Cloning and expression in Escherichia coli of the D-aspartate oxidase gene from the yeast Cryptococcus humicola and characterization of the recombinant enzyme.

Cloning and expression in Escherichia coli of the D-aspartate oxidase gene from the yeast Cryptococcus humicola and characterization of the recombinant enzyme. Research Abstract Details 

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Cloning and expression in Escherichia coli of the D-aspartate oxidase gene from the yeast Cryptococcus humicola and characterization of the recombinant enzyme. Abstract Text:

Shouji Takahashi,Toshiyuki Takahashi,Yoshio Kera,Ryuji Matsunaga,Hiroo Shibuya,Ryo-hei Yamada,

The D-aspartate oxidase (DDO) from the yeast Cryptococcus humicola UJ1 (ChDDO) is highly specific to D-aspartate. The gene encoding ChDDO was cloned and expressed in Escherichia coli. Sequence analysis of the ChDDO gene showed that an open reading frame of 1,110 bp interrupted by two introns encodes a protein of 370 amino acids. The deduced amino acid sequence showed an FAD-binding motif and a peroxisomal targeting signal 1 in the N-terminal region and at the C-terminus, respectively, and also the presence of certain catalytically important amino acid residues corresponding to those catalytically important in D-amino acid oxidase (DAO). The sequence exhibited only a moderate identity to human (27.4%) and bovine (28.0%) DDOs, and a rather higher identity to yeast and fungal DAOs (30.4-33.2%). Similarly, phylogenetic analysis showed that ChDDO is more closely related to yeast and fungal DAOs than to mammalian DDOs. The gene expression was regulated at the transcriptional level and specifically induced by the presence of D-aspartate as the sole nitrogen source. ChDDO was expressed in an active form in E. coli to an approximately 5-fold greater extent than in yeast. The purified recombinant enzyme was identical to the native enzyme in physicochemical and catalytic properties.

Cloning and expression in Escherichia coli of the D-aspartate oxidase gene from the yeast Cryptococcus humicola and characterization of the recombinant enzyme. Publishing Authors By Initials

S Takahashi,T Takahashi,Y Kera,R Matsunaga,H Shibuya,RH Yamada,

For similar environment and public health: environment: environment, controlled: temperature research abstracts see: environment and public health: environment: environment, controlled: temperature research

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Cloning and expression in Escherichia coli of the D-aspartate oxidase gene from the yeast Cryptococcus humicola and characterization of the recombinant enzyme. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 135

Page Numbers: 533-40

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Apr

YEAR: 2004

Cloning and expression in Escherichia coli of the D-aspartate oxidase gene from the yeast Cryptococcus humicola and characterization of the recombinant enzyme. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Cloning and expression in Escherichia coli of the D-aspartate oxidase gene from the yeast Cryptococcus humicola and characterization of the recombinant enzyme. Keywords Mesh Terms:

KEYWORDS: Temperature

MESH TERMS: metabolism

Chemical & Substance for Abstract: Cloning and expression in Escherichia coli of the D-aspartate oxidase gene from the yeast Cryptococcus humicola and characterization of the recombinant enzyme. Information

Substance Name: D-Amino-Acid Oxidase

Registry Number: EC 1.4.3.3

Grant and Affiliation Information for Cloning and expression in Escherichia coli of the D-aspartate oxidase gene from the yeast Cryptococcus humicola and characterization of the recombinant enzyme.

AFFILIATION: Department of Environmental Systems Engineering, Nagaoka University of Technology, Nagaoka, Niigata 940-2188.

Country: Japan

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MEDLINETA: J Biochem

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ACCESSION NUMBER: AB121230

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