Nucleoside Diphosphate Kinase from Psychrophilic Pseudoalteromonas Sp. AS-131 Isolated from Antarctic Ocean

Overview

Journal Protein J

Publisher Springer

Specialty Biochemistry

Date 2015 Aug 6

PMID 26242868

Citations 2

Authors

Yasushi Yonezawa

Aiko Nagayama

Hiroko Tokunaga

Matsujiro Ishibashi

Shigeki Arai

Ryota Kuroki

Keiichi Watanabe

Tsutomu Arakawa

Masao Tokunaga

Affiliations

Soon will be listed here.

Abstract

Nucleoside diphosphate kinase isolated from psychrophilic Pseudoalteromonas sp. AS-131 (ASNDK) was expressed in Escherichia coli and purified to homogeneity. Comparing to mesophilic NDK isolated from Pseudomonas aeruginosa, ASNDK exhibited highly elevated thermolability: E. coli expression at 37 °C as a denatured insoluble form, 30 °C lower optimum temperature of enzymatic activity, and greatly reduced heat stability with 38 °C lower Tm value, fourfold higher Km and reduced Kcat/Km by 0.4-fold upon reaction temperature increase from 20 to 37 °C. The subunit structure of ASNDK was suggested to be dimer, as in NDKs isolated from moderate halophiles.

Citing Articles

Structure, Folding and Stability of Nucleoside Diphosphate Kinases.

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Reversible Activation of Halophilic β-lactamase from Methanol-Induced Inactive Form: Contrast to Irreversible Inactivation of Non-Halophilic Counterpart.

Tokunaga H, Maeda J, Arakawa T, Tokunaga M Protein J. 2017; 36(3):228-237.

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