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Results 1 - 10 of 22 > >>
EC Number Cofactor Commentary Reference
Show all pathways known for 5.4.3.5Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.55'-deoxyadenosylcobalamin - 747193, 747565, 748182
Show all pathways known for 5.4.3.5Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.55'-deoxyadenosylcobalamin Km value 0.00043 652199
Show all pathways known for 5.4.3.5Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.55'-deoxyadenosylcobalamin shows ability to produce highly reactive 5'-deoxyadenosyl radical in enzymatic environments 727644
Show all pathways known for 5.4.3.5Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.5adenosylcobalamin - 704658
Show all pathways known for 5.4.3.5Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.5adenosylcobalamin binding analysis with recombinant wild-type and mutant enzymes, overview 727036
Show all pathways known for 5.4.3.5Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.5adenosylcobalamin dependent on 693191, 727677, 747073
Show all pathways known for 5.4.3.5Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.5adenosylcobalamin paramagnetic Co2+ metal center of the cob(II)alamin cofactor 727131
Show all pathways known for 5.4.3.5Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.5more 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
Show all pathways known for 5.4.3.5Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.5more 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
Show all pathways known for 5.4.3.5Display the word mapDisplay the reaction diagram Show all sequences 5.4.3.5more 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
Results 1 - 10 of 22 > >>