Structural Insights into 6-Hydroxypseudooxynicotine Amine Oxidase from <i>Pseudomonas geniculata</i> N1, the Key Enzyme Involved in Nicotine Degradation
Gongquan Liu, Weiwei Wang, Fangyuan He, Peng Zhang, Ping Xu, Hongzhi Tang
Abstract
Nicotine is a major tobacco alkaloid in tobacco waste. Pyridine and pyrrolidine pathways are the two best-elucidated nicotine metabolic pathways; Pseudomonas geniculata N1 catabolizes nicotine via a hybrid between the pyridine and pyrrolidine pathways. The crucial enzyme, 6-hydroxypseudooxynicotine amine oxidase (HisD), links the upstream and downstream portions of the VPP pathway; however, there is little structural information about this important enzyme. In this study, we determined the crystal structure of HisD from Pseudomonas geniculata N1. Its basic insights about the structure may help us to guide the engineering of such enzymes for bioremediation and bioconversion applications.