Alan Berry

Affiliations: 
1994- University of Leeds, Leeds, England, United Kingdom 
Area:
Molecular Enzymology, Directed evolution, Protein engineering, Aldolases, enzymes
Website:
https://astbury.leeds.ac.uk/people/alan-berry/
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"Alan Berry"
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Parents

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Peter 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
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