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New-to-nature CO-dependent acetyl-CoA assimilation enabled by an engineered B-dependent acyl-CoA mutase.
Nat Commun
November 2024
Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch-Str. 10, Marburg, Germany.
Acetyl-CoA is a key metabolic intermediate and the product of various natural and synthetic one-carbon (C1) assimilation pathways. While an efficient conversion of acetyl-CoA into other central metabolites, such as pyruvate, is imperative for high biomass yields, available aerobic pathways typically release previously fixed carbon in the form of CO. To overcome this loss of carbon, we develop a new-to-nature pathway, the Lcm module, in this study.
View Article and Find Full Text PDFChemical Antiquity in Metabolism.
Acc Chem Res
August 2024
Institute of Molecular Evolution, Faculty of Mathematics and Natural Sciences, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.
ConspectusLife is an exergonic chemical reaction. The same was true when the very first cells emerged at life's origin. In order to live, all cells need a source of carbon, energy, and electrons to drive their overall reaction network (metabolism).
View Article and Find Full Text PDFCharacterization of a Structurally Distinct ATP-Dependent Reactivating Factor of Adenosylcobalamin-Dependent Lysine 5,6-Aminomutase.
Biochemistry
April 2024
Department of Chemistry, University of British Columbia, Okanagan Campus, 3247 University Way, Kelowna V1V 1V7, Canada.
Article Synopsis
- * 5,6-LAM requires ATP and isopeptide formation to function properly, but can become inactivated, necessitating the need for reactivation proteins, KamB and KamC, which were identified as crucial for this process.
- * KamBC enhances the reactivation of 5,6-LAM by replacing a damaged cofactor and is specific to 5,6-LAM, differing structurally from other known proteins that assist B12 enzyme activity.
Structural insight into G-protein chaperone-mediated maturation of a bacterial adenosylcobalamin-dependent mutase.
J Biol Chem
September 2023
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA; Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA; Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA. Electronic address:
G-protein metallochaperones are essential for the proper maturation of numerous metalloenzymes. The G-protein chaperone MMAA in humans (MeaB in bacteria) uses GTP hydrolysis to facilitate the delivery of adenosylcobalamin (AdoCbl) to AdoCbl-dependent methylmalonyl-CoA mutase, an essential metabolic enzyme. This G-protein chaperone also facilitates the removal of damaged cobalamin (Cbl) for repair.
View Article and Find Full Text PDFThe vitamin B analog cobinamide ameliorates azide toxicity in cells, , and mice.
Clin Toxicol (Phila)
April 2023
Department of Medicine, University of California, San Diego, CA, USA.
Context: The azide anion (N-) is highly toxic. It exists most commonly as sodium azide, which is used widely and is readily available, raising the potential for occupational incidents and use as a weapon of mass destruction. Azide-poisoned patients present with vomiting, seizures, hypotension, metabolic acidosis, and coma; death can occur.
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