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Role of tyrosine 131 in the active site of paAzoR1, an azoreductase with specificity for the inflammatory bowel disease prodrug balsalazide

Role of tyrosine 131 in the active site of paAzoR1, an azoreductase with specificity for the... 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 Å resolution and compared with the wild‐type structure. Tyr131 is important in the architecture of the active site but is not essential for enzymic activity. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Role of tyrosine 131 in the active site of paAzoR1, an azoreductase with specificity for the inflammatory bowel disease prodrug balsalazide

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References (37)

Publisher
Wiley
Copyright
International Union of Crystallography, 2010
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309109044741
pmid
20057057
Publisher site
See Article on Publisher Site

Abstract

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 Å resolution and compared with the wild‐type structure. Tyr131 is important in the architecture of the active site but is not essential for enzymic activity.

Journal

Acta Crystallographica Section FWiley

Published: Jan 1, 2010

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