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Air-Mediated Biomimetic Synthesis of Polyhydroxyalkanoate with C4 Diol.
Angew Chem Int Ed Engl
December 2024
Chemistry and Chemical Engineering Guangdong Laboratory, 515031, Shantou, China.
Article Synopsis
- Poly(4-hydroxybutyrate) (P4HB) is a biodegradable polymer traditionally made through complex and costly genetic engineering processes involving 1,4-butanediol (BDO).
- A new catalytic method using a ruthenium-phosphine system for the oxidation of BDO has shown improved efficiency and cost-effectiveness, converting BDO into valuable products like γ-butyrolactone and oligomeric P4HB.
- This approach not only enhances production yield but also offers the potential for sustainable and large-scale manufacturing of high-value polyhydroxyalkanoates (PHAs) from non-grain feedstocks.
A High-Throughput Method for Directed Evolution of NAD(P)-Dependent Dehydrogenases for the Reduction of Biomimetic Nicotinamide Analogues.
ACS Catal
December 2019
Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, 32 West 7th Avenue, Tianjin Airport Economic Area, Tianjin 300308, China.
Engineering flavin-free NAD(P)-dependent dehydrogenases to reduce biomimetic nicotinamide analogues (mNADs) is of importance for eliminating the need for costly NAD(P) in coenzyme regeneration systems. Current redox dye-based screening methods for engineering the mNAD specificity of dehydrogenases are frequently encumbered by a background signal from endogenous NAD(P) and intracellular reducing compounds, making the detection of low mNAD-based activities a limiting factor for directed evolution. Here, we develop a high-throughput screening method, NAD(P)-eliminated solid-phase assay (NESPA), which can reliably identify mNAD-active mutants of dehydrogenases with a minimal background signal.
View Article and Find Full Text PDFImproved resistance to transition metals of a cobalt-substituted alcohol dehydrogenase 1 from Saccharomyces cerevisiae.
J Biotechnol
November 2001
Dipartimento di Biologia Animale e dell'Uomo, Università di Torino, Via Accademia Albertina 13, 10123, Torino, Italy.
Cobalt-substituted alcohol dehydrogenase 1 was purified from a yeast culture of Saccharomyces cerevisiae. Its reactivity towards different transition metals was tested and compared with the native zinc enzyme. The cobalt enzyme displayed a catalytic efficiency 100-fold higher than that of the zinc enzyme.
View Article and Find Full Text PDFFurther insights into the mechanism of action of methylmalonyl-CoA mutase by electron paramagnetic resonance studies.
Eur J Biochem
October 1997
Lehrstuhl für Biochemie, Universität Karlsruhe, Germany.
Novel analogues of methylmalonyl-CoA and succinyl-CoA have been prepared and used for mechanistic investigations on the coenzyme-B12-dependent methylmalonyl-CoA mutase. 1-Carboxyethyl-CoA (1) and 2-carboxyethyl-CoA (2) as well as their sulphoxides (3 and 4) were moderately good inhibitors with Ki values 4-20 times higher than the Km for succinyl-CoA. 2-Carboxyethyl-CoA (2) and its sulphoxide 4 induced EPR signals when bound to the enzyme-coenzyme-B12 complex.
View Article and Find Full Text PDFRemoval of substrate inhibition in a lactate dehydrogenase from human muscle by a single residue change.
FEBS Lett
December 1996
Molecular Recognition Centre and Department of Biochemistry, School of Medical Sciences, University Walk, Bristol, UK.
High concentrations of ketoacid substrates inhibit most natural hydroxyacid dehydrogenases due to the formation of an abortive enzyme-NAD+-ketoacid complex. It was postulated that this substrate inhibition could be eliminated from lactate dehydrogenases if the rate of NAD+ dissociation could be increased. An analysis of the crystal structure of mammalian LDHs showed that the amide of the nicotinamide cofactor formed a water-bridged hydrogen bond to S163.
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