5.4.3.5	5'-deoxyadenosylcobalamin	-	747193, 747565, 748182	
5.4.3.5	5'-deoxyadenosylcobalamin	Km value 0.00043	652199	
5.4.3.5	5'-deoxyadenosylcobalamin	shows ability to produce highly reactive 5'-deoxyadenosyl radical in enzymatic environments	727644	
5.4.3.5	adenosylcobalamin	-	704658	
5.4.3.5	adenosylcobalamin	binding analysis with recombinant wild-type and mutant enzymes, overview	727036	
5.4.3.5	adenosylcobalamin	dependent on	693191, 727677, 747073	
5.4.3.5	adenosylcobalamin	paramagnetic Co2+ metal center of the cob(II)alamin cofactor	727131	
5.4.3.5	additional information	adenosylcobalamin-dependent ornithine 4,5-aminomutase from Clostridium sticklandii utilizes pyridoxal 5'-phosphate to interconvert D-ornithine to 2,4-diaminopentanoate via a multistep mechanism that involves two hydrogen transfer steps	747073	
5.4.3.5	additional information	ornithine 4,5-aminomutase is a 5'-deoxyadenosylcobalamin and pyridoxal 5'-phosphate co-dependent radical enzyme. Identification of a dynamic interface between the cobalamin and pyridoxal 5'-phosphate-binding domains, overview. Following ligand binding-induced cleavage of the Lys629-pyridoxal 5'-phosphate covalent bond, dynamic motion of the cobalamin-binding domain leads to conformational sampling of the available space. This supports radical catalysis through transient formation of a catalytically competent active state. Crucially, it appears that the formation of the state containing both a substrate/product radical and Co(II) does not restrict cobalamin domain motion	748182	
5.4.3.5	additional information	ornithine 4,5-aminomutase is a 5'-deoxyadenosylcobalamin and pyridoxal 5'-phosphate co-dependent radical enzyme. The conserved residues include S162 and N226, which form hydrogen bonds to the pyridine nitrogen and the phenolic group of pyridoxal 5'-phosphate, respectively. Other residues include Y187 and Y160, which flank the pyridine ring. The former aromatic side chain also forms a hydrogen bond to the pyridoxal 5'-phosphate phosphate, while the latter side chain forms a hydrogen bond to AdoCbl in a modelled closed conformation of the enzyme	747193