EC Number   |
Inhibitors |
Structure |
|---|
   4.2.1.30 | (2,3-dihydroxypropyl)cobalamin |
competes with coenzyme B12 |
   |
| 4.2.1.30 | (S)-but-3-ene-1,2-diol |
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 |
|
| 4.2.1.30 | Ag+ |
0.1 mM AgNO3, apoenzyme: 97% loss of activity, inactive enzyme complex with hydroxocobalamin: 19% loss of activity |
|
| 4.2.1.30 | CN- |
KCN, pH 6.0, slowly inactivates |
|
| 4.2.1.30 | Cobeta-2,3-dihydroxypropyl-[1'-O-(4-tolyl)cobamide] |
moderate inhibitor |
|
| 4.2.1.30 | cyanocobalamin |
quite inhibitory to enzyme activity if it is added to the apoenzyme before the 5,6-dimethylbenzimidazolylcobamide |
|
| 4.2.1.30 | EDTA |
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+ |
|
| 4.2.1.30 | EDTA |
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 |
|
| 4.2.1.30 | glycerol |
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+ |
|
| 4.2.1.30 | glycerol |
- |
|
