Hydroxylation of Indole by Laboratory-evolved 2-Hydroxybiphenyl 3-Monooxygenase

Meyer, Andreas; Würsten, Michael; Schmid, Andreas; Kohler, Hans‐Peter E.; Witholt, Bernard

doi:10.1074/jbc.m205621200

Cited by 65 publications

(54 citation statements)

References 47 publications

(63 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…[123] Unfortunately, no BVMO three-dimensional structure is known to date, preventing a knowledge-based site-directed mutagenesis approach to re-engineer the biocatalytic properties of a specific BVMO. Nonetheless, successful application of random mutagenesis techniques has already been reported for a flavoprotein monooxygenase for which structural data are lacking [124,125] . Therefore, the availability of sequence-related BVMO genes will allow fine-tuning of catalytic properties by exploiting random mutagenesis and gene shuf-fling methods.…”

Section: Discussionmentioning

confidence: 97%

Baeyer–Villiger Monooxygenases, an Emerging Family of Flavin‐Dependent Biocatalysts

Janssen²,

et al. 2003

View full text Add to dashboard Cite

Abstract:Baeyer±Villiger monooxygenases (BVMOs) are flavoenzymes that catalyze a remarkably wide variety of oxidative reactions such as regioand enantioselective Baeyer±Villiger oxidations and sulfoxidations. Several of these conversions are difficult to achieve using chemical approaches. Due to their selectivity and catalytic efficiency, BVMOs are highly valuable biocatalysts for the synthesis of a broad range of fine chemicals. For a long time, only one member of this class of flavin-containing biocatalysts had been cloned and overexpressed which has limited their application for synthetic processes. Recently a number of new genes that encode BVMOs have been sequenced and overexpressed. In this paper the biocatalytic properties of recently cloned BVMOs are reviewed. Furthermore, the potential for obtaining novel BVMOs from sequenced genomes will be discussed.

show abstract

Section: Discussionmentioning

confidence: 97%

Baeyer–Villiger Monooxygenases, an Emerging Family of Flavin‐Dependent Biocatalysts

Janssen²,

et al. 2003

View full text Add to dashboard Cite

show abstract

“…Therefore, biological fermentation by recombinant microorganisms may provide a cleaner alternative for large-scale indigo production (Murdock et al 1993). In addition to indigo, different kinds of indigoid pigments, including indirubin can also be produced by E. coli expressing indole oxygenases (O'Connor et al 1997;O'Connor and Hartmans 1998;Nakamura et al 2001;Meyer et al 2002;Choi et al 2003;Furuya et al 2004;Lim et al 2005;McClay et al 2005;Rui et al 2005). Moreover, human cytochrome P450 and bacterial cytochrome P450 proteins have been engineered to produce a variety of indigoids in E. coli (Gillam et al 1999;Li et al 2000;Nakamura et al 2001;Celik et al 2005;Wu et al 2005;Rosic et al 2007;Rosic 2009).…”

Section: Introductionmentioning

confidence: 97%

Identification and characterization of an indigo-producing oxygenase involved in indole 3-acetic acid utilization by Acinetobacter baumannii

Lin

Chen

Huang

et al. 2012

Antonie van Leeuwenhoek

View full text Add to dashboard Cite

Acinetobacter baumannii harbours a gene cluster similar to the iac locus of Pseudomonas putida 1290, which can catabolize the plant hormone indole 3-acetic acid (IAA) as an energy source. However, there has been no evidence showing that IAA can be utilized by A. baumannii. This study showed that A. baumannii can grow in M9 minimal medium containing IAA as the sole carbon source. A mutagenesis study indicated that iacA, encoded in the iac locus of A. baumannii, is involved in the catabolism of IAA. As shown by western blotting analysis, the IacA protein was detected in A. baumannii grown in M9 minimal medium with IAA but not with pyruvate, suggesting that the expression of iacA is regulated by the presence of IAA. In vitro studies have shown that IacA can oxidize indole, an IAA-like molecule, converting it to indoxyl, which spontaneously dimerises to form indigo. In this study, we show that the crude extracts from either wild-type A. baumannii or Escherichia coli overexpressing IacA can oxidize IAA. These results imply that the iac gene cluster of A. baumannii is involved in IAA degradation and that the iacA gene is upregulated when cells encounter IAA in their native environments.

show abstract

“…The transformation of indole to indigo by StyA has also been reported (31). A monooxygenase (2-hydroxybiphenyl 3-monooxygenase) in Pseudomonas azelaica has also been reported to produce indigo, indirubin, and isatin, although it shares little sequence similarity with MoxY (30). These data suggest that moxY is a member of a gene family involved in microbial oxidative or hydroxylative pathways.…”

Section: Activity Of Qsm-1 Is Luxr Dependentmentioning

confidence: 73%

Signal Mimics Derived from a Metagenomic Analysis of the Gypsy Moth Gut Microbiota

Guan

Borlee

et al. 2007

Appl Environ Microbiol

View full text Add to dashboard Cite

Bacterial signaling is an important part of community life, but little is known about the signal transduction pathways of the as-yet-uncultured members of microbial communities. To address this gap, we aimed to identify genes directing the synthesis of signals in uncultured bacteria associated with the midguts of gypsy moth larvae. We constructed a metagenomic library consisting of DNA extracted directly from the midgut microbiota and analyzed it using an intracellular screen designated METREX, which detects inducers of quorum sensing. In this screen, the metagenomic DNA and a biosensor reside in the same cell. The biosensor consists of a quorum-sensing promoter, which requires an acylhomoserine lactone or other small molecule ligand for activation, driving the expression of the reporter gene gfp. We identified an active metagenomic clone encoding a monooxygenase homologue that mediates a pathway of indole oxidation that leads to the production of a quorum-sensing inducing compound. The signal from this clone induces the activities of LuxR from Vibrio fischeri and CviR from Chromobacterium violaceum. This study is the first to identify a new structural class of quorum-sensing inducer from uncultured bacteria.

show abstract

Hydroxylation of Indole by Laboratory-evolved 2-Hydroxybiphenyl 3-Monooxygenase

Cited by 65 publications

References 47 publications

Baeyer–Villiger Monooxygenases, an Emerging Family of Flavin‐Dependent Biocatalysts

Baeyer–Villiger Monooxygenases, an Emerging Family of Flavin‐Dependent Biocatalysts

Identification and characterization of an indigo-producing oxygenase involved in indole 3-acetic acid utilization by Acinetobacter baumannii

Signal Mimics Derived from a Metagenomic Analysis of the Gypsy Moth Gut Microbiota

Contact Info

Product

Resources

About