9HNF

Beta-keto acid cleavage enzyme from Paracoccus denitrificans with bound acetoacetate and acetyl-CoA

Summary for 9HNF

• Entry DOI: 10.2210/pdb9hnf/pdb
• Related: 8RIP 8RIQ
• Descriptor: 3-keto-5-aminohexanoate cleavage protein, ACETYL COENZYME *A, ACETOACETIC ACID, ... (5 entities in total)
• Functional Keywords: aldolase, acetyl-coa, acetoacetate, bkace, lyase
• Biological source: Paracoccus denitrificans PD1222
• Total number of polymer chains: 2
• Total formula weight: 74810.40

Authors

Marchal, D.G.,Zarzycki, J.,Erb, T.J. (deposition date: 2024-12-10, release date: 2025-04-16)

Primary citation

Satanowski, 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

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

Experimental method

X-RAY DIFFRACTION (2.1 Å)