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Literature summary extracted from

  • Churbanova, I.Y.; Poulos, T.L.; Sevrioukova, I.F.
    Production and characterization of a functional putidaredoxin reductase-putidaredoxin covalent complex (2010), Biochemistry, 49, 58-67.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.5 Pseudomonas putida
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Subunits

EC Number Subunits Comment Organism
1.18.1.5 More cross-linking of putidaredoxin and putidaredoxin reductase by 1-ethyl 3-[3-(dimethylamino)propyl]carbodiimide, EDC. EDC promotes formation of stoichiometric Pdr-Pdx complexes only when carboxyl groups on putidaredoxin are activated. The putidaredoxin-putidaredoxin reductase C73S/C85S conjugate protein is more efficient in electron transfer to cytochrome c and, in the presence of saturating levels of P450cam, more effectively supports camphor hydroxylation. The cross-linked complex is physiologically relevant and represents a suitable model for mechanistic studies, and molecular recognition between putidaredoxin and putidaredoxin reductase is redox-controlled and assisted by the putidaredoxin Glu72 and putidaredoxin reducase Lys409 charge-charge interactions Pseudomonas putida