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S-Adenosylmethionine-Dependent Methyltransferases: Structures And Functions
Abstract
This invaluable volume, written by an international group of scientists, presents an overview of the AdoMet-dependent methyltransferases, with special emphasis on structure-function relationships.S-adenosyl-L-methionine (AdoMet) is the second most commonly used enzyme cofactor after ATP. The AdoMet-dependent methyltransferases act on a wide variety of target molecules, including DNA, RNA, protein, polysaccharides, lipids and a range of small molecules.The well-conserved architecture of these enzymes, and the implications of this conservation for their evolutionary history, are major themes of this book. The thirteen chapters describe in detail the structures, enzyme kinetics and biological roles of the AdoMet-dependent methyltransferases from a wide range of cell types: plant, animal, bacterial and archaeal.
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Cited by
The Sulfur-Containing Amino Acids: An Overview
Brosnan, J. T., & Brosnan, M. E. (2006) · The Journal of Nutrition · doi:10.1093/jn/136.6.1636s · Cited by 1,220
James, S. J., Cutler, P., Melnyk, S., Jernigan, S., Janak, L., Gaylor, D. W., & Neubrander, J. A. (2004) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/80.6.1611 · Cited by 955
Many paths to methyltransfer: a chronicle of convergence
Schubert, H. L., Blumenthal, R. M., & Cheng, X. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00090-2 · Cited by 876
Self-citationZüst, R., Cervantes-Barragan, L., Habjan, M., Maier, R., Neuman, B. W., Ziebuhr, J., Szretter, K. J., Baker, S. C., Barchet, W., Diamond, M. S., et al. (2011) · Nature Immunology · doi:10.1038/ni.1979 · Cited by 811
Kobayashi, I. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.18.3742 · Cited by 513
Metadata
- Authors
- Cheng, X., & Blumenthal, R. M.
- Venue
- WORLD SCIENTIFIC eBooks
- Publisher
- WORLD SCIENTIFIC
- Published
- 1999-07
- DOI
- 10.1142/4098
- OpenAlex
- W655841519
- Cited by
- 321
- References
- 0
- FWCI
- 9.50
- Type
- book
- Language
- en
- Open access
- closed
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