Literature DB >> 20193654

The FMN-dependent two-component monooxygenase systems.

Holly R Ellis1.   

Abstract

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. Copyright 2010 Elsevier Inc. All rights reserved.

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Year:  2010        PMID: 20193654     DOI: 10.1016/j.abb.2010.02.007

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN: 0003-9861            Impact factor:   4.013


  38 in total

1.  Interactions with the substrate phenolic group are essential for hydroxylation by the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase.

Authors:  Chanakan Tongsook; Jeerus Sucharitakul; Kittisak Thotsaporn; Pimchai Chaiyen
Journal:  J Biol Chem       Date:  2011-11-03       Impact factor: 5.157

2.  The C-terminal domain of 4-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii is an autoinhibitory domain.

Authors:  Thanawat Phongsak; Jeerus Sucharitakul; Kittisak Thotsaporn; Worrapoj Oonanant; Jirundon Yuvaniyama; Jisnuson Svasti; David P Ballou; Pimchai Chaiyen
Journal:  J Biol Chem       Date:  2012-06-03       Impact factor: 5.157

3.  StyA1 and StyA2B from Rhodococcus opacus 1CP: a multifunctional styrene monooxygenase system.

Authors:  Dirk Tischler; René Kermer; Janosch A D Gröning; Stefan R Kaschabek; Willem J H van Berkel; Michael Schlömann
Journal:  J Bacteriol       Date:  2010-07-30       Impact factor: 3.490

4.  pH-dependent studies reveal an efficient hydroxylation mechanism of the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase.

Authors:  Nantidaporn Ruangchan; Chanakan Tongsook; Jeerus Sucharitakul; Pimchai Chaiyen
Journal:  J Biol Chem       Date:  2010-10-28       Impact factor: 5.157

5.  Cloning and expression of three ladA-type alkane monooxygenase genes from an extremely thermophilic alkane-degrading bacterium Geobacillus thermoleovorans B23.

Authors:  Chanita Boonmak; Yasunori Takahashi; Masaaki Morikawa
Journal:  Extremophiles       Date:  2014-03-30       Impact factor: 2.395

6.  Microbial Degradation of Pyridine: a Complete Pathway in Arthrobacter sp. Strain 68b Deciphered.

Authors:  Vida Časaitė; Rūta Stanislauskienė; Justas Vaitekūnas; Daiva Tauraitė; Rasa Rutkienė; Renata Gasparavičiūtė; Rolandas Meškys
Journal:  Appl Environ Microbiol       Date:  2020-07-20       Impact factor: 4.792

7.  Fluorescent Mechanism-Based Probe for Aerobic Flavin-Dependent Enzyme Activity.

Authors:  Ian P McCulloch; James J La Clair; Matt J Jaremko; Michael D Burkart
Journal:  Chembiochem       Date:  2016-08-05       Impact factor: 3.164

Review 8.  Monooxygenation of aromatic compounds by flavin-dependent monooxygenases.

Authors:  Pirom Chenprakhon; Thanyaporn Wongnate; Pimchai Chaiyen
Journal:  Protein Sci       Date:  2019-01       Impact factor: 6.725

9.  Aminoperoxide adducts expand the catalytic repertoire of flavin monooxygenases.

Authors:  Arne Matthews; Raspudin Saleem-Batcha; Jacob N Sanders; Frederick Stull; K N Houk; Robin Teufel
Journal:  Nat Chem Biol       Date:  2020-02-17       Impact factor: 15.040

10.  Camphor pathway redux: functional recombinant expression of 2,5- and 3,6-diketocamphane monooxygenases of Pseudomonas putida ATCC 17453 with their cognate flavin reductase catalyzing Baeyer-Villiger reactions.

Authors:  Hiroaki Iwaki; Stephan Grosse; Hélène Bergeron; Hannes Leisch; Krista Morley; Yoshie Hasegawa; Peter C K Lau
Journal:  Appl Environ Microbiol       Date:  2013-03-22       Impact factor: 4.792

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