Cloning and overexpression in Escherichia coli of the gene encoding dihydroxyacetone kinase isoenzyme I from Schizosaccharomyces pombe, and its application to dihydroxyacetone phosphate production

被引：0

作者：

N. Itoh

Y. Tujibata

J. Q. Liu

机构：

[1] Biotechnology Research Center,

[2] Toyama Prefectural University,undefined

[3] 5180 Kurokawa Kosugi,undefined

[4] Toyama 939-0398,undefined

[5] Japan e-mail: itoh@pu-toyama.ac.jp Tel.: +81-766-56-7500,undefined

[6] ext. 560 Fax: +81-766-56-2498,undefined

[7] Department of Applied Chemistry and Biotechnology,undefined

[8] Faculty of Engineering,undefined

[9] Fukui University,undefined

[10] Bunkyo 3-9-1,undefined

[11] Fukui 910-8507,undefined

[12] Japan,undefined

来源：

Applied Microbiology and Biotechnology | 1999年 / 51卷

关键词：

Enzyme; Phosphate; Escherichia Coli; Acetone; Amino Acid Sequence;

D O I：

暂无

中图分类号：

学科分类号：

摘要：

The gene dak1 encoding a dihydroxyacetone kinase (DHAK) isoenzyme I, one of two isoenzymes in the Schizosaccharomyces pombe IFO 0354 strain, was cloned and sequenced. The dak1 gene comprises 1743 bp and encodes a protein of 62 245 Da. The deduced amino acid sequence showed a similarity to a putative DHAK of Saccharomyces cerevisiae and DHAK of Citrobacter freundii. The dak1 gene was expressed at a high level in Escherichia coli, and the recombinant enzyme was purified to homogeneity and characterized. The acetone powder of recombinant E. coli cells was used to produce dihydroxyacetone phosphate.

引用

页码：193 / 200

页数：7