ArticleApplied and environmental microbiology2015
Reassessment of the transhydrogenase/malate shunt pathway in Clostridium thermocellum ATCC 27405 through kinetic characterization of malic enzyme and malate dehydrogenase.
Article in Applied and environmental microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 55 citations in OpenAlex.
- Effects of heterologous expression of glycolysis enzymes on product formation inMetabolic engineering communications · 2026Article
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- Pyrophosphate-free glycolysis in Clostridium thermocellum increases both thermodynamic driving force and ethanol titers.Biotechnology for biofuels and bioproducts · 2024Article
- Kinetic characterization of annotated glycolytic enzymes present in cellulose-fermenting Clostridium thermocellum suggests different metabolic roles.Biotechnology for biofuels and bioproducts · 2023Article
- The Roles of Nicotinamide Adenine Dinucleotide Phosphate Reoxidation and Ammonium Assimilation in the Secretion of Amino Acids as Byproducts of Clostridium thermocellum.Applied and environmental microbiology · 2023Article
- Increasing the Thermodynamic Driving Force of the Phosphofructokinase Reaction inApplied and environmental microbiology · 2022Article
- Functional Analysis of HApplied and environmental microbiology · 2022Article
- The PEP-pyruvate-oxaloacetate node: variation at the heart of metabolism.FEMS microbiology reviews · 2021Article
- Article
- Metabolic Fluxes of Nitrogen and Pyrophosphate in Chemostat Cultures of Clostridium thermocellum and Thermoanaerobacterium saccharolyticum.Applied and environmental microbiology · 2020Article
- Effects of COBMC microbiology · 2020Article
- Article
- Role of the malic enzyme in metabolism of the halotolerant methanotroph Methylotuvimicrobium alcaliphilum 20Z.PloS one · 2019Article
- Assessing Cofactor Usage inFrontiers in microbiology · 2019Article
- Investigating the Central Metabolism of Clostridium thermosuccinogenes.Applied and environmental microbiology · 2018Article
- Isotope-Assisted Metabolite Analysis Sheds Light on Central Carbon Metabolism of a Model Cellulolytic BacteriumFrontiers in microbiology · 2018Article
- Improved growth rate inBiotechnology for biofuels · 2017Article
- Development of a coreBiotechnology for biofuels · 2017Article
- CO2-fixing one-carbon metabolism in a cellulose-degrading bacterium Clostridium thermocellum.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Exploring complex cellular phenotypes and model-guided strain design with a novel genome-scale metabolic model of Clostridium thermocellum DSM 1313 implementing an adjustable cellulosome.Biotechnology for biofuels · 2016Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Clostridium thermocellum produces ethanol as one of its major end products from direct fermentation of cellulosic biomass. Therefore, it is viewed as an attractive model for the production of biofuels via consolidated bioprocessing. However, a better understanding of the metabolic pathways, along with their putative regulation, could lead to improved strategies for increasing the production of ethanol. In the absence of an annotated pyruvate kinase in the genome, alternate means of generating pyruvate have been sought. Previous proteomic and transcriptomic work detected high levels of a malate dehydrogenase and malic enzyme, which may be used as part of a malate shunt for the generation of pyruvate from phosphoenolpyruvate. The purification and characterization of the malate dehydrogenase and malic enzyme are described in order to elucidate their putative roles in malate shunt and their potential role in C. thermocellum metabolism. The malate dehydrogenase catalyzed the reduction of oxaloacetate to malate utilizing NADH or NADPH with a kcat of 45.8 s(-1) or 14.9 s(-1), respectively, resulting in a 12-fold increase in catalytic efficiency when using NADH over NADPH. The malic enzyme displayed reversible malate decarboxylation activity with a kcat of 520.8 s(-1). The malic enzyme used NADP(+) as a cofactor along with NH4 (+) and Mn(2+) as activators. Pyrophosphate was found to be a potent inhibitor of malic enzyme activity, with a Ki of 0.036 mM. We propose a putative regulatory mechanism of the malate shunt by pyrophosphate and NH4 (+) based on the characterization of the malate dehydrogenase and malic enzyme.
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