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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.
    View publication on PubMedView publication on EuropePMC

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