto-5-aminohexanoate cleavage protein, MALONATE ION, COENZYME A, ... (5 entities in total)
Functional Keywordsaldolase, coa, coenzyme a, bkace, lyase
Biological sourceParacoccus denitrificans PD1222
Total number of polymer chains4
Total formula weight147917.42
Authors
Marchal, D.G.,Zarzycki, J.,Erb, T.J. (deposition date: 2023-12-19, release date: 2025-01-01, Last modification date: 2025-04-16)
Primary citationSatanowski, A.,Marchal, D.G.,Perret, A.,Petit, J.L.,Bouzon, M.,Doring, V.,Dubois, I.,He, H.,Smith, E.N.,Pellouin, V.,Petri, H.M.,Rainaldi, V.,Nattermann, M.,Burgener, S.,Paczia, N.,Zarzycki, J.,Heinemann, M.,Bar-Even, A.,Erb, T.J.
Design and implementation of aerobic and ambient CO 2 -reduction as an entry-point for enhanced carbon fixation.
Nat Commun, 16:3134-3134, 2025
Cited by
PubMed Abstract: The direct reduction of CO into one-carbon molecules is key to highly efficient biological CO-fixation. However, this strategy is currently restricted to anaerobic organisms and low redox potentials. In this study, we introduce the CORE cycle, a synthetic metabolic pathway that converts CO to formate at aerobic conditions and ambient CO levels, using only NADPH as a reductant. Combining theoretical pathway design and analysis, enzyme bioprospecting and high-throughput screening, modular assembly and adaptive laboratory evolution, we realize the CORE cycle in vivo and demonstrate that the cycle supports growth of E. coli by supplementing C1-metabolism and serine biosynthesis from CO. We further analyze the theoretical potential of the CORE cycle as a new entry-point for carbon in photorespiration and autotrophy. Overall, our work expands the solution space for biological carbon reduction, offering a promising approach to enhance CO fixation processes such as photosynthesis, and opening avenues for synthetic autotrophy.
PubMed: 40169551
DOI: 10.1038/s41467-025-57549-4
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.81 Å)
Structure validation

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