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Literature summary extracted from

  • Park, K.; Mera, P.E.; Escalante-Semerena, J.C.; Brunold, T.C.
    Spectroscopic characterization of active-site variants of the PduO-type ATP:corrinoid adenosyltransferase from Lactobacillus reuteri: insights into the mechanism of four-coordinate Co(II)corrinoid formation (2012), Inorg. Chem., 51, 4482-4494.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.17 gene pduO, recombinant overexpression of His-tagged wild-type and mutant PduOs in Escherichia coli Limosilactobacillus reuteri

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.17 D35N site-directed mutagenesis Limosilactobacillus reuteri
2.5.1.17 F112A site-directed mutagenesis Limosilactobacillus reuteri
2.5.1.17 F112H site-directed mutagenesis Limosilactobacillus reuteri
2.5.1.17 F187A site-directed mutagenesis Limosilactobacillus reuteri
2.5.1.17 R128K site-directed mutagenesis Limosilactobacillus reuteri
2.5.1.17 R132K site-directed mutagenesis Limosilactobacillus reuteri
2.5.1.17 S159A site-directed mutagenesis Limosilactobacillus reuteri
2.5.1.17 V186A site-directed mutagenesis Limosilactobacillus reuteri

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.17 ATP + cob(I)alamin Limosilactobacillus reuteri
-
 triphosphate + adenosylcob(I)alamine
-
 ?
2.5.1.17 ATP + cobinamide Limosilactobacillus reuteri
-
 triphosphate + adenosylcobinamide
-
 ?
2.5.1.17 additional information Limosilactobacillus reuteri The PduO-type ATP:corrinoid adenosyltransferase catalyzes the transfer of the adenosyl-group of ATP to Co1+-cobalamin and Co1+-cobinamide substrates to synthesize adenosylcobalamin and adenosylcobinamide, respectively ?
-
 ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.17 recombinant His-tagged wild-type and mutant PduOs from Escherichia coli by nickel affinity chromatography to over 99% homogeneity Limosilactobacillus reuteri

Reaction

EC Number Reaction Comment Organism Reaction ID
2.5.1.17 2 ATP + 2 cob(II)alamin + a reduced flavoprotein = 2 triphosphate + 2 adenosylcob(III)alamin + an oxidized flavoprotein to overcome the thermodynamically challenging Co2+ -> Co1+ reduction, the enzyme drastically weakens the axial ligand-Co2+ bond so as to generate effectively four-coordinate Co2+-corrinoid species, mechanism, overview. The entire hydrophobic pocket below the corrin ring, and not just residue F112, is critical for the removal of the axial ligand from the cobalt center of the Co2+-corrinoids. Large role of the ATP-induced active-site conformational changes with respect to the formation of 4c Co(II)Cbl Limosilactobacillus reuteri
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.17 ATP + cob(I)alamin
-
 Limosilactobacillus reuteri triphosphate + adenosylcob(I)alamine
-
 ?
2.5.1.17 ATP + cobinamide
-
 Limosilactobacillus reuteri triphosphate + adenosylcobinamide
-
 ?
2.5.1.17 additional information The PduO-type ATP:corrinoid adenosyltransferase catalyzes the transfer of the adenosyl-group of ATP to Co1+-cobalamin and Co1+-cobinamide substrates to synthesize adenosylcobalamin and adenosylcobinamide, respectively Limosilactobacillus reuteri ?
-
 ?
2.5.1.17 additional information to overcome the thermodynamically challenging Co2+ -> Co1+ reduction, the enzyme drastically weakens the axial ligand-Co2+ bond so as to generate effectively four-coordinate Co2+-corrinoid species, mechanism, overview. The entire hydrophobic pocket below the corrin ring, and not just residue F112, is critical for the removal of the axial ligand from the cobalt center of the Co2+-corrinoids. Large role of the ATP-induced active-site conformational changes with respect to the formation of 4c Co(II)Cbl Limosilactobacillus reuteri ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.17 PduO
-
 Limosilactobacillus reuteri
2.5.1.17 PduO-type adenosine 5'-triphosphate:corrinoid adenosyltransferase
-
 Limosilactobacillus reuteri
2.5.1.17 PduO-type ATP:corrinoid adenosyltransferase
-
 Limosilactobacillus reuteri

General Information

EC Number General Information Comment Organism
2.5.1.17 additional information active-site region of wild-type and mutant PduOs complexed with Co(II)Cbl and cosubstrate ATP, structure determination and modeling, overview Limosilactobacillus reuteri