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Literature summary for 4.2.1.28 extracted from

  • Masuda, J.; Shibata, N.; Morimoto, Y.; Toraya, T.; Yasuoka, N.
    How a protein generates a catalytic radical from coenzyme B(12): X-ray structure of a diol-dehydratase-adeninylpentylcobalamin complex (2000), Structure Fold. Des., 8, 775-788.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Klebsiella oxytoca

Crystallization (Commentary)

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

Organism

Organism UniProt Comment Textmining
Klebsiella oxytoca
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Purification (Commentary)

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

Reaction

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 and Products (Substrate)

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
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Cofactor

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