4.2.1.28: propanediol dehydratase
This is an abbreviated version!
For detailed information about propanediol dehydratase, go to the full flat file.
Word Map on EC 4.2.1.28
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4.2.1.28
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cobiialamin
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oxytoca
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cyanocobalamin
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5'-deoxyadenosine
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homolysis
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propionaldehyde
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1,2-ethanediol
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hydroxocobalamine
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cobamide
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5,6-dimethylbenzimidazole
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cobalt-carbon
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microcompartment
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spectator
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base-on
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carbon-cobalt
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corrins
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5\'-deoxyadenosyl
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acetobacterium
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synthesis
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degradation
- 4.2.1.28
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cobiialamin
- oxytoca
- cyanocobalamin
- 5'-deoxyadenosine
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homolysis
- propionaldehyde
- 1,2-ethanediol
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hydroxocobalamine
- cobamide
- 5,6-dimethylbenzimidazole
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cobalt-carbon
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microcompartment
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spectator
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base-on
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carbon-cobalt
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corrins
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5\'-deoxyadenosyl
- acetobacterium
- synthesis
- degradation
Reaction
Synonyms
1,2-propanediol dehydratase, 1,2-propanediol hydro-lyase, adenosylcobalamin-dependent diol dehydratase, AdoCbl-dependent diol dehydratase, cobalamin-dependent diol dehydratase, coenzyme B12-dependent diol dehydrase, coenzyme B12-dependent diol dehydratase, coenzyme-B12-dependent diol dehydratase, DDH, dehydratase, diol, dehydratase, propanediol, diol dehydrase, diol dehydratase, diol dehydratase alpha subunit, dioldehydrase, dioldehydratase, DL-1,2-propanediol hydro-lyase, DL-1,2-propanediol hydrolyase, GldCDE, meso-2,3-butanediol dehydrase, PduCDE, PduCDEGH, Propanediol dehydrase
ECTree
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Cofactor
Cofactor on EC 4.2.1.28 - propanediol dehydratase
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Cobalamin
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roles of adenine anchoring and ion pairing at the coenzyme B12-binding site, overview. Presence of a positive charge at the beta135 residue increases the affinity for cobalamins but is not essential for catalysis, and the introduction of a negative charge there prevents the enzyme-cobalamin interaction
cobamide
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role during catalysis: dissociation of C-Co bond of the coenzyme and Co-binding to substrate, effect of analogues, one binding site per enzyme molecule
cobamide
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Km of cytoplasmic enzyme: 0.0008 mM, Km of membrane-bound enzyme: 0.002 mM
cobamide
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analogue studies show that phosphodiester moiety of nucleotide loop is crucial for apoenzyme binding
cobamide
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importance of apoenzyme tertiary structure for coenzyme-substrate interaction
cobamide
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kinetic investigations with inhibitors that mimic posthomolysis intermediate of reaction, inhibitors act as competitive inhibitors with respect to coenzyme B12
coenzyme B12
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adenosylcobalamin. Glycerol-inactivated and oxygen inactivated enzyme undergoes rapid reactivation in the presence of the cofactor, ATP and Mg2+
coenzyme B12
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adenosylcobalamin. Glycerol-inactivated and oxygen inactivated enzyme undergoes rapid reactivation in the presence of the cofactor, ATP and Mg2+
coenzyme B12
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adenosylcobalamin. Glycerol-inactivated and oxygen inactivated enzyme undergoes rapid reactivation in the presence of the reactivating factor, the cofactor, ATP and Mg2+
coenzyme B12
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adenosylcobalamin. Glycerol-inactivated enzyme undergoes reactivation in the presence of the reactivating factor, the cofactor, ATP and Mg2+
coenzyme B12
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adenosylcobalamin. Glycerol-inactivated enzyme undergoes reactivation in the presence of the reactivating factor, the cofactor, ATP and Mg2+
coenzyme B12
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adenosylcobalamin. Radical initiator
coenzyme B12
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adenosylcobalamin. There is a strict specificity of the enzyme for the coenzyme adenosyl group
coenzyme B12
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adenosylcobalamin, dependent on, two mol of 5'-deoxyadenosine per mol of enzyme are formed as an inactivation product from the coenzyme adenosyl group in presence of inhibitors, overview
presence of 2.80 equivalents of iron and 2.71 ± 0.02 equivalents of sulfur per monomer
[4Fe-4S]-center
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presence of 2.80 equivalents of iron and 2.71 ± 0.02 equivalents of sulfur per monomer
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adeninylpentylcobalamin and cyanocobalamin are inactive as cofactors
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additional information
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adenosylcobinamide 3-benzimidazolylpropyl phosphate, beta-adenosyl-alpha-benzimidazolylcobamide and beta-adenosyl-alpha-imidazolylcobamide are active coenzymes. No coenzyme activity: adenosylcobinamide 3-(2-methylbenzimidazolyl)propyl phosphate
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