A stereochemical study of the mechanism of activation of donor oligonucleotides by RNA ligase from bacteriophage T4 infected Escherichia coli.
RNA ligase from bacteriophage T4 infected Escherichia coli catalyzes the activation of adenosine 3',5'-bisphosphate (representing the donor oligonucleotide) by adenosine 5'-[(S)-alpha-17O,alpha,alpha-18O2]triphosphate with retention of configuration at P alpha. Since single-step enzyme-catalyzed nucleotidyl transfer reactions proceed with inversion, this stereochemical result provides support for a double displacement mechanism involving an adenylyl-enzyme intermediate as proposed previously from isotope exchange experiments.
D000227:Adenine Nucleotides / Q000378:metabolism; D000249:Adenosine Monophosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D004789:Enzyme Activation; D004926:Escherichia coli / Q000201:enzymology*; D043564:Inorganic Pyrophosphatase; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D009841:Oligonucleotides / Q000378:metabolism*; D010103:Oxygen Isotopes; D011118:Polynucleotide Ligases / Q000378:metabolism*; D011755:Pyrophosphatases / Q000378:metabolism; D011130:RNA Ligase (ATP) / Q000378:metabolism*; D013604:T-Phages / Q000201:enzymology*
D000227:Adenine Nucleotides; D009841:Oligonucleotides; D010103:Oxygen Isotopes; C017990:adenosine 3'-diphosphate 5'-diphosphate; D000249:Adenosine Monophosphate; D000255:Adenosine Triphosphate; D011755:Pyrophosphatases; D043564:Inorganic Pyrophosphatase; D011118:Polynucleotide Ligases; D011130:RNA Ligase (ATP)