The scientist’s investigation covers issues in Stereochemistry, Biochemistry, Cytochrome P450, Active site and Oxidoreductase. His work deals with themes such as Biocatalysis, Chemical physics, Catalysis, Substrate and Electron transfer, which intersect with Stereochemistry. His study in the fields of Enzyme, Cofactor and Mutagenesis under the domain of Biochemistry overlaps with other disciplines such as PARG and Dehalobacter.
His Cytochrome P450 research is multidisciplinary, incorporating elements of Protein structure, Mycobacterium tuberculosis, Binding site and Heme. The Active site study combines topics in areas such as Steady state, Fatty-acid peroxygenase and Hydroxylation. His work carried out in the field of Oxidoreductase brings together such families of science as Dicoumarol, NADH Dehydrogenase, NAD+ kinase and Coumarin.
David Leys mainly focuses on Stereochemistry, Biochemistry, Enzyme, Cofactor and Oxidoreductase. His studies deal with areas such as Crystal structure, Heme, Active site, Substrate and Flavin group as well as Stereochemistry. David Leys has researched Active site in several fields, including Lyase and Binding site.
His Enzyme research includes themes of Mutagenesis, Mutant and Escherichia coli. His research investigates the connection with Cofactor and areas like Carboxylation which intersect with concerns in Biocatalysis. He has included themes like Halogenation and Fumarate reductase in his Oxidoreductase study.
His scientific interests lie mostly in Stereochemistry, Cofactor, Enzyme, Flavin group and Biochemistry. His Stereochemistry study combines topics from a wide range of disciplines, such as Oxidoreductase, Carboxylation, Active site, Decarboxylation and Substrate. His biological study spans a wide range of topics, including Lyase, Carboxylic acid and Electron transfer.
Reduction Activity, Sequence, Nonribosomal peptide, Docking and Adenylylation is closely connected to Aldehyde in his research, which is encompassed under the umbrella topic of Enzyme. His Flavin group research is multidisciplinary, relying on both Hydrolase, Isomerization and Prenylation, Prenyltransferase. His Cytochrome P450 study incorporates themes from Imidazole and Mycobacterium tuberculosis.
Stereochemistry, Cofactor, Enzyme, Biocatalysis and Active site are his primary areas of study. His studies in Stereochemistry integrate themes in fields like Oxidoreductase, Decarboxylation, Substrate, Flavin group and Prenyltransferase. His Cofactor study necessitates a more in-depth grasp of Biochemistry.
His work on Flavin mononucleotide, Binding site and Monoterpene as part of general Biochemistry research is often related to Streptomyces clavuligerus and Linalool, thus linking different fields of science. The concepts of his Enzyme study are interwoven with issues in Photosynthesis, Docking and Aldehyde. His Active site research incorporates themes from Combinatorial chemistry and Fragment-based lead discovery.
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P450 BM3: the very model of a modern flavocytochrome.
Andrew W Munro;David G Leys;Kirsty J McLean;Ker R Marshall.
Trends in Biochemical Sciences (2002)
Atomic description of an enzyme reaction dominated by proton tunneling
Laura Masgrau;Anna Roujeinikova;Linus O. Johannissen;Parvinder Hothi.
The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase.
Dea Slade;Mark S. Dunstan;Eva Barkauskaite;Ria Weston.
Overview of organohalide-respiring bacteria and a proposal for a classification system for reductive dehalogenases
Laura A. Hug;Farai Maphosa;David Leys;Frank E. Löffler;Frank E. Löffler.
Philosophical Transactions of the Royal Society B (2013)
Reductive dehalogenase structure suggests a mechanism for B12-dependent dehalogenation
Karl A. P. Payne;Carolina P. Quezada;Karl Fisher;Mark S. Dunstan.
Structure and mechanism of the flavocytochrome c fumarate reductase of Shewanella putrefaciens MR-1.
David Leys;Alexandre S. Tsapin;Kenneth H. Nealson;Terrance E. Meyer.
Nature Structural & Molecular Biology (1999)
New cofactor supports α,β-unsaturated acid decarboxylation via 1,3-dipolar cycloaddition
Karl A. P. Payne;Mark D. White;Karl Fisher;Basile Khara.
Atomic structure of Mycobacterium tuberculosis CYP121 to 1.06 Å reveals novel features of cytochrome P450
David G Leys;Christopher G. Mowat;Kirsty J McLean;Alison Richmond.
Journal of Biological Chemistry (2003)
Reengineering orthogonally selective riboswitches
Neil Dixon;John N. Duncan;Torsten Geerlings;Mark S. Dunstan.
Proceedings of the National Academy of Sciences of the United States of America (2010)
UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis
Mark D. White;Karl A. P. Payne;Karl Fisher;Stephen A. Marshall.
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