4.2.1.30: glycerol dehydratase
This is an abbreviated version!
For detailed information about glycerol dehydratase, go to the full flat file.
Word Map on EC 4.2.1.30
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4.2.1.30
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pneumoniae
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klebsiella
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1,3-propanediol
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diol
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3-hydroxypropionaldehyde
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3-hydroxypropionic
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butyricum
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adenosylcobalamin-dependent
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adenosylcobalamin
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aerobacter
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synthesis
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freundii
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reactivase
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pdors
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2,3-butanediol
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pasteurianum
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1,2-ethanediol
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poly3-hydroxypropionate
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reuterin
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adocbl
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coenzyme-b12-dependent
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analysis
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biotechnology
- 4.2.1.30
- pneumoniae
- klebsiella
- 1,3-propanediol
- diol
- 3-hydroxypropionaldehyde
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3-hydroxypropionic
- butyricum
-
adenosylcobalamin-dependent
- adenosylcobalamin
-
aerobacter
- synthesis
- freundii
-
reactivase
-
pdors
- 2,3-butanediol
- pasteurianum
- 1,2-ethanediol
-
poly3-hydroxypropionate
-
reuterin
-
adocbl
-
coenzyme-b12-dependent
- analysis
- biotechnology
Reaction
Synonyms
B12-dependent enzyme glycerol dehydratase, B12-dependent glycerol dehydratase, B12-independent GDH, B12-independent glycerol dehydratase, dehydratase, glycerol, DhaB, DhaB1, DhaBCE, DhaC, DhaE, GDH, GDHt, glycerol dehdydrogenase, glycerol dehydrase, glycerol dehydratase, glycerol hydro-lyase, glycerol hydrolyase, KpG, KpGDHt, vitamin B12-independent glycerol dehydratase
ECTree
4.2.1.30 glycerol dehydrataseAdvanced search results
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results (Activating Compound
Activating Compound on EC 4.2.1.30 - glycerol dehydratase
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
GdrA protein
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recombinant GdrA and GdrB proteins form a tight complex of (GdrA)2(GdrB)2, which reactivates the glycerol- or O2-inactivated enzyme as well as the as the enzyme-cyanocobalamin complex in the presence of ATP, Mg2+ and adenosylcobalamin
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GdrB protein
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recombinant GdrA and GdrB proteins form a tight complex of (GdrA)2(GdrB)2, which reactivates the glycerol- or O2-inactivated enzyme as well as the as the enzyme-cyanocobalamin complex in the presence of ATP, Mg2+ and adenosylcobalamin
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glycerol dehydratase activating enzyme
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glycerol dehydratase is activated by another enzyme termed the glycerol dehydratase activating enzyme, GD-AE, leading to formation of a glycyl radical. Formation of the glycyl radical requires a reduced iron-sulfur cluster, contained by GD-AE, and S-adenosyl-L-methionine. The GD-AE harbors adenosine and catalytic cluster (CX3CX2C) binding motifs, an additional [4Fe-4S] cluster binding motifs in the primary structure of the GD-AE and multiple Fe-S clusters that may or may not be spin-coupled
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S-adenosyl-L-methionine
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glycerol dehydratase requires S-adenosyl-L-methionine and strictly anoxic conditions
adenosylcobalamin
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bound at the interface between the alpha and beta subunits
ATP
is critical to the reactivation of glycerol dehydratase
coenzyme B12
is critical to the reactivation of glycerol dehydratase
coenzyme B12
GDHt utilizes adenosylcobalamin, i.e. AdoCbl or CoB12, as a cofactor, Km is 10.03 nM
DhaF
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formerly OrfZ, DhaF-DhaG alpha2beta2 complex rapidly reactivates glycerol-or O2-inactivated hologlycerol dehydratase and activates the enzyme cyanocobalamin complex in the presence of coenzyme B12, ATP and Mg2+
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DhaG
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formerly OrfX, DhaF-DhaG alpha2beta2 complex rapidly reactivates glycerol-or O2-inactivated hologlycerol dehydratase and activates the enzyme cyanocobalamin complex in the presence of coenzyme B12, ATP and Mg2+
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GdrA
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GdrA-GdrB complex reactivates the enzyme in the presence of ATP, Mg2+ and adenosylcobalamin, the reactivating factor mediates ATP-dependent exchange of the enzyme-bound, adenine-lacking cobalamin, for free adenosylcobalamin, an adenine-containing cobalamin, through intermediary formation of apoenzyme in the presence of ATP and Mg2+
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GdrA
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GdrA-GdrB complex reactivates the enzyme in the presence of ATP, Mg2+ and adenosylcobalamin
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GdrA
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GdrA-GdrB complex reactivates the enzyme in the presence of ATP, Mg2+ and adenosylcobalamin, the reactivating factor mediates ATP-dependent exchange of the enzyme-bound, adenine-lacking cobalamin, for free adenosylcobalamin, an adenine-containing cobalamin, through intermediary formation of apoenzyme in the presence of ATP and Mg2+
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GdrB
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GdrA-GdrB complex reactivates the enzyme in the presence of ATP, Mg2+ and adenosylcobalamin, the reactivating factor mediates ATP-dependent exchange of the enzyme-bound, adenine-lacking cobalamin, for free adenosylcobalamin, an adenine-containing cobalamin, through intermediary formation of apoenzyme in the presence of ATP and Mg2+
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GdrB
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GdrA-GdrB complex reactivates the enzyme in the presence of ATP, Mg2+ and adenosylcobalamin
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GdrB
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GdrA-GdrB complex reactivates the enzyme in the presence of ATP, Mg2+ and adenosylcobalamin, the reactivating factor mediates ATP-dependent exchange of the enzyme-bound, adenine-lacking cobalamin, for free adenosylcobalamin, an adenine-containing cobalamin, through intermediary formation of apoenzyme in the presence of ATP and Mg2+
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reactivating factor for diol dehydratase
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efficiently reactivates the glycerol-inactivated glycerol dehydratase in the presence of ATP, Mg2+ and adenosylcobalamin
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reactivating factor for diol dehydratase
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reactivates the glycerol-inactivated glycerol dehydratase in the presence of ATP, Mg2+ and adenosylcobalamin with only little efficiency
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additional information
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glycerol dehydratase requires strictly anoxic conditions
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additional information
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highly specific antagonistic effect of sodium versus potassium
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