316
Bhatia, S. (2018). Enzymes, proteins and bioinformatics. In Introduction to pharmaceutical biotechnology (2nd ed.). Bristol, UK: IOP Publishing. https://doi.org/10.1088/978- 0- 7503- 1302- 5ch1
Borro, L. C., Oliveira, S. R. M., Yamagishi, M. E. B., Mancini, A. L., Jardine, J. G., Mazoni, I., …
Neshich, G. (2006). Predicting enzyme class from protein structure using Bayesian classification. Genetics and Molecular Research, 5(1), 193–202.
Bugg, T. D. H. (2004). Introduction to enzyme and coenzyme chemistry (2nd ed.). Oxford, UK:
Blackwell Publishing Ltd.
Cai, Y. D., Zhou, G. P., & Chou, K. C. (2005). Predicting enzyme family classes by hybridizing
gene product composition and pseudo-amino acid composition. Journal of Theoretical Biology,
234(1), 145–149.
Creighton, T. E. (1993). Proteins (2nd ed.). New York, NY: W. H. Freeman and Company, 507pp.
Cuesta, S. M., Rahman, S. A., Furnham, N., & Thornton, J. M. (2015). The classification and
evolution of enzyme function. Biophysical Journal, 109, 1082–1086.
Danielson, M. A., & Falke, J. J. (1996). Use of 19F NMR to probe protein structure and conformational changes. Annual Review of Biophysics and Biomolecular Structure, 25, 163–195.
Dixon M, Webb EC (1979) Enzymes 3rd ed. Academic Press, New York, NY, 1116pp. Drauz K,
Waldmann H (2002) Enzyme catalysis in organic synthesis, vol II. Weinhein, Germany: Wiley
VCH, 998pp.
Dobson, P. D., & Doig, A. J. (2005). Predicting enzyme class from protein structure without alignments. Journal of Molecular Biology, 345(1), 187–199.
Feiten, M. C., Luccio, M. D., Santos, K. F., de Oliveira, D., & Oliveira, J. V. (2017). X-ray crystallography as a tool to determine three-dimensional structures of commercial enzymes subjected
to treatment in pressurized fluids. Applied Biochemistry and Biotechnology, 182(2), 429–451.
Geric, J. T. (1981). Fluorine magnetic resonance in biochemistry. In L. J. Berliner & J. Reuben
(Eds.), Biological magnetic resonance (Vol. 1, pp. 139–203). New York, NY: Plenum Press.
Helliwell, J. R. (2017). New developments in crystallography: exploring its technology, methods
and scope in the molecular biosciences. Bioscience Reports, 37, BSR20170204. https://doi.
org/10.1042/BSR20170204
Huang, C., & Kalodimos, C. G. (2017). Structures of large protein complexes determined by
nuclear magnetic resonance spectroscopy. Annual Review of Biophysics, 46, 317–336.
Ilari, A., & Savino, C. (2008). Protein structure determination by X-ray crystallography. In
J. M. Keith (Ed.), Bioinformatics, volume I: Data, sequence analysis, and evolution. Totowa,
NJ: Humana Press. https://doi.org/10.1007/978- 1- 60327- 159- 2
Illanes, A. (2008). Enzyme biocatalysis: Principles and applications. Dordrecht, Netherlands:
Springer.
Juncker, A. S., Jensen, L. J., Pierleoni, A., Bernsel, A., Tress, M. L., Bork, P., … Brunak, S. (2009).
Sequence-based feature prediction and annotation of proteins. Genome Biology, 10(2), 206.
Kaptein, R. (1982). Photo-CIDNP studies. In L. J. Berliner & J. Reuben (Eds.), Proteins in biological magnetic resonance (Vol. 4, pp. 145–191). New York, NY: Plenum Press.
Kersey, P. J., Allen, J. E., & Staines, D. M. (2014). Ensembl Genomes 2013: scaling up access to
genome-wide data. Nucleic Acids Research, 42, D546–D552.
Kevin, H., Lewis, G., & Kay, E. (1998). The use of 2H, 13C, 15N multidimensional NMR to
study the structure and dynamics of proteins. Annual Review of Biophysics and Biomolecular
Structure, 27, 357–406.
Kleywegt, G., Hoier, H., & Jones, T. (1996). A re-evaluation of the crystal structure of chloromuconate cycloisomerase. Acta Crystallographica. Section D, Biological Crystallography, 52,
858–863.
Kleywegt, G. J., Harris, M. R., Zou, J. Y., Taylor, T. C., Wahlby, A., & Jones, T. A. (2004).
The Uppsala Electron-Density server. Acta Crystallographica. Section D, Biological
Crystallography, 60, 2240–2249.
Kristensen, D. M., Ward, R. M., Lisewski, A. M., Erdin, S., Chen, B. Y., Fofanov, V. Y., …
Lichtarge, O. (2008). Prediction of enzyme function based on 3D templates of evolutionarily
important amino acids. BMC Bioinformatics, 9, 17.
S. A. Rather et al.
Bhatia, S. (2018). Enzymes, proteins and bioinformatics. In Introduction to pharmaceutical biotechnology (2nd ed.). Bristol, UK: IOP Publishing. https://doi.org/10.1088/978- 0- 7503- 1302- 5ch1
Borro, L. C., Oliveira, S. R. M., Yamagishi, M. E. B., Mancini, A. L., Jardine, J. G., Mazoni, I., …
Neshich, G. (2006). Predicting enzyme class from protein structure using Bayesian classification. Genetics and Molecular Research, 5(1), 193–202.
Bugg, T. D. H. (2004). Introduction to enzyme and coenzyme chemistry (2nd ed.). Oxford, UK:
Blackwell Publishing Ltd.
Cai, Y. D., Zhou, G. P., & Chou, K. C. (2005). Predicting enzyme family classes by hybridizing
gene product composition and pseudo-amino acid composition. Journal of Theoretical Biology,
234(1), 145–149.
Creighton, T. E. (1993). Proteins (2nd ed.). New York, NY: W. H. Freeman and Company, 507pp.
Cuesta, S. M., Rahman, S. A., Furnham, N., & Thornton, J. M. (2015). The classification and
evolution of enzyme function. Biophysical Journal, 109, 1082–1086.
Danielson, M. A., & Falke, J. J. (1996). Use of 19F NMR to probe protein structure and conformational changes. Annual Review of Biophysics and Biomolecular Structure, 25, 163–195.
Dixon M, Webb EC (1979) Enzymes 3rd ed. Academic Press, New York, NY, 1116pp. Drauz K,
Waldmann H (2002) Enzyme catalysis in organic synthesis, vol II. Weinhein, Germany: Wiley
VCH, 998pp.
Dobson, P. D., & Doig, A. J. (2005). Predicting enzyme class from protein structure without alignments. Journal of Molecular Biology, 345(1), 187–199.
Feiten, M. C., Luccio, M. D., Santos, K. F., de Oliveira, D., & Oliveira, J. V. (2017). X-ray crystallography as a tool to determine three-dimensional structures of commercial enzymes subjected
to treatment in pressurized fluids. Applied Biochemistry and Biotechnology, 182(2), 429–451.
Geric, J. T. (1981). Fluorine magnetic resonance in biochemistry. In L. J. Berliner & J. Reuben
(Eds.), Biological magnetic resonance (Vol. 1, pp. 139–203). New York, NY: Plenum Press.
Helliwell, J. R. (2017). New developments in crystallography: exploring its technology, methods
and scope in the molecular biosciences. Bioscience Reports, 37, BSR20170204. https://doi.
org/10.1042/BSR20170204
Huang, C., & Kalodimos, C. G. (2017). Structures of large protein complexes determined by
nuclear magnetic resonance spectroscopy. Annual Review of Biophysics, 46, 317–336.
Ilari, A., & Savino, C. (2008). Protein structure determination by X-ray crystallography. In
J. M. Keith (Ed.), Bioinformatics, volume I: Data, sequence analysis, and evolution. Totowa,
NJ: Humana Press. https://doi.org/10.1007/978- 1- 60327- 159- 2
Illanes, A. (2008). Enzyme biocatalysis: Principles and applications. Dordrecht, Netherlands:
Springer.
Juncker, A. S., Jensen, L. J., Pierleoni, A., Bernsel, A., Tress, M. L., Bork, P., … Brunak, S. (2009).
Sequence-based feature prediction and annotation of proteins. Genome Biology, 10(2), 206.
Kaptein, R. (1982). Photo-CIDNP studies. In L. J. Berliner & J. Reuben (Eds.), Proteins in biological magnetic resonance (Vol. 4, pp. 145–191). New York, NY: Plenum Press.
Kersey, P. J., Allen, J. E., & Staines, D. M. (2014). Ensembl Genomes 2013: scaling up access to
genome-wide data. Nucleic Acids Research, 42, D546–D552.
Kevin, H., Lewis, G., & Kay, E. (1998). The use of 2H, 13C, 15N multidimensional NMR to
study the structure and dynamics of proteins. Annual Review of Biophysics and Biomolecular
Structure, 27, 357–406.
Kleywegt, G., Hoier, H., & Jones, T. (1996). A re-evaluation of the crystal structure of chloromuconate cycloisomerase. Acta Crystallographica. Section D, Biological Crystallography, 52,
858–863.
Kleywegt, G. J., Harris, M. R., Zou, J. Y., Taylor, T. C., Wahlby, A., & Jones, T. A. (2004).
The Uppsala Electron-Density server. Acta Crystallographica. Section D, Biological
Crystallography, 60, 2240–2249.
Kristensen, D. M., Ward, R. M., Lisewski, A. M., Erdin, S., Chen, B. Y., Fofanov, V. Y., …
Lichtarge, O. (2008). Prediction of enzyme function based on 3D templates of evolutionarily
important amino acids. BMC Bioinformatics, 9, 17.
S. A. Rather et al.