H. Wilks

发表

A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework.

H. Muirhead, H. Wilks, K. Hart, 1988, Science.

Design and synthesis of new enzymes based on the lactate dehydrogenase framework.

H. Muirhead, H. Wilks, C. Dunn, 1991, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

An investigation of the contribution made by the carboxylate group of an active site histidine-aspartate couple to binding and catalysis in lactate dehydrogenase.

H. Wilks, W. Chia, D. Barstow, 1988, Biochemistry.

On the effect on specificity of Thr246----Gly mutation in L-lactate dehydrogenase of Bacillus sterothermophilus.

H. Wilks, K. Hart, J. Holbrook, 1989, Biochemical and biophysical research communications.

Rational construction of a 2-hydroxyacid dehydrogenase with new substrate specificity.

H. Wilks, K. Hart, W. Chia, 1987, Biochemical and biophysical research communications.

Enzymology below 200 K: The kinetics and thermodynamics of the photochemistry catalyzed by protochlorophyllide oxidoreductase

H. Wilks, C. Hunter, A. Ruban, 2002, Proceedings of the National Academy of Sciences of the United States of America.

NADPH:protochlorophyllide oxidoreductase from Synechocystis: overexpression, purification and preliminary characterisation

H. Wilks, C. Hunter, D. Heyes, 2000, FEBS letters.

The role of protein surface charge in catalytic activity and chloroplast membrane association of the pea NADPH: protochlorophyllide oxidoreductase (POR) as revealed by alanine scanning mutagenesis

H. Wilks, M. Timko, N. Lebedev, 2004, Plant Molecular Biology.

Designs for a broad substrate specificity keto acid dehydrogenase.

H. Wilks, W. Chia, T. Atkinson, 1990, Biochemistry.

A light-dependent complementation system for analysis of NADPH:protochlorophyllide oxidoreductase: identification and mutagenesis of two conserved residues that are essential for enzyme activity.

H. Wilks, M. Timko, H M Wilks, 1995, Proceedings of the National Academy of Sciences of the United States of America.

Purification and kinetic analysis of pea (Pisum sativum L.) NADPH:protochlorophyllide oxidoreductase expressed as a fusion with maltose-binding protein in Escherichia coli.

H. Wilks, M. Timko, G. E. Martin, 1997, The Biochemical journal.

Opportunities and limits in creating new enzymes. Experiences with the NAD-dependent lactate dehydrogenase frameworks of humans and bacteria.

H. Wilks, A. Clarke, J. Holbrook, 1992, Annals of the New York Academy of Sciences.

Alteration of enzyme specificity and catalysis by protein engineering.

H. Wilks, J. Holbrook, J.John Holbrook, 1991, Current opinion in biotechnology.

Mapping motion in large proteins by single tryptophan probes inserted by site-directed mutagenesis: lactate dehydrogenase.

H. Wilks, K. Hart, W. Chia, 1987, Biochemical Society transactions.

Construction of a stable dimer of Bacillus stearothermophilus lactate dehydrogenase.

R. Jackson, H. Wilks, J. Holbrook, 1992, Biochemistry.