Cobalamin-binding domain superfamily
Short name | Cobalamin-bd_sf |
Overlapping entries |
Description
* Animal and prokaryotic methionine synthase (
* Animal and prokaryotic methylmalonyl-CoA mutase (
* Prokaryotic lysine 5,6-aminomutase (
* Prokaryotic glutamate mutase (
* Prokaryotic methyleneglutarate mutase (
* Prokaryotic isobutyryl-CoA mutase (
References
1.Domain alternation switches B(12)-dependent methionine synthase to the activation conformation. Bandarian V, Pattridge KA, Lennon BW, Huddler DP, Matthews RG, Ludwig ML. Nat. Struct. Biol. 9, 53-6, (2002). View articlePMID: 11731805
2.How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 A resolution. Mancia F, Keep NH, Nakagawa A, Leadlay PF, McSweeney S, Rasmussen B, Bosecke P, Diat O, Evans PR. Structure 4, 339-50, (1996). View articlePMID: 8805541
3.Structure-based perspectives on B12-dependent enzymes. Ludwig ML, Matthews RG. Annu. Rev. Biochem. 66, 269-313, (1997). View articlePMID: 9242908
4.The many faces of vitamin B12: catalysis by cobalamin-dependent enzymes. Banerjee R, Ragsdale SW. Annu. Rev. Biochem. 72, 209-47, (2003). View articlePMID: 14527323
5.Vitamin B12: chemistry and biochemistry. Krautler B. Biochem. Soc. Trans. 33, 806-10, (2005). View articlePMID: 16042603
6.How a protein binds B12: A 3.0 A X-ray structure of B12-binding domains of methionine synthase. Drennan CL, Huang S, Drummond JT, Matthews RG, Lidwig ML. Science 266, 1669-74, (1994). View articlePMID: 7992050
7.Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights. Reitzer R, Gruber K, Jogl G, Wagner UG, Bothe H, Buckel W, Kratky C. Structure 7, 891-902, (1999). View articlePMID: 10467146
GO terms
biological process
- None
molecular function
cellular component
- None
Cross References
Contributing Member Database Entry
- SUPERFAMILY:SSF52242