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  1. Article ; Online: Unravelling the complexity of enzyme catalysis.

    Scrutton, Nigel S

    The FEBS journal

    2023  Volume 290, Issue 9, Page(s) 2204–2207

    Abstract: The study of enzymes never disappoints. Despite its long history-almost 150 years following the first documented use of the word enzyme in 1878-the field of enzymology advances apace. This long journey has witnessed landmark developments that have ... ...

    Abstract The study of enzymes never disappoints. Despite its long history-almost 150 years following the first documented use of the word enzyme in 1878-the field of enzymology advances apace. This long journey has witnessed landmark developments that have defined modern enzymology as a broad discipline, leading to improved understanding at the molecular level, as we aspire to discover the complex relationships between enzyme structures, catalytic mechanisms and biological function. How enzymes are regulated at the gene and post-translational levels and how catalytic activity is modulated by interactions with small ligands and macromolecules, or the broader enzyme environment, are topical areas of study. Insights from such studies guide the exploitation of natural and engineered enzymes in biomedical or industrial processes; for example, in diagnostics, pharmaceuticals manufacture and processing technologies that use immobilised enzymes and enzyme reactor-based systems. In this Focus Issue, The FEBS Journal seeks to highlight breaking science and informative reviews, as well as personal reflections, to illustrate the breadth and importance of contemporary molecular enzymology research.
    MeSH term(s) Thermodynamics ; Catalysis ; Enzymes/genetics ; Enzymes/chemistry
    Chemical Substances Enzymes
    Language English
    Publishing date 2023-05-17
    Publishing country England
    Document type Editorial
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.16796
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  2. Article ; Online: Unravelling the complexity of enzyme catalysis

    Scrutton, Nigel S.

    The FEBS Journal. 2023 May, v. 290, no. 9 p.2204-2207

    2023  

    Abstract: The study of enzymes never disappoints. Despite its long history—almost 150 years following the first documented use of the word enzyme in 1878—the field of enzymology advances apace. This long journey has witnessed landmark developments that have ... ...

    Abstract The study of enzymes never disappoints. Despite its long history—almost 150 years following the first documented use of the word enzyme in 1878—the field of enzymology advances apace. This long journey has witnessed landmark developments that have defined modern enzymology as a broad discipline, leading to improved understanding at the molecular level, as we aspire to discover the complex relationships between enzyme structures, catalytic mechanisms and biological function. How enzymes are regulated at the gene and post‐translational levels and how catalytic activity is modulated by interactions with small ligands and macromolecules, or the broader enzyme environment, are topical areas of study. Insights from such studies guide the exploitation of natural and engineered enzymes in biomedical or industrial processes; for example, in diagnostics, pharmaceuticals manufacture and processing technologies that use immobilised enzymes and enzyme reactor‐based systems. In this Focus Issue, The FEBS Journal seeks to highlight breaking science and informative reviews, as well as personal reflections, to illustrate the breadth and importance of contemporary molecular enzymology research.
    Keywords catalytic activity ; diagnostic techniques ; drugs ; enzymes ; enzymology ; genes ; ligands ; manufacturing
    Language English
    Dates of publication 2023-05
    Size p. 2204-2207.
    Publishing place John Wiley & Sons, Ltd
    Document type Article ; Online
    Note EDITORIAL
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.16796
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  3. Article ; Online: Editorial overview: Catalysis and regulation: The chemistry of catalysis.

    Scrutton, Nigel S / Fujimori, Danica Galonić

    Current opinion in structural biology

    2022  Volume 77, Page(s) 102499

    Language English
    Publishing date 2022-11-10
    Publishing country England
    Document type Editorial
    ZDB-ID 1068353-7
    ISSN 1879-033X ; 0959-440X
    ISSN (online) 1879-033X
    ISSN 0959-440X
    DOI 10.1016/j.sbi.2022.102499
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  4. Article ; Online: Nonsterile microbial production of chemicals based on Halomonas spp.

    Zhang, Jing / Yan, Xu / Park, Helen / Scrutton, Nigel S / Chen, Tao / Chen, Guo-Qiang

    Current opinion in biotechnology

    2024  Volume 85, Page(s) 103064

    Abstract: The use of extremophile organisms such as Halomomas spp. can eliminate the need for fermentation sterilization, significantly reducing process costs. Microbial fermentation is considered a pivotal strategy to reduce reliance on fossil fuel resources; ... ...

    Abstract The use of extremophile organisms such as Halomomas spp. can eliminate the need for fermentation sterilization, significantly reducing process costs. Microbial fermentation is considered a pivotal strategy to reduce reliance on fossil fuel resources; however, sustainable processes continue to incur higher costs than their chemical industry counterparts. Most organisms require equipment sterilization to prevent contamination, a practice that introduces complexity and financial strain. Fermentations involving extremophile organisms can eliminate the sterilization process, relying instead on conditions that are conductive solely to the growth of the desired organism. This review discusses current challenges in pilot- and industrial-scale bioproduction when using the extremophile bacteria Halomomas spp. under nonsterile conditions.
    MeSH term(s) Halomonas ; Fermentation ; Bacteria
    Language English
    Publishing date 2024-01-22
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1052045-4
    ISSN 1879-0429 ; 0958-1669
    ISSN (online) 1879-0429
    ISSN 0958-1669
    DOI 10.1016/j.copbio.2023.103064
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  5. Article ; Online: Flavin oxidation state impacts on nitrofuran antibiotic binding orientation in nitroreductases.

    Toogood, Helen S / Scrutton, Nigel S

    The Biochemical journal

    2021  Volume 478, Issue 18, Page(s) 3423–3428

    Abstract: Nitroreductases catalyse the NAD(P)H-dependent nitro reduction in nitrofuran antibiotics, which activates them into cytotoxic molecules leading to cell death. The design of new effective nitrofuran antibiotics relies on knowledge of the kinetic mechanism ...

    Abstract Nitroreductases catalyse the NAD(P)H-dependent nitro reduction in nitrofuran antibiotics, which activates them into cytotoxic molecules leading to cell death. The design of new effective nitrofuran antibiotics relies on knowledge of the kinetic mechanism and nitrofuran binding mode of microbial nitroreductases NfsA and NfsB. This has been hampered by multiple co-crystallisation studies revealing ligand binding in non-electron transfer competent states. In a recent study by Day et al. (2021) the authors investigated the likely reaction mechanism and mode of nitrofurantoin binding to NfsA using potentiometry, global kinetics analysis, crystallography and molecular dynamics simulations. Their findings suggest nitrofurantoin reduction proceeds via a direct hydride transfer from reduced FMN, while the crystallographic binding orientation is an inhibitory complex. Molecular dynamics simulations suggest ligand binding orientations is dependent on the oxidation state of the FMN. This study highlights the importance of utilising computational studies alongside traditional crystallographic approaches, when multiple stable ligand binding orientations can occur.
    MeSH term(s) Anti-Bacterial Agents ; Escherichia coli/metabolism ; Flavins ; Kinetics ; Nitrofurans ; Nitroreductases/metabolism ; Oxidation-Reduction
    Chemical Substances Anti-Bacterial Agents ; Flavins ; Nitrofurans ; Nitroreductases (EC 1.7.-)
    Language English
    Publishing date 2021-09-23
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 2969-5
    ISSN 1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
    ISSN (online) 1470-8728
    ISSN 0006-2936 ; 0306-3275 ; 0264-6021
    DOI 10.1042/BCJ20210489
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    Uc I Zs.110: Show issues Location:
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  6. Article ; Online: PHA is not just a bioplastic!

    Park, Helen / He, Hongtao / Yan, Xu / Liu, Xu / Scrutton, Nigel S / Chen, Guo-Qiang

    Biotechnology advances

    2024  Volume 71, Page(s) 108320

    Abstract: Polyhydroxyalkanoates (PHA) have evolved into versatile biopolymers, transcending their origins as mere bioplastics. This extensive review delves into the multifaceted landscape of PHA applications, shedding light on the diverse industries that have ... ...

    Abstract Polyhydroxyalkanoates (PHA) have evolved into versatile biopolymers, transcending their origins as mere bioplastics. This extensive review delves into the multifaceted landscape of PHA applications, shedding light on the diverse industries that have harnessed their potential. PHA has proven to be an invaluable eco-conscious option for packaging materials, finding use in films foams, paper coatings and even straws. In the textile industry, PHA offers a sustainable alternative, while its application as a carbon source for denitrification in wastewater treatment showcases its versatility in environmental remediation. In addition, PHA has made notable contributions to the medical and consumer sectors, with various roles ranging from 3D printing, tissue engineering implants, and cell growth matrices to drug delivery carriers, and cosmetic products. Through metabolic engineering efforts, PHA can be fine-tuned to align with the specific requirements of each industry, enabling the customization of material properties such as ductility, elasticity, thermal conductivity, and transparency. To unleash PHA's full potential, bridging the gap between research and commercial viability is paramount. Successful PHA production scale-up hinges on establishing direct supply chains to specific application domains, including packaging, food and beverage materials, medical devices, and agriculture. This review underscores that PHA's future rests on ongoing exploration across these industries and more, paving the way for PHA to supplant conventional plastics and foster a circular economy.
    MeSH term(s) Polyhydroxyalkanoates/metabolism ; Biopolymers ; Food
    Chemical Substances Polyhydroxyalkanoates ; Biopolymers
    Language English
    Publishing date 2024-01-23
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 47165-3
    ISSN 1873-1899 ; 0734-9750
    ISSN (online) 1873-1899
    ISSN 0734-9750
    DOI 10.1016/j.biotechadv.2024.108320
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  7. Article ; Online: Enzymes make light work of hydrocarbon production.

    Scrutton, Nigel S

    Science (New York, N.Y.)

    2017  Volume 357, Issue 6354, Page(s) 872–873

    MeSH term(s) Enzymes ; Hydrocarbons ; Light ; Microalgae ; Photochemistry
    Chemical Substances Enzymes ; Hydrocarbons
    Language English
    Publishing date 2017-08-31
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.aao4399
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    Zs.A 27: Show issues Location:
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  8. Article ; Online: Alternative metabolic pathways and strategies to high-titre terpenoid production in

    Rinaldi, Mauro A / Ferraz, Clara A / Scrutton, Nigel S

    Natural product reports

    2022  Volume 39, Issue 1, Page(s) 90–118

    Abstract: Covering: up to 2021Terpenoids are a diverse group of chemicals used in a wide range of industries. Microbial terpenoid production has the potential to displace traditional manufacturing of these compounds with renewable processes, but further titre ... ...

    Abstract Covering: up to 2021Terpenoids are a diverse group of chemicals used in a wide range of industries. Microbial terpenoid production has the potential to displace traditional manufacturing of these compounds with renewable processes, but further titre improvements are needed to reach cost competitiveness. This review discusses strategies to increase terpenoid titres in
    MeSH term(s) Escherichia coli/metabolism ; Metabolic Engineering/methods ; Metabolic Networks and Pathways ; Terpenes/metabolism
    Chemical Substances Terpenes
    Language English
    Publishing date 2022-01-26
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2002546-4
    ISSN 1460-4752 ; 0265-0568
    ISSN (online) 1460-4752
    ISSN 0265-0568
    DOI 10.1039/d1np00025j
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  9. Article ; Online: Flavin doesn't put all oxygens in one basket.

    Leys, David / Scrutton, Nigel S

    Nature chemical biology

    2020  Volume 16, Issue 5, Page(s) 485–486

    MeSH term(s) Catalysis ; Flavins ; Mixed Function Oxygenases ; Oxygen
    Chemical Substances Flavins ; Mixed Function Oxygenases (EC 1.-) ; Oxygen (S88TT14065)
    Language English
    Publishing date 2020-04-22
    Publishing country United States
    Document type News ; Comment
    ZDB-ID 2202962-X
    ISSN 1552-4469 ; 1552-4450
    ISSN (online) 1552-4469
    ISSN 1552-4450
    DOI 10.1038/s41589-020-0523-z
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  10. Article ; Online: Catalysis by Nature's photoenzymes.

    Taylor, Aoife / Heyes, Derren J / Scrutton, Nigel S

    Current opinion in structural biology

    2022  Volume 77, Page(s) 102491

    Abstract: Photoenzymes use light to initiate biochemical reactions. Although rarely found in nature, their study has advanced understanding of how light energy can be harnessed to facilitate enzyme catalysis, which is also of importance to the design and ... ...

    Abstract Photoenzymes use light to initiate biochemical reactions. Although rarely found in nature, their study has advanced understanding of how light energy can be harnessed to facilitate enzyme catalysis, which is also of importance to the design and engineering of man-made photocatalysts. Natural photoenzymes can be assigned to one of two families, based broadly on the nature of the light-sensing chromophores used, those being chlorophyll-like tetrapyrroles or flavins. In all cases, light absorption leads to excited state electron transfer, which in turn initiates photocatalysis. Reviewed here are recent findings relating to the structures and mechanisms of known photoenzymes. We highlight recent advances that have deepened understanding of mechanisms in biological photocatalysis.
    Language English
    Publishing date 2022-10-30
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1068353-7
    ISSN 1879-033X ; 0959-440X
    ISSN (online) 1879-033X
    ISSN 0959-440X
    DOI 10.1016/j.sbi.2022.102491
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