Bacolla, A <br/><br/>
Recombinant human DNA (cytosine-5) methyltransferase. II. Steady-state kinetics reveal allosteric activation by methylated dna.  [electronic resource] 

 -  The Journal of biological chemistry  Nov 1999 
 - 33011-9 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0021-9258 
<br/><br/><label>Standard No.: </label>10.1074/jbc.274.46.33011  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Allosteric Regulation<br/>Binding Sites<br/>DNA (Cytosine-5-)-Methyltransferase 1<br/>DNA (Cytosine-5-)-Methyltransferases<br/>DNA Methylation<br/>DNA, Superhelical--chemistry<br/>DNA-Binding Proteins--chemistry<br/>Enzyme Activation<br/>Enzyme Inhibitors--pharmacology<br/>Humans<br/>Kinetics<br/>Oligodeoxyribonucleotides--chemistry<br/>Recombinant Proteins--chemistry<br/>Ribonucleoproteins, Small Nuclear--chemistry<br/>S-Adenosylhomocysteine--pharmacology<br/>S-Adenosylmethionine--chemistry<br/>Trinucleotide Repeats