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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
15
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pubmed:dateCreated |
1983-9-9
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pubmed:abstractText |
The inactive complex of diol dehydrase with hydroxocobalamin was resolved by treatment with SO2-3, followed by dialysis to remove SO2-3, giving the apoenzyme which was reconstitutable into catalytically active holoenzyme upon addition of adenosylcobalamin ("re-activation"). Spectral evidence showed that the enzyme-bound hydroxocobalamin undergoes a Co beta-ligand exchange reaction forming sulfitocobalamin. Sulfitocobalamin was bound to diol dehydrase only loosely, and therefore dissociated from the enzyme. In contrast, neither the enzyme-hydroxocobalamin-5'-deoxyadenosine nor the enzyme-hydroxocobalamin-adenosine complex was resolved and thus re-activated by this procedure. It was shown spectroscopically that the hydroxocobalamin in these complexes does not react with SO2-3, or even with CN-, indicating that the OH group in the Co beta-position was blocked spatially by these enzyme-bound nucleosides. Neither O2-inactivated holoenzyme nor the holoenzyme inactivated suicidally by glycerol or 1,2-ethanediol during dehydration reaction was also re-activated by the same procedure. The complex of the enzyme with cyanocobalamin or methylcobalamin was not resolvable by the SO2-3 treatment. This was because these cobalamins bound to the enzyme were not subject to a ligand exchange reaction with SO2-3.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cobamides,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyadenosines,
http://linkedlifedata.com/resource/pubmed/chemical/Hydro-Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxocobalamin,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleosides,
http://linkedlifedata.com/resource/pubmed/chemical/Propanediol Dehydratase,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfoxides,
http://linkedlifedata.com/resource/pubmed/chemical/Vitamin B 12,
http://linkedlifedata.com/resource/pubmed/chemical/cobamamide,
http://linkedlifedata.com/resource/pubmed/chemical/mecobalamin
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
258
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
9296-301
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:6603460-Cobamides,
pubmed-meshheading:6603460-Deoxyadenosines,
pubmed-meshheading:6603460-Hydro-Lyases,
pubmed-meshheading:6603460-Hydroxocobalamin,
pubmed-meshheading:6603460-Magnesium,
pubmed-meshheading:6603460-Nucleosides,
pubmed-meshheading:6603460-Propanediol Dehydratase,
pubmed-meshheading:6603460-Spectrophotometry,
pubmed-meshheading:6603460-Sulfoxides,
pubmed-meshheading:6603460-Vitamin B 12
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pubmed:year |
1983
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pubmed:articleTitle |
Ligand exchange reactions of diol dehydrase-bound cobalamins and the effect of the nucleoside binding.
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pubmed:publicationType |
Journal Article
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