[Oligomerization of DNA-(adenine-N6)-methyltransferase from phage T4 and its effect on the catalytic characteristics of the enzyme].
The structural and catalytic properties of the phage T4 DNA-(adenine-N6)-methyltransferase (EC 2.1.1.72) were studied at different enzyme-substrate concentration ratios by chemical cross-linking of the protein subunits and by measuring the presteady state kinetics of the reactions. Various structural states of the methyltransferase were correlated with its catalytic activity, and it was shown that the oligomeric forms of the enzyme are catalytically active but are characterized by the reaction parameters different from those of the monomer.
Ovechkina
L G
LG
Zinov'ev
V V
VV
Gorbunov
Iu A
IuA
Malygin
E G
EG
D017122:Bacteriophage T4 / Q000201:enzymology*; D001483:Base Sequence; D001704:Biopolymers / Q000737:chemistry*; D002384:Catalysis; D017931:DNA Primers; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific) / Q000378:metabolism*
D001704:Biopolymers; D017931:DNA Primers; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific)
Oligomerizatsiia DNK-(adenin-N6)-metiltransferazy faga T4 i ee vliianie na katalitcheskie kharakteristiki fermenta.