Literature summary for 4.2.1.28 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.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Klebsiella oxytoca

Crystallization (Commentary)

Crystallization (Comment)	Organism
sandwich-drop vapor diffusion method, 4ºC	Klebsiella oxytoca

Organism

Organism	UniProt	Comment	Textmining
Klebsiella oxytoca	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
chromatography on DEAE-cellulose	Klebsiella oxytoca

Reaction

Reaction	Comment	Organism	Reaction ID
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	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1,2-propanediol	(S) and (R) stereoisomers	Klebsiella oxytoca	propanal	-	?

Cofactor

Cofactor	Comment	Organism	Structure
coenzyme B12	adenosylcobalamin	Klebsiella oxytoca

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Release 2023.1 (January 2023)