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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 1(66), p. 2-7, 2009

DOI: 10.1107/s1744309109044741

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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

Journal article published in 2009 by Chan-Ju Wang, Nicola Laurieri, Areej Abuhammad ORCID, Edward Lowe, Isaac Westwood, Ali Ryan, Edith Sim
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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 A 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.