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Literature summary extracted from

  • Wallis, O.C.; Johnson, A.W.; Lappert, M.F.
    Studies on the subunit structure of the adenosylcobalamin-dependent enzyme ethanolamine ammonia-lyase (1979), FEBS Lett., 97, 196-199.
    View publication on PubMed

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.1.7 36000
-
x * 36000 + x * 51000, the 2 subunits are probably present in equimolar proportions, SDS-PAGE Clostridium sp.
4.3.1.7 51000
-
x * 36000 + x * 51000, the 2 subunits are probably present in equimolar proportions, SDS-PAGE Clostridium sp.

Organism

EC Number Organism UniProt Comment Textmining
4.3.1.7 Clostridium sp.
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.1.7
-
Clostridium sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.1.7 ethanolamine
-
Clostridium sp. acetaldehyde + NH3
-
?

Subunits

EC Number Subunits Comment Organism
4.3.1.7 oligomer x * 36000 + x * 51000, the 2 subunits are probably present in equimolar proportions, SDS-PAGE Clostridium sp.

Cofactor

EC Number Cofactor Comment Organism Structure
4.3.1.7 adenosylcobalamin dependent on Clostridium sp.