The FMN-dependent two-component monooxygenase systems

被引：110

作者：

Ellis, Holly R. ^{[1
]}

机构：

[1] Auburn Univ, Dept Chem & Biochem, Auburn, AL 36849 USA

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 2010年 / 497卷 / 1-2期

关键词：

Two-component monooxygenase systems; FMN reductase; FMN-dependent monooxygenase; Flavin mononucleotide; Flavin transfer; REDUCED FLAVIN MONONUCLEOTIDE; ENCODING NITRILOTRIACETATE MONOOXYGENASE; P-HYDROXYPHENYLACETATE; 3-HYDROXYLASE; BACILLUS-THERMOGLUCOSIDASIUS A7; ISOBUTYLAMINE N-HYDROXYLASE; UNUSUAL FOLDED CONFORMATION; 2-PROTEIN COMPONENT ENZYME; VIBRIO-HARVEYI LUCIFERASE; SITE-DIRECTED MUTATION; HEINTZII ATCC 29600;

D O I：

10.1016/j.abb.2010.02.007

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 FMN-dependent two-component monooxygenase systems catalyze a diverse range of reactions. These two-component systems are composed of an FMN reductase enzyme and a monooxygenase enzyme that catalyze the oxidation of various substrates. The role of the reductase is to supply reduced Flavin to the monooxygenase enzyme, while the monooxygenase enzyme utilizes the reduced flavin to activate molecular oxygen. Unlike flavoproteins with a tightly or covalently bound prosthetic group, these enzymes catalyze the reductive and oxidative half-reaction on two separate enzymes. An interesting feature of these enzymes is their ability to transfer reduced Flavin from the reductase to the monooxygenase enzyme. This review covers the reported mechanistic and structural properties of these enzyme systems, and evaluates the mechanism of flavin transfer. (C) 2010 Elsevier Inc. All rights reserved.

引用

页码：1 / 12

页数：12

共 99 条

[1] Detection of protein-protein interactions in the alkanesulfonate monooxygenase system from Escherichia coli [J].

Abdurachim, Kholis ;

Ellis, Holly R. .

JOURNAL OF BACTERIOLOGY, 2006, 188 (23) :8153-8159

[2]

ABUSOUD HM, 1993, J BIOL CHEM, V268, P7699

[3] Structure of the monooxygenase component of a two-component flavoprotein monooxygenase [J].

Alfieri, Andrea ;

Fersini, Francesco ;

Ruangchan, Nantidaporn ;

Prongjit, Methinee ;

Chaiyen, Pimchai ;

Mattevi, Andrea .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2007, 104 (04) :1177-1182

[4]

ARUNACHALAM U, 1992, J BIOL CHEM, V267, P25848

[5]

BALDWIN TO, 1978, J BIOL CHEM, V253, P5551

[6] SITE-DIRECTED MUTAGENESIS OF BACTERIAL LUCIFERASE - ANALYSIS OF THE ESSENTIAL THIOL [J].

BALDWIN, TO ;

CHEN, LH ;

CHLUMSKY, LJ ;

DEVINE, JH ;

ZIEGLER, MM .

JOURNAL OF BIOLUMINESCENCE AND CHEMILUMINESCENCE, 1989, 4 (01) :40-48

[7] COVALENT STRUCTURE OF SUBUNITS OF BACTERIAL LUCIFERASE - NH2-TERMINAL SEQUENCE DEMONSTRATES SUBUNIT HOMOLOGY [J].

BALDWIN, TO ;

ZIEGLER, MM ;

POWERS, DA .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1979, 76 (10) :4887-4889

[8]

BALDWIN TO, 1992, CHEM BIOCH FLAVOENZY, P467

[9] Multiple pathways guide oxygen diffusion into flavoenzyme active sites [J].

Baron, Riccardo ;

Riley, Conor ;

Chenprakhon, Pirom ;

Thotsaporn, Kittisak ;

Winter, Remko T. ;

Alfieri, Andrea ;

Forneris, Federico ;

van Berkel, Willem J. H. ;

Chaiyen, Pimchai ;

Fraaije, Marco W. ;

Mattevi, Andrea ;

McCammon, J. Andrew .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2009, 106 (26) :10603-10608

[10] CLONING AND ANALYSIS OF STRUCTURAL GENES FROM STREPTOMYCES-PRISTINAESPIRALIS ENCODING ENZYMES INVOLVED IN THE CONVERSION OF PRISTINAMYCIN-IIB TO PRISTINAMYCIN-IIA (PIIA) - PIIA SYNTHASE AND NADH-RIBOFLAVIN 5'-PHOSPHATE OXIDOREDUCTASE [J].

BLANC, V ;

LAGNEAUX, D ;

DIDIER, P ;

GIL, P ;

LACROIX, P ;

CROUZET, J .

JOURNAL OF BACTERIOLOGY, 1995, 177 (18) :5206-5214

← 1 2 3 4 5 6 7 8 9 10 →