Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Klebsiella oxytoca |
Crystallization (Comment) | Organism |
---|---|
sandwich-drop vapor diffusion method, 4ΒΊC | Klebsiella oxytoca |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Klebsiella oxytoca | - |
- |
- |
Purification (Comment) | Organism |
---|---|
chromatography on DEAE-cellulose | Klebsiella oxytoca |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
propane-1,2-diol = propanal + H2O | binding of the substrate to the active site converts a hexacoordinated complex of K+ into the heptacoordinated one. A relatively large binding energy is released upon coordination of the two hydroxyl groups to K+, displacing a sixth ligand, H2O. Interaction of the coenzyme with the enzyme cleaves its Co-C bond, forming an adenosyl radical and cob(II)alamin. The radical abstracts the pro-S hydrogen of the S-enantiomer forming a substrate-derived radical and 5'-deoxyadenosine. The substrate-radical undergoes the 1,2-shift of the hydroxyl group, forming a product-derived gem-diol radical. The C2 of the product radical, abstracts a hydrogen back from deoxyadenosine with inversion of the configuration of C2, producing a 1,1-gem-diol, which undergoes dehydration, forming propionaldehyde and H2O | Klebsiella oxytoca |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1,2-propanediol | the substrate is located near to K+ rather than to the cobalt atom of cobalamin | Klebsiella oxytoca | propanal | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
coenzyme B12 | adenosylcobalamin. There is a strict specificity of the enzyme for the coenzyme adenosyl group | Klebsiella oxytoca | |
additional information | adeninylpentylcobalamin and cyanocobalamin are inactive as cofactors | Klebsiella oxytoca |