S-Adenosylmethionine-Dependent Methyltransferases
Structures and Functions
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Author
Contributions
- Robert M. Blumenthal (Editor) - Contributor
Publication
2000-07-01 - World Scientific Publishing Company
Language
English
Word Count
100,000 words, Guess
Page Count
400 pages
Physical Format
Hardcover
Identifiers
- Open LibraryOL9194971M
- ISBN-139789810238704
- ISBN-109810238703
- OCLC Control Number42749686
- OCLC Control Numbersadenosylmethion00chen
and 2 more
- Goodreads7171057
- LibraryThing6706587
Classifications
- LCCQP563.A3 S23 1999
Description
"This 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, proteins, polysaccharides, lipids, and a range of small molecules."--Jacket.
First Sentence
It was in the 1940s that Du Vigneaud and colleagues found that a substantial fraction of the methyl groups in cell metabolites derived from methionine, and in the 1950s [10] Cantoni and colleagues found that the actual methyl donor is the ATP-activated form of methionine, S-adenosyl-L-methionine (AdoMet).
Subjects
Other Editions
- S-Adenosylmethionine-Dependent Methyltransferases: Structures and Functions
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