Identification of a Baeyer–Villiger monooxygenase sequence motif

@article{Fraaije2002IdentificationOA,
  title={Identification of a Baeyer–Villiger monooxygenase sequence motif},
  author={M. Fraaije and N. Kamerbeek and W. V. van Berkel and D. Janssen},
  journal={FEBS Letters},
  year={2002},
  volume={518}
}
Baeyer–Villiger monooxygenases (BVMOs) form a distinct class of flavoproteins that catalyze the insertion of an oxygen atom in a C–C bond using dioxygen and NAD(P)H. Using newly characterized BVMO sequences, we have uncovered a BVMO‐identifying sequence motif: FXGXXXHXXXW(P/D). Studies with site‐directed mutants of 4‐hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB suggest that this fingerprint sequence is critically involved in catalysis. Further sequence analysis showed that… Expand
Evolution study of the Baeyer-Villiger monooxygenases enzyme family: functional importance of the highly conserved residues.
TLDR
Interestingly, residues at the enzyme binding site were found less conserved in terms of sequence evolution, leading sometimes to some important amino acid changes, which could explain the enzyme selectivity and specificity for different ligands. Expand
Discovery of a thermostable Baeyer–Villiger monooxygenase by genome mining
TLDR
This study demonstrates that, using effective annotation tools, genomes can efficiently be exploited as a source of novel BVMOs, and identifies a newly identified biocatalyst that is relatively thermostable and able to perform sulfur oxidations. Expand
Identifying determinants of NADPH specificity in Baeyer-Villiger monooxygenases.
TLDR
The results indicate that the strict NADPH dependency of this class of monooxygenases is based upon recognition of the coenzyme by several basic residues, which could be extrapolated to the sequence-related cyclohexanone monoxygenase. Expand
Crystal structure of a Baeyer-Villiger monooxygenase.
TLDR
The structural studies highlight the functional complexity of this class of flavoenzymes, which coordinate the binding of three substrates in proximity of the flavin cofactor with formation of two distinct catalytic intermediates. Expand
The Origin and Evolution of Baeyer—Villiger Monooxygenases (BVMOs): An Ancestral Family of Flavin Monooxygenases
TLDR
It is proposed that BVMO genes were already present in the last universal common ancestor (LUCA) and their current taxonomic distribution is the result of differential duplication and loss of paralogous genes. Expand
Functional divergence between closely related Baeyer-Villiger monooxygenases from Aspergillus flavus
Baeyer-Villiger monooxygenases (BVMOs) catalyse the chemo-, regio- and enantioselective oxidation of ketones to esters and lactones. To date, most of the cloned BVMOs available are derived fromExpand
Pseudomonad Cyclopentadecanone Monooxygenase Displaying an Uncommon Spectrum of Baeyer-Villiger Oxidations of Cyclic Ketones
TLDR
A new BVMO, cyclopentadecanone monooxygenase (CPDMO), originally derived from Pseudomonas sp. Expand
Discovery of Baeyer-Villiger monooxygenases from photosynthetic eukaryotes
a b s t r a c t Baeyer-Villiger monooxygenases are attractive "green" catalysts able to produce chiral esters or lactones starting from ketones. They can act as natural equivalents of peroxyacidsExpand
Isolation and initial characterization of a novel type of Baeyer–Villiger monooxygenase activity from a marine microorganism
TLDR
Although low, abundance was detected in samples from many marine provinces, confirming the potential for biodiscovery in marine microorganisms. Expand
Genome mining reveals new bacterial type I Baeyer-Villiger monooxygenases with (bio)synthetic potential
Abstract Baeyer-Villiger monooxygenases (BVMOs) are oxidorreductases that catalyze the oxidation of ketones in a very selective manner. By genome mining we detected seven putative type I BVMOs inExpand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 61 REFERENCES
4-Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB. A novel flavoprotein catalyzing Baeyer-Villiger oxidation of aromatic compounds.
TLDR
Characterization of the purified enzyme showed that 4-hydroxyacetophenone monooxygenase (HAPMO) is a homodimer of approximately 140 kDa with each subunit containing a noncovalently bound FAD molecule. Expand
A hydrophobic sequence motif common to N-hydroxylating enzymes.
The first committed step in the biosynthesis of various bacterial and fur,gal siderophores (low-molecular-weight iron chelators that are produc~ in response '~o iron deficiency) of the hydroxamateExpand
New sequence motifs in flavoproteins: Evidence for common ancestry and tools to predict structure
TLDR
It is proposed that flavoproteins have evolved from a well‐differentiated NAD(P)H‐binding protein, and a classification of dinucleotide‐binding proteins that could also serve as an evolutionary scheme is presented. Expand
Identification of a novel conserved sequence motif in flavoprotein hydroxylases with a putative dual function in FAD/NAD(P)H binding
TLDR
A novel conserved sequence motif has been located among the flavoprotein hydroxylases and is proposed to play a dual function in both FAD and NAD(P)H binding. Expand
Structure and mechanism of para‐hydroxybenzoate hydroxylase
  • B. Entsch, W. V. van Berkel
  • Chemistry, Medicine
  • FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 1995
TLDR
The chemical and kinetic mechanisms of this enzyme are described and integrated with an outline of the structure of the protein from crystallographic analysis, unusual because there is no recognizable domain for the binding of NADPH involved in the reaction. Expand
Mechanistic studies of cyclohexanone monooxygenase: chemical properties of intermediates involved in catalysis.
TLDR
The rate-determining step in catalysis was shown to be the release of NADP from the oxidized enzyme, which is consistent with a Baeyer-Villiger rearrangement mechanism for the enzymatic oxygenation of cyclohexanone. Expand
Mechanistic studies on cyclohexanone oxygenase.
TLDR
The accumulated results presented here support a Baeyer-Villiger rearrangement mechanism for the enzymatic oxygenation of cyclohexanone. Expand
Structural studies and synthetic applications of Baeyer-Villiger monooxygenases.
  • A. Willetts
  • Chemistry, Medicine
  • Trends in biotechnology
  • 1997
TLDR
This article reviews some of the established applications, and considers the merits of the various predictive models used to explain the exquisite and unusual selectivity of BVMOs. Expand
Acinetobacter cyclohexanone monooxygenase: gene cloning and sequence determination.
The gene coding for cyclohexanone monooxygenase from Acinetobacter sp. strain NCIB 9871 was isolated by immunological screening methods. We located and determined the nucleotide sequence of the gene.Expand
Flavin-containing monooxygenases: enzymes adapted for multisubstrate specificity.
  • D. Ziegler
  • Chemistry, Medicine
  • Trends in pharmacological sciences
  • 1990
TLDR
Microsomal flavin-containing monooxygenases appears to be ideally adapted to catalyse the detoxification of structurally diverse soft nucleophiles so abundant in food derived from plants. Expand
...
1
2
3
4
5
...