Literature summary extracted from
St Maurice, M.; Mera, P.; Park, K.; Brunold, T.C.; Escalante-Semerena, J.C.; Rayment, I.
Structural characterization of a human-type corrinoid adenosyltransferase confirms that coenzyme B12 is synthesized through a four-coordinate intermediate (2008), Biochemistry, 47, 5755-5766.
Application
EC Number |
Application |
Comment |
Organism |
---|
2.5.1.17 |
medicine |
ACA-mediated catalysis provides insights in molecular basis for dysfunction in methylmalonic aciduria |
Limosilactobacillus reuteri |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.5.1.17 |
trimer of three independent five-helix bundles, active sites at the interface between adjacent monomers, no significant structural changes accompany catalysis, precatalytic complex with ATP: cob(II)alamin (PDB: 3CI1, four-coordinate, base-off cob(II)alamin intermediate, enzyme with fully ordered six C-terminal residues and potassium ion in active site), complex with tripolyphosphate: adenosylcobalamin (PDB: 3CI3, partially occupied with five-coordinate adenosylcobalamin), precatalytic complex with ATP: cob(II)inamide (PDB: 3CI4, cob(II)inamide-binding structurally indistinguishable from cob(II)alamin-binding), binding of cobalamin and cobinamide (lacking dimethylbenzimidazole moiety) in identical positions and orientation, space group R3, one molecule in asymmetric unit, unit cell parameters: a: 67.8-68, b: 67.8-68, c: 110.9-111.3, beta: 90°, molecular replacement using PDB: 2NT8 as model; vapour-diffusion with tag-cleaved protein solution (18-22 mg/ml, in presence of hydroxycobalamin and/or adenosylcobalamin or dicyanocobinamide, ATP etc.) and reservoir solution (10-13% (w/v) PEG 8000, pH 6), cubic crystals, crystallisation under anoxic conditions in presence of flavin-dependent reducing system |
Limosilactobacillus reuteri |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
2.5.1.17 |
cobinamide |
substrate inhibition |
Limosilactobacillus reuteri |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.5.1.17 |
Limosilactobacillus reuteri |
- |
- |
- |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
2.5.1.17 |
2 ATP + 2 cob(II)yrinic acid a,c-diamide + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)yrinic acid a,c-diamide + an oxidized flavoprotein |
not yet confimed |
Limosilactobacillus reuteri |
|
Specific Activity [micromol/min/mg]
EC Number |
Specific Activity Minimum [µmol/min/mg] |
Specific Activity Maximum [µmol/min/mg] |
Comment |
Organism |
---|
2.5.1.17 |
0.0005 |
- |
in presence of 1 mM ATP, 20 mM NADH, 2 mM FMN, 0.5 mM hydroxycobalamin and NAD(P)H: flavin oxidoreductase, 1.5 mM MgCl2, 100 mM KCl, pH 6 |
Limosilactobacillus reuteri |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.5.1.17 |
ATP + hydroxycobalamin |
coenzyme B12 synthesis from vitamin B12, dimethylbenzimidazole arm of vitamin B12 plays no role in substrate positioning, corrinoid adenosylation assay: anaerobic, pH 6, 25°C, 1 or 2 mM FMN, 10 or 20 mM NADH, NAD(P)H: flavin oxidoreductase, 2 h incubation for complete reduction of hydroxycobalamin to cob(II)alamin before initiation of adenosyltransfer |
Limosilactobacillus reuteri |
tripolyphosphate + adenosylcobalamin + H2O |
measuring difference in absorbance by adenosylcobalamin at 525 nm |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.5.1.17 |
human-type ATP: cob(I)alamin adenosyltransferase |
- |
Limosilactobacillus reuteri |
2.5.1.17 |
LrPduO |
- |
Limosilactobacillus reuteri |
2.5.1.17 |
PduO-type ACA |
- |
Limosilactobacillus reuteri |
Turnover Number [1/s]
EC Number |
Turnover Number Minimum [1/s] |
Turnover Number Maximum [1/s] |
Substrate |
Comment |
Organism |
Structure |
---|
2.5.1.17 |
additional information |
- |
additional information |
adenosylation of cobalamin and cobinamide (lacking dimethylbenzimidazole moiety) at similar rates |
Limosilactobacillus reuteri |
|