David Leys

The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase

Dea Slade, Mark S. Dunstan, Eva Barkauskaite et al. · Nature · 2011 · 371 citations · Full text

Biochemistry, Natural Sciences, Biocatalysis +4

Atomic Description of an Enzyme Reaction Dominated by Proton Tunneling

Laura Masgrau, Anna Roujeinikova, Linus O. Johannissen et al. · Science · 2006 · 330 citations

Reaction Chemistry, Biochemistry, Protein Folding +12

Reductive dehalogenase structure suggests a mechanism for B12-dependent dehalogenation

K.A.P. Payne, Carolina Paz Quezada, Karl Fisher et al. · Nature · 2014 · 310 citations · Full text

Biochemistry, Natural Sciences, Biochemical Genetics +3

New cofactor supports α,β-unsaturated acid decarboxylation via 1,3-dipolar cycloaddition

K.A.P. Payne, Mark D. White, Karl Fisher et al. · Nature · 2015 · 235 citations · Full text

Organic Chemistry, New Cofactor, Enantioselective Synthesis +1

UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis

Mark D. White, K.A.P. Payne, Karl Fisher et al. · Nature · 2015 · 199 citations · Full text

Biosynthesis, Engineering, Synthetic Biology +8