[Coenzyme properties of adenosylcobalamin analogs with modifications in the purine nucleus of the alpha-ligand].
The interaction of cobalamin-dependent glycerol dehydratase from Klebsiella pneumoniae ATCC 25955 with two adenosylcobalamin analogs with modifications in the nucleotide alpha-ligand was studied. It was shown that substitution of 5,6-dimethylbenzimidazole of the alpha-ligand for adenine or 2-methyladenine does not alter the coenzyme activity of glycerol dehydratase and does not affect the substrate binding site of the holoenzyme. These adenosylcobalamin modifications change the affinity of the analogs for the apoenzyme.
D003038:Cobamides / Q000494:pharmacology*; D006836:Hydro-Lyases / Q000378:metabolism*; D007700:Kinetics; D007711:Klebsiella pneumoniae / Q000201:enzymology; D011485:Protein Binding; D013329:Structure-Activity Relationship
D003038:Cobamides; D006836:Hydro-Lyases; C020671:glycerol dehydratase; C000913:cobamamide
Kofermentnye svoĭstva analogov adenozilkobalamina s izmenennym purinovym iadrom al'fa-liganda.