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Literature summary extracted from

  • Kuznetsov, V.Y.; Blair, E.; Farmer, P.J.; Poulos, T.L.; Pifferitti, A.; Sevrioukova, I.F.
    The putidaredoxin reductase-putidaredoxin electron transfer complex: theoretical and experimental studies (2005), J. Biol. Chem., 280, 16135-16142.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.18.1.5 expression in Escherichia coli Pseudomonas putida

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.18.1.5 computational modeling based on crystal structures of putidaredoxin Ptxand putidaredoxin reductase PdR. In the model, Pdx is docked above the isoalloxazine ring of FAD of Pdr with the distance between the flavin and [2Fe-2S] of 14.6 A. This mode of interaction allows Pdx to easily adjust and optimize orientation of its cofactor relative to Pdr. The key residues of Pdx located at the center are Asp38 and Trp106, and at the edge of the protein-protein interface are Tyr33 and Arg66 Pseudomonas putida

Protein Variants

EC Number Protein Variants Comment Organism
1.18.1.5 D38A mutation does not affect assembly of the [2Fe-2S] cluster and results in a marginal change in the redox potential of Pdx. 45% of wild-type activity Pseudomonas putida
1.18.1.5 D38N mutation does not affect assembly of the [2Fe-2S] cluster and results in a marginal change in the redox potential of Pdx. 33% of wild-type activity Pseudomonas putida
1.18.1.5 R66A mutation does not affect assembly of the [2Fe-2S] cluster and results in a marginal change in the redox potential of Pdx. 25% of wild-type activity Pseudomonas putida
1.18.1.5 R66E mutation does not affect assembly of the [2Fe-2S] cluster and results in a marginal change in the redox potential of Pdx. 21% of wild-type activity Pseudomonas putida
1.18.1.5 W106A mutation does not affect assembly of the [2Fe-2S] cluster and results in a marginal change in the redox potential of Pdx. 54% of wild-type activity Pseudomonas putida
1.18.1.5 W106Delta mutation does not affect assembly of the [2Fe-2S] cluster and results in a marginal change in the redox potential of Pdx. 102% of wild-type activity Pseudomonas putida
1.18.1.5 W106F mutation does not affect assembly of the [2Fe-2S] cluster and results in a marginal change in the redox potential of Pdx. 83% of wild-type activity Pseudomonas putida
1.18.1.5 Y33A mutation does not affect assembly of the [2Fe-2S] cluster and results in a marginal change in the redox potential of Pdx. 26% of wild-type activity Pseudomonas putida
1.18.1.5 Y33F mutation does not affect assembly of the [2Fe-2S] cluster and results in a marginal change in the redox potential of Pdx. 21% of wild-type activity Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.5 Pseudomonas putida P16640
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.5 additional information bulky side chains of Tyr33, Arg66, and Trp106 prevent tight binding of oxidized Pdx and facilitate dissociation of the reduced iron-sulfur protein from Pdr. Transfer of an electron from FAD to [2Fe-2S] can occur with various orientations between the cofactors through multiple electron transfer pathways that do not involve Trp106 but are likely to include Asp38 and Cys39 Pseudomonas putida ?
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Subunits

EC Number Subunits Comment Organism
1.18.1.5 More Pdr-Pdx complex formation is mainly driven by steric complementarity, bulky side chains of Tyr33, Arg66, and Trp106 prevent tight binding of oxidized Pdx and facilitate dissociation of the reduced iron-sulfur protein from Pdr Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.5 iron-sulfur centre [2Fe-2S] cluster Pseudomonas putida