Helena Schulz-Mirbach
@mirbachh
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Metabolic engineer for a better future 👩🏼🔬. Former Bar-Even member and PhD student @erblabs 🥳🪄.
Joined December 2021
RT @MichaelCJewett: What is needed to accelerate enzyme engineering using machine learning? #Data We develop a ML-guided platform that int…
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Major congrats to @NoamPrywes and everyone involved, very glad to see this work out !
Nature research paper: A map of the rubisco biochemical landscape
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RT @PabloINik: CIFR (Clone–Integrate–Flip-out–Repeat): A toolset for iterative #genome and pathway #engineering of Gram-negative #bacteria—…
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RT @PabloINik: Leveraging engineered #Pseudomonas putida minicells for bioconversion of organic acids into short-chain methyl ketones by @K…
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RT @biooekonomieDE: Ein Forschungsteam vom Max-Planck-Institut (@mpi_marburg) hat einen neuen Weg gefunden, CO2 wirkungsvoll zu fixieren u…
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Thanks for the highlight !
How to get a slow enzyme 🐌 to perform new tricks🏃 ? @mirbachh, @p__wichmann @erblabs, @AriSatanowski and colleagues have developed a new-to-nature #enzyme for efficient conversion of #CO2 into valuable products via AcetylCoA. 🌿🧪 #SynBio
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RT @AriSatanowski: Paper alert! 🎉 Excited to share this collaboration from my PhD time @wethebarevenlab and @erblabs! We built a new bridge…
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7 - This work had many contributors through the years – many thanks to all of them, and especially my co-first authors and amazing collaborators @p__wichmann , @arisatanowski, and of course @erblabs – it was an honour.
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6 - The mutations obtained in this evolution weren't targets we would have chosen for rational enzyme design – there is lots more for us to learn in the future. Hopefully, the Lcm lays a foundation to the success of new metabolism (for example CO2 fixation cycles!).
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5 - This #growth dependency combined with the eMutaT7 system for in vivo #mutagenesis and selection for improved activity yielded three Lcm variants with 5-10 fold efficiency improvements!
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4 - Indeed, the wild type Lcm activity was very slow (0.03 s-1) – but sufficed to support minute metabolic fluxes in vivo required for growth of a β-alanine #auxotrophic strain.
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3 - For this, we repurposed a 2-HIB-CoA mutase to interconvert 3-HP-CoA and lactyl-CoA (Lcm reaction). After characterizing the novel activity in vitro & showing its functionality within our acetyl-CoA assimilation route, we set out to generate better enzyme variants.
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2 - We identified the lactyl-CoA mutase reaction as #newtonature enzyme activity and used it to build the shortest oxygen tolerant route to condense CO2 with acetyl-CoA and make the C3 intermediate pyruvate from it.
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Despite its prevalence in #C1metabolism, the aerobic formation of gluconeogenic C3 compounds from acetyl-CoA has a pitfall: available routes either waste precious #carbon or are resource intensive. To overcome this limitation, we add a novel design to the pool: the Lcm module!
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