Alan Berry
Affiliations: | 1994- | University of Leeds, Leeds, England, United Kingdom |
Area:
Molecular Enzymology, Directed evolution, Protein engineering, Aldolases, enzymesWebsite:
https://astbury.leeds.ac.uk/people/alan-berry/Google:
"Alan Berry"Mean distance: (not calculated yet)
Parents
Sign in to add mentorPeter M. Shoolingin-Jordan | grad student | 1979-1983 | University of Southampton | |
(Mechanism of tetrapyrrole biosynthesis) | ||||
Duilio Arigoni | post-doc | 1983-1985 | ETH Zürich | |
Richard Perham | post-doc | 1985-1987 | Cambridge |
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Publications
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Branch J, Rajagopal BS, Paradisi A, et al. (2021) C-type cytochrome-initiated reduction of bacterial lytic polysaccharide monooxygenases. The Biochemical Journal |
Drulyte I, Obajdin J, Trinh CH, et al. (2019) Crystal structure of the putative cyclase IdmH from the indanomycin nonribosomal peptide synthase/polyketide synthase. Iucrj. 6: 1120-1133 |
Windle CL, Simmons KJ, Ault JR, et al. (2017) Extending enzyme molecular recognition with an expanded amino acid alphabet. Proceedings of the National Academy of Sciences of the United States of America |
Windle CL, Müller M, Nelson A, et al. (2014) Engineering aldolases as biocatalysts. Current Opinion in Chemical Biology. 19: 25-33 |
Daniels AD, Campeotto I, van der Kamp MW, et al. (2014) Reaction mechanism of N-acetylneuraminic acid lyase revealed by a combination of crystallography, QM/MM simulation, and mutagenesis. Acs Chemical Biology. 9: 1025-32 |
Timms N, Windle CL, Polyakova A, et al. (2013) Structural insights into the recovery of aldolase activity in N-acetylneuraminic acid lyase by replacement of the catalytically active lysine with γ-thialysine by using a chemical mutagenesis strategy. Chembiochem : a European Journal of Chemical Biology. 14: 474-81 |
Campeotto I, Bolt AH, Harman TA, et al. (2010) Structural insights into substrate specificity in variants of N-acetylneuraminic Acid lyase produced by directed evolution. Journal of Molecular Biology. 404: 56-69 |
Horsfall LE, Nelson A, Berry A. (2010) Identification and characterization of important residues in the catalytic mechanism of CMP-Neu5Ac synthetase from Neisseria meningitidis. The Febs Journal. 277: 2779-90 |
Campeotto I, Carr SB, Trinh CH, et al. (2009) Structure of an Escherichia coli N-acetyl-D-neuraminic acid lyase mutant, E192N, in complex with pyruvate at 1.45 angstrom resolution. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 65: 1088-90 |
Nelson A, Williams G, Woodhall T, et al. (2007) Stereochemically Complementary Biocatalysts Created by Directed Evolution Synfacts. 2007: 0208-0208 |