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Int. J. Mol. Sci. 2015, 16(12), 28270-28284;

Characterization of Aspartate Kinase from Corynebacterium pekinense and the Critical Site of Arg169

College of Food Science and Engineering, Jilin Agricultural University, Changchun 130118, China
National Engineering Laboratory of Wheat and Corn Deep Processing, Changchun 130118, China
Author to whom correspondence should be addressed.
Academic Editor: Qiang “Shawn” Chen
Received: 19 August 2015 / Revised: 10 November 2015 / Accepted: 11 November 2015 / Published: 27 November 2015
(This article belongs to the Special Issue Protein Engineering)
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Aspartate kinase (AK) is the key enzyme in the biosynthesis of aspartate-derived amino acids. Recombinant AK was efficiently purified and systematically characterized through analysis under optimal conditions combined with steady-state kinetics study. Homogeneous AK was predicted as a decamer with a molecular weight of ~48 kDa and a half-life of 4.5 h. The enzymatic activity was enhanced by ethanol and Ni2+. Moreover, steady-state kinetic study confirmed that AK is an allosteric enzyme, and its activity was inhibited by allosteric inhibitors, such as Lys, Met, and Thr. Theoretical results indicated the binding mode of AK and showed that Arg169 is an important residue in substrate binding, catalytic domain, and inhibitor binding. The values of the kinetic parameter Vmax of R169 mutants, namely, R169Y, R169P, R169D, and R169H AK, with l-aspartate as the substrate, were 4.71-, 2.25-, 2.57-, and 2.13-fold higher, respectively, than that of the wild-type AK. Furthermore, experimental and theoretical data showed that Arg169 formed a hydrogen bond with Glu92, which functions as the entrance gate. This study provides a basis to develop new enzymes and elucidate the corresponding amino acid production. View Full-Text
Keywords: Corynebacterium pekinense; aspartate kinase; characterization; molecular docking Corynebacterium pekinense; aspartate kinase; characterization; molecular docking

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Min, W.; Li, H.; Li, H.; Liu, C.; Liu, J. Characterization of Aspartate Kinase from Corynebacterium pekinense and the Critical Site of Arg169. Int. J. Mol. Sci. 2015, 16, 28270-28284.

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