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
-
spectator
-
base-on
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carbon-cobalt
-
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
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General Information on EC 4.2.1.28 - propanediol dehydratase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
physiological function
additional information
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Salmonella enterica produces a proteinaceous microcompartment for B12-dependent 1,2-propanediol utilization, Pdu MCP. The Pdu MCP consists of catabolic enzymes encased within a protein shell and its function is to sequester propionaldehyde, a toxic intermediate of 1,2-propanediol degradation, overview. A short N-terminal region of the medium subunit, PduD, is required for packaging the coenzyme B12-dependent diol dehydratase, PduCDE, into the lumen of the Pdu MCP. PduD subunit also mediates packaging of itself and other subunits of diol dehydratase, PduC and PduE, into the Pdu MCP
physiological function
enzyme undergoes mechanism-based inactivation by glycerol and O2 inactivation in the absence of substrate, which accompanies irreversible cleavage of the coenzyme Co-C bond. Diol dehydratase activity is maintained through coenzyme recycling by a reactivating system for diol dehydratase composed of diol dehydratase-reactivase, PduO adenosyltransferase, and a reducing system. The releasing factor diol dehydratase-reactivase is essential for the recycling of adenosycobalamin, and PduO is a specific adenosylating enzyme for the diol dehydratase reactivation, whereas CobA and EutT exert their effects through free synthesized coenzyme
physiological function
mechanistic comparison between glycyl radical-dependent enzyme from Roseburia inulinivorans and vitamin B12-dependent enzyme from Klebsiella oxytoca. Unlike B12-dependent propanediol dehydratase, the glycyl radical-dependent enzyme appears to catalyze the direct elimination of a hydroxyl group from an initially formed substrate-based radical, avoiding the generation of a 1,1-gem diol intermediate
physiological function
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mechanistic comparison between glycyl radical-dependent enzyme from Roseburia inulinivorans and vitamin B12-dependent enzyme from Klebsiella oxytoca. Unlike B12-dependent propanediol dehydratase, the glycyl radical-dependent enzyme appears to catalyze the direct elimination of a hydroxyl group from an initially formed substrate-based radical, avoiding the generation of a 1,1-gem diol intermediate
physiological function
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mechanistic comparison between glycyl radical-dependent enzyme from Roseburia inulinivorans and vitamin B12-dependent enzyme from Klebsiella oxytoca. Unlike B12-dependent propanediol dehydratase, the glycyl radical-dependent enzyme appears to catalyze the direct elimination of a hydroxyl group from an initially formed substrate-based radical, avoiding the generation of a 1,1-gem diol intermediate
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physiological function
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enzyme undergoes mechanism-based inactivation by glycerol and O2 inactivation in the absence of substrate, which accompanies irreversible cleavage of the coenzyme Co-C bond. Diol dehydratase activity is maintained through coenzyme recycling by a reactivating system for diol dehydratase composed of diol dehydratase-reactivase, PduO adenosyltransferase, and a reducing system. The releasing factor diol dehydratase-reactivase is essential for the recycling of adenosycobalamin, and PduO is a specific adenosylating enzyme for the diol dehydratase reactivation, whereas CobA and EutT exert their effects through free synthesized coenzyme
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physiological function
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mechanistic comparison between glycyl radical-dependent enzyme from Roseburia inulinivorans and vitamin B12-dependent enzyme from Klebsiella oxytoca. Unlike B12-dependent propanediol dehydratase, the glycyl radical-dependent enzyme appears to catalyze the direct elimination of a hydroxyl group from an initially formed substrate-based radical, avoiding the generation of a 1,1-gem diol intermediate
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