1 Parent Features
| DB identifier | Type | Name |
|---|---|---|
| IPR003208 | Family | Diol/glycerol dehydratase/dehydratase reactivating factor |
| Type: | Family | Name: | Diol/glycerol dehydratase reactivating factor, small subunit |
| Description: | Diol dehydratase (propanediol dehydratase) and glycerol dehydratase undergo concomitant, irreversible inactivation by glycerol during catalysis [, ]. This inactivation is mechanism-based and involves cleavage of the Co-C bond of the cobalamin cofactor, coenzyme B12 (AdoCbl), forming 5 -deoxyadenosine and a modified coenzyme []. Irreversible inactivation of the enzyme results from tight binding to the modified, inactive cobalamin [, ].The glycerol-inactivated enzyme undergoes rapid reactivation in the presence of free AdoCbl, ATP, and Mg2+(or Mn2+) []. Reactivation is mediated by a complex of two proteins: a large subunit (DdrA/PduG, ) and a small subunit (DdrB/PduH) [, ].The two subunits of the reactivating factor for glycerol dehydratase have been shown to form a tight complex that serves to reactivate the glycerol-inactivated holoenzyme, as well as O2-inactivated holoenzyme in vitro []. It is believed that this reactivating factor replaces an enzyme-bound, adenine-lacking inactive cobalamin with a free, adenine-containing active cobalamin [].PduG and PduH, part of the propanediol utilization pduoperon, are believed to have a similar function in the reactivation of propanediol dehydratase. PduG was also proposed, on the basis of genetic tests, to be a cobalamin adenosyltransferase involved in the conversion of inactive cobalamin (B12) to AdoCbl []. However, this function has since been shown to belong to another protein, PduO []. | Short Name: | Diol/glycerol_deHydtase_re_ssu |
| DB identifier | Type | Name |
|---|---|---|
| IPR003208 | Family | Diol/glycerol dehydratase/dehydratase reactivating factor |
