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Published online before print June 23, 2008, 10.1110/ps.035725.108
Protein Science (2008), 17:1603-1610. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society
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Engineering of halophilic enzymes: Two acidic amino acid residues at the carboxy-terminal region confer halophilic characteristics to Halomonas and Pseudomonas nucleoside diphosphate kinases

Hiroko Tokunaga1, Tsutomu Arakawa2, and Masao Tokunaga1

1 Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University, Kagoshima 890-0065, Japan
2 Alliance Protein Laboratories, Thousand Oaks, California 91360, USA

(RECEIVED April 8, 2008; FINAL REVISION June 13, 2008; ACCEPTED June 13, 2008)

Nucleoside diphosphate kinase from Halomonas sp. 593 (HaNDK) exhibits halophilic characteristics. Residues 134 and 135 in the carboxy-terminal region of HaNDK are Glu–Glu, while those of its homologous counterpart of non-halophilic Pseudomonas NDK (PaNDK) are Ala–Ala. The double mutation, E134A-E135A, in HaNDK results in the loss of the halophilic characteristics, and, conversely, the double mutation of A134E-A135E in PaNDK confers halophilic characters to this enzyme, indicating that the charged state of these two residues that are located in the C-terminal region plays a critical role in determining halophilic characteristics. The importance of these two residues versus the net negative charges will be discussed in relation to the halophilicity of NDK.

Keywords: halophilic; Halomonas; nucleoside diphosphate kinase; negative charge; solubility; reversibility; stability


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