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Literature summary extracted from

  • Park, K.; Mera, P.; Escalante-Semerena, J.; Brunold, T.
    Kinetic and spectroscopic studies of the ATP:corrinoid adenosyltransferase PduO from Lactobacillus reuteri: Substrate specificity and insights into the mechanism of Co(II)corrinoid reduction (2008), Biochemistry, 47, 9007-9015.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.17 expressed in Escherichia coli as an N-terminal His-tagged fusion protein Limosilactobacillus reuteri

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.17 0.000096
-
 cob(I)inamide
-
 Limosilactobacillus reuteri
2.5.1.17 0.00013
-
 cob(I)alamin
-
 Limosilactobacillus reuteri

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.17 Limosilactobacillus reuteri
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.17 using Ni-NTA chromatography Limosilactobacillus reuteri

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.17 cob(I)alamin + ATP upon binding to LrPduO that is preincubated with ATP, both Co2+corrinoids undergo a partial (40-50%) conversion to distinct paramagnetic Co2+ species. The spectroscopic signatures of these species are consistent with essentially four-coordinate, square-planar Co2+ complexes. For effecting Co2+ to Co1+ reduction the formation of an activated Co2+ corrinoid intermediate that lacks any significant axial bonding interactions is involved to stabilize the redoxactive, Co 3dz2-based molecular orbital Limosilactobacillus reuteri adenosylcobalamin + triphosphate
-
 ?
2.5.1.17 cob(I)inamide + ATP upon binding to LrPduO that is preincubated with ATP, both Co2+corrinoids undergo a partial (40-50%) conversion to distinct paramagnetic Co2+ species. The spectroscopic signatures of these species are consistent with essentially four-coordinate, square-planar Co2+ complexes. For effecting Co2+ to Co1+ reduction the formation of an activated Co2+ corrinoid intermediate that lacks any significant axial bonding interactions is involved to stabilize the redoxactive, Co 3dz2-based molecular orbital Limosilactobacillus reuteri adenosylcobinamide + triphosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.17 LrPduO
-
 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 0.02
-
 cob(I)inamide
-
 Limosilactobacillus reuteri
2.5.1.17 0.024
-
 cob(I)alamin
-
 Limosilactobacillus reuteri

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.5.1.17 180
-
 cob(I)alamin
-
 Limosilactobacillus reuteri
2.5.1.17 210
-
 cob(I)inamide
-
 Limosilactobacillus reuteri