Production of completely flavinylated histamine dehydrogenase, unique covalently bound flavin, and iron-sulfur cluster-containing enzyme of Nocardioides simplex in Escherichia coli, and its properties

被引：12

作者：

Fujieda, N ^{[1
]}

Tsuse, N ^{[1
]}

Satoh, A ^{[1
]}

Ikeda, T ^{[1
]}

Kano, K ^{[1
]}

机构：

[1] Kyoto Univ, Grad Sch Agr, Div Appl Life Sci, Sakyo Ku, Kyoto 6068502, Japan

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 2005年 / 69卷 / 12期

基金：

日本学术振兴会;

关键词：

histamine dehydrogenase; trimethylamine; dehydrogenase; amine dehydrogenase; 6-S-cysteinyl-FMN; iron-sulfur flavoprotein;

D O I：

10.1271/bbb.69.2459

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The hind gene of histamine dehydrogenase from Nocardioides simplex was overexpressed in Escherichia coli, and the resulting enzyme was purified to homogeneity. The purified recombinant enzyme is almost identical with the native enzyme in view of molecular weight and specific activity, and is stoichiometrically assembled with the three cofactors 6-S-cysteinyl FMN, 4Fe-4S cluster, and ADP.

引用

页码：2459 / 2462

页数：4

共 18 条

[1] Over-expression in Escherichia coli, functional characterization and refolding of rat dimethylglycine dehydrogenase [J].

Brizio, C ;

Brandsch, R ;

Bufano, D ;

Pochini, L ;

Indiveri, C ;

Barile, M .

PROTEIN EXPRESSION AND PURIFICATION, 2004, 37 (02) :434-442

[2] INHIBITION OF METHYLENE-BLUE FORMATION DURING DETERMINATION OF ACID-LABILE SULFIDE OF IRON-SULFUR PROTEIN SAMPLES CONTAINING DITHIONITE [J].

CHEN, JS ;

MORTENSON, LE .

ANALYTICAL BIOCHEMISTRY, 1977, 79 (1-2) :157-165

[3] Structure of a quinohemoprotein amine dehydrogenase with an uncommon redox cofactor and highly unusual crosslinking [J].

Datta, S ;

Mori, Y ;

Takagi, K ;

Kawaguchi, K ;

Chen, ZW ;

Okajima, T ;

Kuroda, S ;

Ikeda, T ;

Kano, K ;

Tanizawa, K ;

Mathews, FS .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (25) :14268-14273

[4] 6-S-cysteinyl flavin mononucleotide-containing histamine dehydrogenase from Nocardioides simplex:: Molecular cloning, sequencing, overexpression, and characterization of redox centers of enzyme [J].

Fujieda, N ;

Satoh, A ;

Tsuse, N ;

Kano, K ;

Ikeda, T .

BIOCHEMISTRY, 2004, 43 (33) :10800-10808

[5] PROCESSING OF BACILLUS-SUBTILIS SUCCINATE-DEHYDROGENASE AND CYTOCHROME B-558 POLYPEPTIDES - LACK OF COVALENTLY BOUND FLAVIN IN THE BACILLUS ENZYME EXPRESSED IN ESCHERICHIA-COLI [J].

HEDERSTEDT, L ;

BERGMAN, T ;

JORNVALL, H .

FEBS LETTERS, 1987, 213 (02) :385-390

[6] Cloning and characterization of histamine dehydrogenase from Nocardioide simplex [J].

Limburg, J ;

Mure, M ;

Klinman, JP .

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2005, 436 (01) :8-22

[7] A NEW COFACTOR IN A PROKARYOTIC ENZYME - TRYPTOPHAN TRYPTOPHYLQUINONE AS THE REDOX PROSTHETIC GROUP IN METHYLAMINE DEHYDROGENASE [J].

MCINTIRE, WS ;

WEMMER, DE ;

CHISTOSERDOV, A ;

LIDSTROM, ME .

SCIENCE, 1991, 252 (5007) :817-824

[8] DIMETHYLAMINE DEHYDROGENASE FROM HYPHOMICROBIUM-X - PURIFICATION AND SOME PROPERTIES OF A NEW ENZYME THAT OXIDIZES SECONDARY-AMINES [J].

MEIBERG, JBM ;

HARDER, W .

JOURNAL OF GENERAL MICROBIOLOGY, 1979, 115 (NOV) :49-58

[9] Crystal structure of quinohemoprotein amine dehydrogenase from Pseudomonas putida -: Identification of a novel quinone cofactor encaged by multiple thioether cross-bridges [J].

Satoh, A ;

Kim, JK ;

Miyahara, I ;

Devreese, B ;

Vandenberghe, I ;

Hacisalihoglu, A ;

Okajima, T ;

Kuroda, S ;

Adachi, O ;

Duine, JA ;

Van Beeumen, J ;

Tanizawa, K ;

Hirotsu, K .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (04) :2830-2834

[10]

SCRUTTON NS, 1994, J BIOL CHEM, V269, P13942

← 1 2 →