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
4.2.1.28 propanediol dehydrataseAdvanced search results
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results (Inhibitors
Inhibitors on EC 4.2.1.28 - propanediol dehydratase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
3-butene-1,2-diol
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holodiol dehydratase undergoes rapid and irreversible inactivation, the inactivation cleaves the Co-C bond of adenosylcobalamin irreversibly forming unidentified radicals and cob(II)alamin that resist oxidation even in the presence of oxygen, inactivation mechanism, overview
3-butyne-1,2-diol
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holodiol dehydratase undergoes rapid and irreversible inactivation, the inactivation cleaves the Co-C bond of adenosylcobalamin irreversibly forming unidentified radicals and cob(II)alamin that resist oxidation even in the presence of oxygen, inactivation mechanism, overview
adenosylcobinamide 3-(2-methylbenzimidazolyl)propyl phosphate
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competitive inhibitor with respect to coenzyme B12. Irreversible cleavage of the coenzyme Co-C bond during the inactivation
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adenosylmethylcobalamin
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catalytic efficiency (turnover number to Km-value) of the holoenzyme with adenosylmethylcobalamin is 0.15% of that for the regular coenzyme adenosylcobalamin, Km: 0.0017 mM
ethylene glycol bis -N,N,N,N-tetraacetic acid
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beta-aminoethyl ether
glycolaldehyde hydrate
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induces the formation of cob(II)alamin and 5'-deoxyadenosine from adenosylcobalamin at the active site of the enzyme, and the resulting complex is inactive
thioglycerol
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holodiol dehydratase undergoes rapid and irreversible inactivation, the inactivation cleaves the Co-C bond of adenosylcobalamin irreversibly forming unidentified radicals and cob(II)alamin that resist oxidation even in the presence of oxygen, inactivation mechanism, overview
2,3-Butanediol
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meso isomer strong inactivator and good substrate, Ki: 0.2 mM, same stereospecificity as in normal catalysis, D- and L-isomers competitive inhibitors, Ki: 0.55 mM and 0.59 mM, respectively
adenosylcobalamin
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with e-propionamide group converted to carboxylic acid, inactivation during catalytic process, analogues inhibit if added prior to coenzyme
adenosylcobalamin
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analogue where e-propionamide group is converted to carboxylic acid inactivates complex, forms hydroxycobalamine derivative, leaves apoenzyme intact, which indicates that inactivation occurs from one of the intermediates of the normal reaction, mechanism of inactivation
adenosylcobalamin
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electron paramagnetic resonance data indicate mechanism based mode of coenzyme analogue inactivation, extinction of radical intermediates
cyanocobalamin
a tightly bound inactive coenzyme analogue lacking the adenine ring in the upper axial ligand, imitates the inactivated cofactor; a tightly bound inactive coenzyme analogue lacking the adenine ring in the upper axial ligand, imitates the inactivated cofactor; a tightly bound inactive coenzyme analogue lacking the adenine ring in the upper axial ligand, imitates the inactivated cofactor
EDTA
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EDTA inhibition of apoenzyme is reversible at least in the initial phase
glycerol
adenosylcobalamin-dependent diol dehydratase undergoes suicide inactivation by glycerol, one of its physiological substrates, resulting in the irreversible cleavage of the coenzyme Co-C bond. The damaged cofactor remains tightly bound to the active site, it is not displaced by intact adenosylcobalamin, resulting in the irreversible inactivation of the enzyme. The DD-reactivating factor reactivates the inactivated holoenzyme in the presence of ATP and Mg2+ by mediating the exchange of the tightly bound damaged cofactor for free intact coenzyme, overview; adenosylcobalamin-dependent diol dehydratase undergoes suicide inactivation by glycerol, one of its physiological substrates, resulting in the irreversible cleavage of the coenzyme Co-C bond. The damaged cofactor remains tightly bound to the active site, it is not displaced by intact adenosylcobalmin, resulting in the irreversible inactivation of the enzyme. The DD-reactivating factor reactivates the inactivated holoenzyme in the presence of ATP and Mg2+ by mediating the exchange of the tightly bound damaged cofactor for free intact coenzyme, overview; adenosylcobalamin-dependent diol dehydratase undergoes suicide inactivation by glycerol, one of its physiological substrates, resulting in the irreversible cleavage of the coenzyme Co-C bond. The damaged cofactor remains tightly bound to the active site, it is not displaced by intact Ado-Cbl, resulting in the irreversible inactivation of the enzyme. The DD-reactivating factor reactivates the inactivated holoenzyme in the presence of ATP and Mg2+ by mediating the exchange of the tightly bound damaged cofactor for free intact coenzyme, overview
glycerol
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suicide inactivation in vitro, reactivation possible in presence of coenzyme, Mg2+, ATP in vivo
glycerol
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stereospecificity: enzyme-R-glycerol complex responsible for product-formation, enzyme-S-glycerol complex responsible for inactivation, several molecules of glycerol per enzyme molecule involved, active-site inhibition, C3-methyl group plays crucial role; suicide inactivation in vitro, reactivation possible in presence of coenzyme, Mg2+, ATP in vivo
glycerol
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stereospecificity: enzyme-R-glycerol complex responsible for product-formation, enzyme-S-glycerol complex responsible for inactivation, several molecules of glycerol per enzyme molecule involved, active-site inhibition, C3-methyl group plays crucial role
glycerol
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reactivation in vivo effected by DdrA, DdrB reactivating factor in the presence of coenzyme, ATP, and Mg2+, reactivation by cobalamin exchange, both genes that produce reactivating factor cloned and expressed in E. coli
glycerol
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suicide inhibitor. The linear increase in beta-hydroxypropionaldehyde formation ceases after 4 min
Propane-1,2-diol
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mechanism-based inactivation obeying first-order reaction kinetics
Propane-1,2-diol
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leads to inactivation of wild-type and mutant enzymes during catalysis, kinetics, overview
additional information
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inactivated holoenzymes undergo reactivation by diol dehydratase-reactivating factor in the presence of ATP, Mg2+ and adenosylcobalamin
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additional information
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no inhibition by 5 mM of 1,10-phenanthroline, 2,2'-dipyridyl, citrate, succinate, tartrate, malate, and salicylate
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additional information
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Asp335 has a strong anticatalytic effect on the OH group migration despite its important role in substrate binding. The synergistic interplay of the O-C bond cleavage by Ca2+ ion and the deprotonation of the spectator OH-group by Glu170 is required to overcome the anticatalytic effect of Asp335
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additional information
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various chemicals and substrate analogues
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