Literature summary extracted from
Shibata, N.; Nakanishi, Y.; Fukuoka, M.; Yamanishi, M.; Yasuoka, N.; Toraya, T.
Structural rationalization for the lack of stereospecificity in coenzyme B12-dependent diol dehydratase (2003), J. Biol. Chem., 278, 22717-22725.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
4.2.1.28 |
expression in Escherichia coli |
Klebsiella oxytoca |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
4.2.1.28 |
sandwich-drop vapor diffusion method, 4ΒΊC |
Klebsiella oxytoca |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.2.1.28 |
Klebsiella oxytoca |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
4.2.1.28 |
chromatography on DEAE-cellulose |
Klebsiella oxytoca |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
4.2.1.28 |
propane-1,2-diol = propanal + H2O |
the enzyme-bound adenosylcobalamin serves as an intermediate hydrogen carrier, accepting a hydrogen atom from C1 of the substrate to C5' of the coenzyme and giving a hydrogen back to C2 of the product. R and S enantiomers are bound to the active site of the enzyme in a symmetrical mode with respect to the plane |
Klebsiella oxytoca |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
4.2.1.28 |
1,2-propanediol |
(S) and (R) stereoisomers |
Klebsiella oxytoca |
propanal |
- |
? |
|
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
4.2.1.28 |
coenzyme B12 |
adenosylcobalamin |
Klebsiella oxytoca |
|