A novel mechanism for azoreduction.

Ryan A; Laurieri N; Westwood I; Wang CJ; Lowe E; Sim E

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A novel mechanism for azoreduction.

机译：偶氮还原的新机制。

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Azoreductases are important due to their ability to activate anti-inflammatory azo pro-drugs and to detoxify azo dyes. Three genes encoding azoreductases have been identified in Pseudomonas aeruginosa. We describe here a comparison of the three enzymes. The pure recombinant proteins each have a distinct substrate specificity profile against a range of azo substrates. Using the structure of P. aeruginosa azoreductase (paAzoR) 1 and the homology models of paAzoR2 and paAzoR3, we have identified residues important for substrate specificity. We have defined a novel flavin mononucleotide binding cradle, which is a recurrent motif in many flavodoxin-like proteins. A novel structure of paAzoR1 with the azo pro-drug balsalazide bound within the active site was determined by X-ray crystallography and demonstrates that the substrate is present in a hydrazone tautomer conformation. We propose that the structure with balsalazide bound represents an enzyme intermediate and, together with the flavin mononucleotide binding cradle, we propose a novel catalytic mechanism.

机译：偶氮还原酶很重要，因为它们具有激活抗炎性偶氮前药和使偶氮染料解毒的能力。在铜绿假单胞菌中已鉴定出三种编码偶氮还原酶的基因。我们在这里描述了三种酶的比较。每个重组蛋白均具有针对一系列偶氮底物的独特底物特异性谱。使用铜绿假单胞菌偶氮还原酶（paAzoR）1的结构以及paAzoR2和paAzoR3的同源性模型，我们确定了对底物特异性重要的残基。我们已经定义了一种新颖的黄素单核苷酸结合摇篮，它是许多黄素类毒素样蛋白中的一个周期性基序。通过X射线晶体学测定了在活性位点内结合有偶氮前药balsalazide的paAzoR1的新型结构，并证明了该底物存在于t互变异构体构象中。我们提出具有结合巴拉沙肼的结构代表一种酶中间体，并与黄素单核苷酸结合摇篮一起，提出了一种新型的催化机制。

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《Journal of Molecular Biology》 |2010年第1期|共14页
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Ryan A; Laurieri N; Westwood I; Wang CJ; Lowe E; Sim E;
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A novel mechanism for azoreduction.

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