The interaction of adeninylalkylcobalamins with ribonucleotide reductase.
Several structural analogs of adenosylcobalamin, containing 2, 3, 4, 5 and 6 methylene carbons instead of the ribofuranose moiety, have been synthesized and their interaction with ribonucleotide reductase from Lactobacillus leichmannii has been investigated. Kinetic studies of the inhibition of the reductase by these analogs showed that the adeninylalkylcobalamins with 4, 5 and 6 carbons interposed between the adenine moiety and the cobalt atom are potent inhibitors of ribonucleotide reduction. The stronger interaction between adeninylpentylcobalamin and the enzyme than that between adenosylcobalamin and the enzyme suggests that the more flexible acyclic analog of adenosine requires fewer adjustments of the protein upon binding.
D000818:Animals; D002854:Chromatography, Paper; D007700:Kinetics; D007778:Lactobacillus / Q000201:enzymology; D012264:Ribonucleotide Reductases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet; D014805:Vitamin B 12 / Q000138:chemical synthesis / Q000378:metabolism* / Q000494:pharmacology
D012264:Ribonucleotide Reductases; D014805:Vitamin B 12