The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Cytochrome P450: taming a wild type enzyme
Open accessAbstract
Protein engineering of cytochrome P450 monooxygenases (P450s) has been very successful in generating valuable non-natural activities and properties, allowing these powerful catalysts to be used for the synthesis of drug metabolites and in biosynthetic pathways for the production of precursors of artemisinin and paclitaxel. Collected experience indicates that the P450s are highly 'evolvable'--they are particularly robust to mutation in their active sites and readily accept new substrates and exhibit new selectivities. Their ability to adapt to new challenges upon mutation may reflect the nonpolar nature of their active sites as well as their high degree of conformational variability.
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Cites
Biocatalytic Asymmetric Synthesis of Chiral Amines from Ketones Applied to Sitagliptin Manufacture
Savile, C. K., Janey, J. M., Mundorff, E. C., Moore, J. C., Tam, S., Jarvis, W. R., Colbeck, J. C., Krebber, A., Fleitz, F. J., Brands, J., et al. (2010) · Science · doi:10.1126/science.1188934 · Cited by 1,756
Medicinal natural products: A biosynthetic approach
(2001) · European Journal of Medicinal Chemistry · doi:10.1016/s0223-5234(01)01302-2 · Cited by 1,700
Isoprenoid Pathway Optimization for Taxol Precursor Overproduction in Escherichia coli
Ajikumar, P. K., Xiao, W.-H., Tyo, K. E. J., Wang, Y., Simeon, F., Leonard, E., Mucha, O., Phon, T. H., Pfeifer, B., & Stephanopoulos, G. (2010) · Science · doi:10.1126/science.1191652 · Cited by 1,677
Enzyme promiscuity: A mechanistic and evolutionary perspective
Tawfik, O. K. A. D. S. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-030409-143718 · Cited by 1,355
Protein stability promotes evolvability
Bloom, J. D., Labthavikul, S. T., Otey, C. R., & Arnold, F. H. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510098103 · Cited by 1,211
Self-citationHydrocarbon Hydroxylation by Cytochrome P450 Enzymes
Ortiz de Montellano, P. R. (2010) · Chemical Reviews · doi:10.1021/cr9002193 · Cited by 1,164
Exploring protein fitness landscapes by directed evolution
Romero, P. A., & Arnold, F. H. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2805 · Cited by 1,161
Self-citationProtein Dynamism and Evolvability
Tokuriki, N., & Tawfik, D. S. (2009) · Science · doi:10.1126/science.1169375 · Cited by 940
Crystal structure of human cytochrome P450 2C9 with bound warfarin
Williams, P. A., Cosme, J., Ward, A., Angove, H. C., Matak Vinković, D., & Jhoti, H. (2003) · Nature · doi:10.1038/nature01862 · Cited by 821
Structural basis for ligand promiscuity in cytochrome P450 3A4
Ekroos, M., & Sjögren, T. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603236103 · Cited by 758
Cited by
Heme Enzyme Structure and Function
Poulos, T. L. (2014) · Chemical Reviews · doi:10.1021/cr400415k · Cited by 1,443
Hanamghar, S. S., Mellor, S. B., Mikkelsen, L., Crocoll, C., Motawie, M. S., Russo, D. A., Jensen, P. E., & Zedler, J. A. Z. (2025) · ACS Synthetic Biology · doi:10.1021/acssynbio.4c00800 · Cited by 9
Metadata
- Authors
- Jung, S. T., Lauchli, R., & Arnold, F. H.
- Venue
- Current Opinion in Biotechnology
- Publisher
- Elsevier BV
- Published
- 2011-12
- Volume
- 22
- Issue
- 6
- Pages
- 809-817
- ISSN
- 0958-1669 (ISSN-L)
- OpenAlex
- W2140615337
- Cited by
- 293
- References
- 38
- FWCI
- 1.54
- Type
- journal article
- Language
- en
- Open access
- bronze
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
