Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 66, Issue -, Pages 2-7Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309109044741
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Funding
- Cancer Research UK [6947] Funding Source: Medline
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Azoreductase 1 from Pseudomonas aeruginosa strain PAO1 (paAzoR1) catalyses the activation of the prodrug balsalazide and reduces the azo dye methyl red using reduced nicotinamide adenine dinucleotide cofactor as an electron donor. To investigate the mechanism of the enzyme, a Y131F mutation was introduced and the enzymic properties of the mutant were compared with those of the wild-type enzyme. The crystallographic structure of the mutant with methyl red bound was solved at 2.1 angstrom resolution and compared with the wildtype structure. Tyr131 is important in the architecture of the active site but is not essential for enzymic activity.
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