TY - JOUR
T1 - Many paths to methyltransfer
T2 - A chronicle of convergence
AU - Schubert, Heidi L.
AU - Blumenthal, Robert M.
AU - Cheng, Xiaodong
N1 - Funding Information:
We thank Osnat Herzberg and Steve Gamblin for early release of coordinates. H.L.S. was supported by grants from NIH (GM56775 and DK02794), R.M.B. was supported by a grant from the U.S. National Science Foundation (MCB-9904523), and X.C. was supported by NIH (GM49245 and GM61355) and the Georgia Research Alliance.
PY - 2003/6/1
Y1 - 2003/6/1
N2 - S-adenosyl-L-methionine (AdoMet) dependent methyltransferases (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.
AB - S-adenosyl-L-methionine (AdoMet) dependent methyltransferases (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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U2 - 10.1016/S0968-0004(03)00090-2
DO - 10.1016/S0968-0004(03)00090-2
M3 - Review article
C2 - 12826405
AN - SCOPUS:0038374971
SN - 0968-0004
VL - 28
SP - 329
EP - 335
JO - Trends in Biochemical Sciences
JF - Trends in Biochemical Sciences
IS - 6
ER -