Expression, Purification, Assay, and Crystal Structure of Perdeuterated Human Arginase I, ⋆,⋆⋆
作者： Luigi Di Costanzo , Martine Moulin , Michael Haertlein , Flora Meilleur , David W. Christianson
DOI: 10.1016/J.ABB.2007.04.036
关键词: Stereochemistry 、 Crystallography 、 Enzyme 、 Isotopic labeling 、 Chemistry 、 Crystal structure 、 Protein structure 、 Arginase 、 Neutron diffraction 、 Hydrolase 、 Yield (chemistry)
摘要: Arginase is a manganese metalloenzyme that catalyzes the hydrolysis of L-arginine to yield L-ornithine and urea. In order establish foundation for future neutron diffraction studies will provide conclusive structural information regarding proton/deuteron positions in enzyme-inhibitor complexes, we have expressed, purified, assayed, determined X-ray crystal structure perdeuterated (i.e., fully deuterated) human arginase I complexed with 2-amino-6-boronohexanoic acid (ABH) at 1.90 A resolution. Prior experiment, it important perdeutaration does not cause any unanticipated or functional changes. Accordingly, find exhibits catalytic activity essentially identical unlabeled enzyme. Additionally, I-ABH complex corresponding Therefore, conclude crystals are suitable crystallographic study.
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