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  1. Book ; Conference proceedings ; Audio / Video: 17th International Conference on Cytochrome P450

    Munro, Andrew W.

    biochemistry, biophysics and structure ; Manchester (UK), June 26 - 30, 2011

    2011  

    Event/congress International Conference on Cytochrome P 450 (17, 2011, Manchester)
    Author's details ed. Andrew W. Munro
    Subject code 612
    Language English
    Size 1 CD-ROM, 12 cm
    Publisher Medimond
    Publishing place Pianoro (Bologna)
    Publishing country Italy
    Document type Book ; Conference proceedings ; Audio / Video
    HBZ-ID HT017156640
    ISBN 978-88-7587-616-6 ; 88-7587-616-9
    Database Catalogue ZB MED Medicine, Health

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    2012 MO 125 order for loan Magazin

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  2. Article ; Online: Cytochrome P450 1A1 opens up to new substrates.

    Munro, Andrew W

    The Journal of biological chemistry

    2018  Volume 293, Issue 50, Page(s) 19211–19212

    Abstract: The cytochromes P450 (CYPs) oxidatively transform a huge number of substrates in both prokaryotic and eukaryotic organisms, but the mechanisms by which they accommodate these diverse molecules remain unclear. A new study by Bart and Scott reports two co- ... ...

    Abstract The cytochromes P450 (CYPs) oxidatively transform a huge number of substrates in both prokaryotic and eukaryotic organisms, but the mechanisms by which they accommodate these diverse molecules remain unclear. A new study by Bart and Scott reports two co-crystal structures of CYP1A1 that reveal structural rearrangements and flexible interaction networks that explain how the active site cavity shapes itself around new ligands. These data open the door to an increased understanding of fundamental enzyme behavior and improved searches for anti-cancer compounds.
    MeSH term(s) Catalytic Domain ; Crystallography, X-Ray ; Cytochrome P-450 CYP1A1/chemistry ; Cytochrome P-450 CYP1A1/metabolism ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/metabolism ; Erlotinib Hydrochloride/chemistry ; Erlotinib Hydrochloride/metabolism ; Furocoumarins/chemistry ; Furocoumarins/metabolism ; Humans ; Ligands ; Protein Binding ; Substrate Specificity
    Chemical Substances Enzyme Inhibitors ; Furocoumarins ; Ligands ; Erlotinib Hydrochloride (DA87705X9K) ; CYP1A1 protein, human (EC 1.14.14.1) ; Cytochrome P-450 CYP1A1 (EC 1.14.14.1) ; bergamottin (JMU611YFRB)
    Language English
    Publishing date 2018-12-14
    Publishing country United States
    Document type Introductory Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.H118.006715
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  3. Article: Computation-Aided Engineering of Cytochrome P450 for the Production of Pravastatin.

    Ashworth, Mark A / Bombino, Elvira / de Jong, René M / Wijma, Hein J / Janssen, Dick B / McLean, Kirsty J / Munro, Andrew W

    ACS catalysis

    2022  Volume 12, Issue 24, Page(s) 15028–15044

    Abstract: CYP105AS1 is a cytochrome P450 ... ...

    Abstract CYP105AS1 is a cytochrome P450 from
    Language English
    Publishing date 2022-11-28
    Publishing country United States
    Document type Journal Article
    ISSN 2155-5435
    ISSN 2155-5435
    DOI 10.1021/acscatal.2c03974
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  4. Article ; Online: A Promiscuous Bacterial P450: The Unparalleled Diversity of BM3 in Pharmaceutical Metabolism.

    Thistlethwaite, Sian / Jeffreys, Laura N / Girvan, Hazel M / McLean, Kirsty J / Munro, Andrew W

    International journal of molecular sciences

    2021  Volume 22, Issue 21

    Abstract: CYP102A1 (BM3) is a catalytically self-sufficient flavocytochrome fusion protein isolated ... ...

    Abstract CYP102A1 (BM3) is a catalytically self-sufficient flavocytochrome fusion protein isolated from
    MeSH term(s) Bacillus megaterium/enzymology ; Bacterial Proteins/metabolism ; Cytochrome P-450 Enzyme System/metabolism ; Inactivation, Metabolic ; NADPH-Ferrihemoprotein Reductase/metabolism
    Chemical Substances Bacterial Proteins ; Cytochrome P-450 Enzyme System (9035-51-2) ; NADPH-Ferrihemoprotein Reductase (EC 1.6.2.4) ; flavocytochrome P450 BM3 monoxygenases (EC 1.6.2.4)
    Language English
    Publishing date 2021-10-21
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms222111380
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  5. Article ; Online: Applications of microbial cytochrome P450 enzymes in biotechnology and synthetic biology.

    Girvan, Hazel M / Munro, Andrew W

    Current opinion in chemical biology

    2016  Volume 31, Page(s) 136–145

    Abstract: Cytochrome P450 enzymes (P450s) are a superfamily of monooxygenase enzymes with enormous potential for synthetic biology applications. Across Nature, their substrate range is vast and exceeds that of other enzymes. The range of different chemical ... ...

    Abstract Cytochrome P450 enzymes (P450s) are a superfamily of monooxygenase enzymes with enormous potential for synthetic biology applications. Across Nature, their substrate range is vast and exceeds that of other enzymes. The range of different chemical transformations performed by P450s is also substantial, and continues to expand through interrogation of the properties of novel P450s and by protein engineering studies. The ability of P450s to introduce oxygen atoms at specific positions on complex molecules makes these enzymes particularly valuable for applications in synthetic biology. This review focuses on the enzymatic properties and reaction mechanisms of P450 enzymes, and on recent studies that highlight their broad applications in the production of oxychemicals. For selected soluble bacterial P450s (notably the high-activity P450-cytochrome P450 reductase enzyme P450 BM3), variants with a multitude of diverse substrate selectivities have been generated both rationally and by random mutagenesis/directed evolution approaches. This highlights the robustness and malleability of the P450 fold, and the capacity of these biocatalysts to oxidise a wide range of chemical scaffolds. This article reviews recent research on the application of wild-type and engineered P450s in the production of important chemicals, including pharmaceuticals and drug metabolites, steroids and antibiotics. In addition, the properties of unusual members of the P450 superfamily that do not follow the canonical P450 catalytic pathway are described.
    MeSH term(s) Bacteria/enzymology ; Biotechnology ; Catalysis ; Crystallography, X-Ray ; Cytochrome P-450 Enzyme System/chemistry ; Cytochrome P-450 Enzyme System/metabolism ; Substrate Specificity
    Chemical Substances Cytochrome P-450 Enzyme System (9035-51-2)
    Language English
    Publishing date 2016-03-22
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 1439176-4
    ISSN 1879-0402 ; 1367-5931
    ISSN (online) 1879-0402
    ISSN 1367-5931
    DOI 10.1016/j.cbpa.2016.02.018
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  6. Article ; Online: Structure Based Discovery of Inhibitors of CYP125 and CYP142 from Mycobacterium tuberculosis.

    Katariya, Mona M / Snee, Matthew / Tunnicliffe, Richard B / Kavanagh, Madeline E / Boshoff, Helena I M / Amadi, Cecilia N / Levy, Colin W / Munro, Andrew W / Abell, Chris / Leys, David / Coyne, Anthony G / McLean, Kirsty J

    Chemistry (Weinheim an der Bergstrasse, Germany)

    2023  Volume 29, Issue 29, Page(s) e202203868

    Abstract: Mycobacterium tuberculosis (Mtb) was responsible for approximately 1.6 million deaths in 2021. With the emergence of extensive drug resistance, novel therapeutic agents are urgently needed, and continued drug discovery efforts required. Host-derived ... ...

    Abstract Mycobacterium tuberculosis (Mtb) was responsible for approximately 1.6 million deaths in 2021. With the emergence of extensive drug resistance, novel therapeutic agents are urgently needed, and continued drug discovery efforts required. Host-derived lipids such as cholesterol not only support Mtb growth, but are also suspected to function in immunomodulation, with links to persistence and immune evasion. Mtb cytochrome P450 (CYP) enzymes facilitate key steps in lipid catabolism and thus present potential targets for inhibition. Here we present a series of compounds based on an ethyl 5-(pyridin-4-yl)-1H-indole-2-carboxylate pharmacophore which bind strongly to both Mtb cholesterol oxidases CYP125 and CYP142. Using a structure-guided approach, combined with biophysical characterization, compounds with micromolar range in-cell activity against clinically relevant drug-resistant isolates were obtained. These will incite further development of much-needed additional treatment options and provide routes to probe the role of CYP125 and CYP142 in Mtb pathogenesis.
    MeSH term(s) Mycobacterium tuberculosis ; Cytochrome P-450 Enzyme System/metabolism ; Cholesterol/chemistry ; Drug Discovery ; Antitubercular Agents/pharmacology ; Antitubercular Agents/chemistry
    Chemical Substances Cytochrome P-450 Enzyme System (9035-51-2) ; Cholesterol (97C5T2UQ7J) ; Antitubercular Agents
    Language English
    Publishing date 2023-04-12
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 1478547-X
    ISSN 1521-3765 ; 0947-6539
    ISSN (online) 1521-3765
    ISSN 0947-6539
    DOI 10.1002/chem.202203868
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  7. Article ; Online: Drug targeting of heme proteins in Mycobacterium tuberculosis.

    McLean, Kirsty J / Munro, Andrew W

    Drug discovery today

    2017  Volume 22, Issue 3, Page(s) 566–575

    Abstract: TB, caused by the human pathogen Mycobacterium tuberculosis (Mtb), causes more deaths than any other infectious disease. Iron is crucial for Mtb to infect the host and to sustain infection, with Mtb encoding large numbers of iron-binding proteins. Many ... ...

    Abstract TB, caused by the human pathogen Mycobacterium tuberculosis (Mtb), causes more deaths than any other infectious disease. Iron is crucial for Mtb to infect the host and to sustain infection, with Mtb encoding large numbers of iron-binding proteins. Many of these are hemoproteins with key roles, including defense against oxidative stress, cellular signaling and regulation, host cholesterol metabolism, and respiratory processes. Various heme enzymes in Mtb are validated drug targets and/or products of genes essential for bacterial viability or survival in the host. Here, we review the structure, function, and druggability of key Mtb heme enzymes and strategies used for their inhibition.
    Language English
    Publishing date 2017-03
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1324988-5
    ISSN 1878-5832 ; 1359-6446
    ISSN (online) 1878-5832
    ISSN 1359-6446
    DOI 10.1016/j.drudis.2016.11.004
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  8. Article ; Online: Healthcare services use by patients with heart failure in Australia: Findings from the SHAPE study.

    Audehm, Ralph G / Neville, A Munro / Piazza, Peter / Haikerwal, Deepak / Sindone, Andrew P / Parsons, Richard W / Lim, Kevin / Liew, Danny

    Australian journal of general practice

    2022  Volume 51, Issue 9, Page(s) 713–720

    Abstract: Background and objectives: General practitioners (GPs) play a central role in healthcare, serving as the first point of contact, making appropriate referrals and coordinating care for chronic conditions such as heart failure (HF). We sought to determine ...

    Abstract Background and objectives: General practitioners (GPs) play a central role in healthcare, serving as the first point of contact, making appropriate referrals and coordinating care for chronic conditions such as heart failure (HF). We sought to determine healthcare use by people with HF in primary care.
    Method: In this Study of Heart failure in the Australian Primary carE setting (SHAPE), we analysed records of 1.93 million adult patients who attended a total of 43 practices between 1 July 2013 and 30 June 2018. We identified and examined the data of 20,219 patients with HF to describe the frequency of visits and use of Medicare Benefits Schedule items.
    Results: Patients with HF saw GPs 14.4 times per annum on average; 59.5% had a General Practice Management Plan (GPMP), 2.9% of GPMPs were reviewed annually or more frequently, and 46.8% of patients had been referred to a cardiologist. A total of 3761 had coexisting anxiety or depression, and of these 37.1% had a mental health plan.
    Discussion: Patients with HF visit their GP frequently, with many not reaching guideline therapy nor referred to cardiologists. Low use of care planning and reviews presents an opportunity for GPs to improve care.
    MeSH term(s) Adult ; Aged ; Australia ; Delivery of Health Care ; General Practitioners/psychology ; Heart Failure/epidemiology ; Heart Failure/therapy ; Humans ; National Health Programs
    Language English
    Publishing date 2022-08-31
    Publishing country Australia
    Document type Journal Article
    ZDB-ID 2924889-9
    ISSN 2208-7958 ; 2208-794X
    ISSN (online) 2208-7958
    ISSN 2208-794X
    DOI 10.31128/AJGP-10-21-6197
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  9. Article ; Online: Heme sensor proteins.

    Girvan, Hazel M / Munro, Andrew W

    The Journal of biological chemistry

    2013  Volume 288, Issue 19, Page(s) 13194–13203

    Abstract: Heme is a prosthetic group best known for roles in oxygen transport, oxidative catalysis, and respiratory electron transport. Recent years have seen the roles of heme extended to sensors of gases such as O2 and NO and cell redox state, and as mediators ... ...

    Abstract Heme is a prosthetic group best known for roles in oxygen transport, oxidative catalysis, and respiratory electron transport. Recent years have seen the roles of heme extended to sensors of gases such as O2 and NO and cell redox state, and as mediators of cellular responses to changes in intracellular levels of these gases. The importance of heme is further evident from identification of proteins that bind heme reversibly, using it as a signal, e.g. to regulate gene expression in circadian rhythm pathways and control heme synthesis itself. In this minireview, we explore the current knowledge of the diverse roles of heme sensor proteins.
    MeSH term(s) Animals ; Carbon Monoxide/metabolism ; Circadian Rhythm ; Gene Expression Regulation ; Guanylate Cyclase/metabolism ; Heme/metabolism ; Hemeproteins/genetics ; Hemeproteins/metabolism ; Homeostasis ; Humans ; Oxidation-Reduction ; Oxidative Stress ; Oxygen/metabolism
    Chemical Substances Hemeproteins ; Heme (42VZT0U6YR) ; Carbon Monoxide (7U1EE4V452) ; Guanylate Cyclase (EC 4.6.1.2) ; Oxygen (S88TT14065)
    Language English
    Publishing date 2013-03-28
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.R112.422642
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  10. Article ; Online: Unusual cytochrome p450 enzymes and reactions.

    Guengerich, F Peter / Munro, Andrew W

    The Journal of biological chemistry

    2013  Volume 288, Issue 24, Page(s) 17065–17073

    Abstract: Cytochrome P450 enzymes primarily catalyze mixed-function oxidation reactions, plus some reductions and rearrangements of oxygenated species, e.g. prostaglandins. Most of these reactions can be rationalized in a paradigm involving Compound I, a high- ... ...

    Abstract Cytochrome P450 enzymes primarily catalyze mixed-function oxidation reactions, plus some reductions and rearrangements of oxygenated species, e.g. prostaglandins. Most of these reactions can be rationalized in a paradigm involving Compound I, a high-valent iron-oxygen complex (FeO(3+)), to explain seemingly unusual reactions, including ring couplings, ring expansion and contraction, and fusion of substrates. Most P450s interact with flavoenzymes or iron-sulfur proteins to receive electrons from NAD(P)H. In some cases, P450s are fused to protein partners. Other P450s catalyze non-redox isomerization reactions. A number of permutations on the P450 theme reveal the diversity of cytochrome P450 form and function.
    MeSH term(s) Animals ; Biocatalysis ; Coenzymes/chemistry ; Coenzymes/physiology ; Cytochrome P-450 Enzyme System/chemistry ; Cytochrome P-450 Enzyme System/physiology ; Humans ; Hydroxylation ; Oxidation-Reduction ; Prostaglandins/biosynthesis ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/physiology
    Chemical Substances Coenzymes ; Prostaglandins ; Recombinant Fusion Proteins ; Cytochrome P-450 Enzyme System (9035-51-2)
    Language English
    Publishing date 2013-04-30
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.R113.462275
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