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

Chan Ju Wang, Nicola Laurieri, Areej Abuhammad, Edward Lowe, Isaac Westwood, Ali Ryan, Edith Sim*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

22 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)2-7
Number of pages6
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume66
Issue number1
DOIs
Publication statusPublished - 25 Dec 2009
Externally publishedYes

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