Wang Chan-Ju, Laurieri Nicola, Abuhammad Areej, Lowe Edward, Westwood Isaac, Ryan Ali, Sim Edith
Department of Pharmacology, University of Oxford, Mansfield Road, Oxford OX1 3QT, England.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt 1):2-7. doi: 10.1107/S1744309109044741. Epub 2009 Dec 25.
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.
铜绿假单胞菌PAO1菌株的偶氮还原酶1(paAzoR1)催化前药巴柳氮的活化,并以还原型烟酰胺腺嘌呤二核苷酸辅因子作为电子供体还原偶氮染料甲基红。为了研究该酶的作用机制,引入了Y131F突变,并将突变体的酶学性质与野生型酶进行了比较。解析了结合甲基红的突变体的晶体结构,分辨率为2.1 Å,并与野生型结构进行了比较。酪氨酸131在活性位点的结构中很重要,但对酶活性不是必需的。