期刊
TRENDS IN BIOCHEMICAL SCIENCES
卷 28, 期 6, 页码 329-335出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/S0968-0004(03)00090-2
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资金
- NIDDK NIH HHS [DK02794] Funding Source: Medline
- NIGMS NIH HHS [R01 GM061355-04, R01 GM061355, GM56775, GM49245, R01 GM049245, R01 GM049245-11, GM61355, R01 GM056775] Funding Source: Medline
S-adenosyl-L-methionine (AdoMet) dependent methyl-transferases (MTases) are involved in biosynthesis, signal transduction, protein repair, chromatin regulation and gene silencing. Five different structural folds (I-V) have been described that bind AdoMet and catalyze methyltransfer to diverse substrates, although the great majority of known MTases have the Class I fold. Even within a particular MTase class the amino-acid sequence similarity can be as low as 10%. Thus, the structural and catalytic requirements for methyltransfer from AdoMet appear to be remarkably flexible.
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