Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Gaudemer, A.; Zylber, J.; Zylber, N.; Baran-Marszac, M.; Hull, W.E.; Fountoulakis, M.; König, A.; Wölfle, K.; Retey, J.
    Reversible cleavage of the cobalt-carbon bond of coenzyme B12 catalyzed by methylmalonyl-CoA mutase from Propionibacterium shermanii. The use of coenzyme B12 stereospecifically deuterated in position 5' (1981), Eur. J. Biochem., 119, 279-285.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
5.4.99.2 Propionibacterium freudenreichii subsp. shermanii
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.99.2 (R)-2-methylmalonyl-CoA
-
 Propionibacterium freudenreichii subsp. shermanii succinyl-CoA
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
5.4.99.2 cobamide enzyme-bound and free 5'-deoxyadenonosylcobalamin molecules are frequently exchanged during incubation, deuterium is transferred from the 5' position of 5'-deoxyadenonosylcobalamin to the solvent, deuterium scrambling between the two diastereotopic 5'-positions occurrs Propionibacterium freudenreichii subsp. shermanii