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Literature summary for 4.2.1.28 extracted from

  • Schwartz, P.A.; Frey, P.A.
    Dioldehydrase: an essential role for potassium ion in the homolytic cleavage of the cobalt-carbon bond in adenosylcobalamin (2007), Biochemistry, 46, 7293-7301.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
oxygen anaerobically no activity Salmonella enterica subsp. enterica serovar Typhimurium

Cloned(Commentary)

Cloned (Comment) Organism
expression vector pT7.7 Salmonella enterica subsp. enterica serovar Typhimurium

Metals/Ions

Metals/Ions Comment Organism Structure
K+
-
Salmonella enterica subsp. enterica serovar Typhimurium

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
207000
-
molecular weight of hexamer Salmonella enterica subsp. enterica serovar Typhimurium

Organism

Organism UniProt Comment Textmining
Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,2-propanediol
-
Salmonella enterica subsp. enterica serovar Typhimurium propionaldehyde + H2O
-
?

Subunits

Subunits Comment Organism
hexamer dimer of heterotrimers, contained within the R-subunit is an (a/b) beta-barrel that houses the active site Salmonella enterica subsp. enterica serovar Typhimurium

Synonyms

Synonyms Comment Organism
dioldehydrase
-
Salmonella enterica subsp. enterica serovar Typhimurium
DL-1,2-propanediol hydro-lyase
-
Salmonella enterica subsp. enterica serovar Typhimurium

Cofactor

Cofactor Comment Organism Structure
adenosylcobalamin
-
Salmonella enterica subsp. enterica serovar Typhimurium