Structural highlights
Function
DDRA_KLEOK Large subunit of the diol dehydratase-reactivating factor (DDR), which reactivates suicidally inhibited adenosylcobalamin-dependent diol dehydratase (DD, pddA, pddB, pddC). DDR acts as a chaperone, reactivating inactivated DD holoenzyme in the presence of ATP, Mg(2+) and free adenosylcobalamin (AdoCbl), by mediating the exchange of the tightly bound damaged cofactor AdoCbl for a free intact one (PubMed:10529189, PubMed:9405397, PubMed:9920879, PubMed:17916188, PubMed:18586770, PubMed:21040475). Reactivation takes place in two steps: ADP-dependent cobalamin release, then ATP-dependent dissociation of the DD apoenzyme-DDR complex. DDR has weak ATPase activity which is required for DD reactivation (PubMed:10529189, PubMed:17916188, PubMed:21040475). This subunit contains the adenosine nucleotide binding site (PubMed:16338403). Activates glycerol-inactivated, O2-inactivated holoenzyme and inactivated enzyme-cyanocobalamin complex (PubMed:9920879). Also reactivates glycerol-inactivated hologlycerol dehydratase, a DD isozyme (PubMed:17916188).[1] [2] [3] [4] [5] [6] [7]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Mori K, Toraya T. Mechanism of reactivation of coenzyme B12-dependent diol dehydratase by a molecular chaperone-like reactivating factor. Biochemistry. 1999 Oct 5;38(40):13170-8. PMID:10529189 doi:10.1021/bi9911738
- ↑ Shibata N, Mori K, Hieda N, Higuchi Y, Yamanishi M, Toraya T. Release of a damaged cofactor from a coenzyme B12-dependent enzyme: X-ray structures of diol dehydratase-reactivating factor. Structure. 2005 Dec;13(12):1745-54. PMID:16338403 doi:10.1016/j.str.2005.08.011
- ↑ Kajiura H, Mori K, Shibata N, Toraya T. Molecular basis for specificities of reactivating factors for adenosylcobalamin-dependent diol and glycerol dehydratases. FEBS J. 2007 Nov;274(21):5556-66. PMID:17916188 doi:10.1111/j.1742-4658.2007.06074.x
- ↑ Toraya T, Tamura N, Watanabe T, Yamanishi M, Hieda N, Mori K. Mechanism-based inactivation of coenzyme B12-dependent diol dehydratase by 3-unsaturated 1,2-diols and thioglycerol. J Biochem. 2008 Oct;144(4):437-46. PMID:18586770 doi:10.1093/jb/mvn086
- ↑ Mori K, Hosokawa Y, Yoshinaga T, Toraya T. Diol dehydratase-reactivating factor is a reactivase--evidence for multiple turnovers and subunit swapping with diol dehydratase. FEBS J. 2010 Dec;277(23):4931-43. PMID:21040475 doi:10.1111/j.1742-4658.2010.07898.x
- ↑ Mori K, Tobimatsu T, Hara T, Toraya T. Characterization, sequencing, and expression of the genes encoding a reactivating factor for glycerol-inactivated adenosylcobalamin-dependent diol dehydratase. J Biol Chem. 1997 Dec 19;272(51):32034-41. PMID:9405397 doi:10.1074/jbc.272.51.32034
- ↑ Toraya T, Mori K. A reactivating factor for coenzyme B12-dependent diol dehydratase. J Biol Chem. 1999 Feb 5;274(6):3372-7. PMID:9920879 doi:10.1074/jbc.274.6.3372