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

BRENDA support

Literature summary for 4.3.1.7 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]

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

Organism

Organism UniProt Comment Textmining
Clostridium sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Clostridium sp.

Substrates and Products (Substrate)

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

Subunits

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

Cofactor

Cofactor Comment Organism Structure
adenosylcobalamin dependent on Clostridium sp.