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
ECTree
4.2.1.30 glycerol dehydrataseAdvanced search results
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results (Inhibitors
Inhibitors on EC 4.2.1.30 - glycerol dehydratase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(S)-but-3-ene-1,2-diol
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irreversibly inactivates. Time-dependent inhibition of GDH to yield a complex that is spectroscopically (EPR) active. Presence of the 1,2-dihydroxybut-3-en-1-yl radical in the reaction, which has relatively high energy
Ag+
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0.1 mM AgNO3, apoenzyme: 97% loss of activity, inactive enzyme complex with hydroxocobalamin: 19% loss of activity
Cobeta-2,3-dihydroxypropyl-[1'-O-(4-tolyl)cobamide]
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moderate inhibitor
cyanocobalamin
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quite inhibitory to enzyme activity if it is added to the apoenzyme before the 5,6-dimethylbenzimidazolylcobamide
hexadecyltrimethylammonium bromide
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0.14%, complete irreversible inactivation of the apoenzyme
Hg2+
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0.1 mM HgCl2, apoenzyme: complete loss of activity, inactive enzyme complex with hydroxocobalamin: 70% loss of activity
HO-(CH2)n-cobalamin
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chain lengths of n=2-5, short chains are more effective
salicylic acid
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causes inactivation by dissociation of the apoenzyme into its subunits
vitamin B12
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inactivated in vitro by all forms of vitamin B12 stoichiometrically
EDTA
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inhibition of the apoenzyme can be completely reversed by Mg2+ in adequate concentrations. Ca2+, Mn2+, Zn2+ and Co2+ also reverse the EDTA inhibitory effect. Glycerol partially reverses the inhibition. Complete inhibition of the enzyme complex with hydroxocobalamin is reversible with an excess of Mg2+
EDTA
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causes inactivation by dissociation of the apoenzyme into its subunits. Inhibition is reversed by dialysis, Mg2+, glycerol or by addition of excess of either subunit
glycerol
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suicide inactivation, 65% activity after 3 min, 3% activity after 30 min
glycerol
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irreversible cleavage of the Co-C bond, forming 5'-deoxyadenosine and an unknown cobalamin species. The unknown cobalamin species is converted very slowly to OH-cobalamin. The cobalamin species that is formed remains tightly bound to the enzyme, inactivating the enzyme irreversibly
glycerol
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inactivation of the enzyme in situ and in vitro during catalysis, glycerol inactivated enzyme in situ is reactivated by ATP and Mn2+ in the presence of free adenosylcobalamin. CTP and GTP are able to replace ATP partially. Mn2+ can be fully replaced by Mg2+
glycerol
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irreversible cleavage of the Co-C bond, forming 5'-deoxyadenosine and an unknown cobalamin species. The unknown cobalamin species is converted very slowly to OH-cobalamin. The cobalamin species that is formed remains tightly bound to the enzyme, inactivating the enzyme irreversibly
glycerol
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similar to the wild-type enzyme, GDHAB/C and GDHALB/C undergo mechanism-based inactivation by glycerol during catalysis and can be reactivated by glycerol dehydratase reactivase (GDHR), adenosylcobalamin, ATP, and MgCl2
glycerol
can inactive the glycerol dehydratase expressed in Escherichia coli quickly in 10 min. Can be effectively reactivated to 98.9% by 50 mM ATP, 10 mM Mg2+ and 0.003 mM coenzyme B12, respectively, when the ratio (w/w) of glycerol dehydratase to reactivation factor is 4:1. Activity of glycerol inactivated GDHt is easier to be recovered than that of O2-inactivated GDHt
glycerol
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GDHt can be quickly reactivated by glycerol dehydratase reactivation factor to 98% in the presence of ATP, Mg2+ and coenzyme B12. In the first 10 min of the reactivation reaction, the average reactivation rate is 0.18 micromol/min for glycerol-inactivated GDHt
O2
can inactive the glycerol dehydratase expressed in Escherichia coli quickly in 10 min. Can be effectively reactivated to 97.3% by 50 mM ATP, 10 mM Mg2+ and 0.003 mM coenzyme B12, respectively, when the ratio (w/w) of glycerol dehydratase to reactivation factor is 4:1. Activity of glycerol inactivated GDHt is easier to be recovered than that of O2-inactivated GDHt
O2
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GDHt can be quickly reactivated by glycerol dehydratase reactivation factor in the presence of ATP, Mg2+ and coenzyme B12. In the first 10 min of the reactivation reaction, the average reactivation rate is 0.12 micromol/min for O2-inactivated GDHt
p-chloromercuribenzoate
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0.1 mM, apoenzyme: complete loss of activity, inactive enzyme complex with hydroxocobalamin: 70% loss of activity
p-chloromercuribenzoate
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2,3-dimercaptopropanol, glutathione and cysteine protect
