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Literature summary for 2.5.1.17 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
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Cloned(Commentary)

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Limosilactobacillus reuteri
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
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

Synonyms Comment Organism
LrPduO
-
 Limosilactobacillus reuteri

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.02
-
 cob(I)inamide
-
 Limosilactobacillus reuteri
0.024
-
 cob(I)alamin
-
 Limosilactobacillus reuteri

kcat/KM [mM/s]

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