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
-
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
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General Information
General Information on EC 4.2.1.30 - glycerol dehydratase
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evolution
malfunction
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GDH loses most of its beta-subunit after purification by either ion exchange chromatography or using a nickel chelate column
metabolism
physiological function
glycerol dehydratase is functionally characterised to two main groups, one is the vitamin B12-dependent and the other the B12-independent. Glycerol dehydratase evolutionary history and analysis of the functional residues responsible for type I divergence, enzyme phylogenetic tree topology with two clades, one for vitamin B12-dependent and the other for B12-independent class, overview
evolution
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glycerol dehydratase is functionally characterised to two main groups, one is the vitamin B12-dependent and the other the B12-independent. Glycerol dehydratase evolutionary history and analysis of the functional residues responsible for type I divergence, enzyme phylogenetic tree topology with two clades, one for vitamin B12-dependent and the other for B12-independent class, overview
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GDHt is the key enzyme and catalyzes the rate limiting step for biotransformation from glycerol to 1,3-propanediol
metabolism
glycerol dehydratase catalyses glycerol reductive conversion to 3-hydroxypropanaldehyde, the first step required for the microbial conversion of glycerol to 1,3-propanodiol
metabolism
3-hydroxypropionic acid production pathway from glycerol
metabolism
the enzyme is involved in the 3-hydroxypropionic acid biosynthetic pathway
metabolism
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GDHt is the key enzyme and catalyzes the rate limiting step for biotransformation from glycerol to 1,3-propanediol
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metabolism
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glycerol dehydratase catalyses glycerol reductive conversion to 3-hydroxypropanaldehyde, the first step required for the microbial conversion of glycerol to 1,3-propanodiol
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overexpressed glycerol dehydratase shows higher enzyme activity than that of wild-strain
physiological function
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recombinant Escherichia coli strain HMS174(DE3)/pCOLADuet-1::dhaB1B2::pduP::phaC1 can accumulate poly(3-hydroxypropionate) at up to 11.98% of the cell dry weight
physiological function
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radical S-adenosyl-L-methionine activation of the B12-independent glycerol dehydratase results in formation of 5-deoxy-5-(methylthio)adenosine and not 5-deoxyadenosine
physiological function
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overexpressed glycerol dehydratase shows higher enzyme activity than that of wild-strain
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