Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

AoiQ Catalyzes Geminal Dichlorination of 1,3-Diketone Natural Products.

ABSTRACT: Enzymes that can perform halogenation of aliphatic carbons are of significant interest to the synthetic and biocatalysis communities. Here we describe the characterization of AoiQ, a single-component flavin-dependent halogenase (FDH) that catalyzes gem-dichlorination of 1,3-diketone substrates in the biosynthesis of dichlorodiaporthin. AoiQ represents the first biochemically reconstituted FDH that can halogenate an enolizable sp³-hybridized carbon atom.

SUBMITTER: Liu M

PROVIDER: S-EPMC8434754 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Publications

AoiQ Catalyzes Geminal Dichlorination of 1,3-Diketone Natural Products.

Liu Mengting M Ohashi Masao M Hung Yiu-Sun YS Scherlach Kirstin K Watanabe Kenji K Hertweck Christian C Tang Yi Y

Journal of the American Chemical Society 20210506 19

Enzymes that can perform halogenation of aliphatic carbons are of significant interest to the synthetic and biocatalysis communities. Here we describe the characterization of AoiQ, a single-component flavin-dependent halogenase (FDH) that catalyzes gem-dichlorination of 1,3-diketone substrates in the biosynthesis of dichlorodiaporthin. AoiQ represents the first biochemically reconstituted FDH that can halogenate an enolizable sp3-hybridized carbon atom. ...[more]

PMID: 33957045

Similar Datasets

Synthesis of 2,2-difluoro-1,3-diketone and 2,2-difluoro-1,3-ketoester derivatives using fluorine gas.

Project description:Solutions of 1,3-diketones and 1,3-ketoester derivatives react with fluorine to give the corresponding 2,2-difluoro-1,3-dicarbonyl derivatives in the presence of quinuclidine. Quinuclidine reacts with fluorine in situ to generate a fluoride ion that facilitates limiting enolization processes, and an electrophilic N-F fluorinating agent that is reactive towards neutral enol species.

| S-EPMC10910478 | biostudies-literature

Using marine natural products to discover a protease that catalyzes peptide macrocyclization of diverse substrates.

Project description:Small N-C terminally cyclic ribosomal peptides are common in nature, yet the mechanisms underlying their biosyntheses remain largely unknown. We recently identified candidate peptide cyclase genes in the metagenomes of marine animals. Here we report that PatG, a protease discovered in this analysis, cleaves variables, short peptides out of a precursor protein, and cyclizes these peptides in vivo and in vitro.

| S-EPMC2645028 | biostudies-literature

Unleashing the Potential of 1,3-Diketone Analogues as Selective LH2 Inhibitors.

Project description:Lysyl hydroxylase 2 (LH2) catalyzes the formation of highly stable hydroxylysine aldehyde-derived collagen cross-links (HLCCs), thus promoting lung cancer metastasis through its capacity to modulate specific types of collagen cross-links within the tumor stroma. Using 1 and 2 from our previous high-throughput screening (HTS) as lead probes, we prepared a series of 1,3-diketone analogues, 1-18, and identified 12 and 13 that inhibit LH2 with IC50's of approximately 300 and 500 nM, respectively. Compounds 12 and 13 demonstrate selectivity for LH2 over LH1 and LH3. Quantum mechanics/molecular mechanics (QM/MM) modeling indicates that the selectivity of 12 and 13 may stem from noncovalent interactions like hydrogen bonding between the morpholine/piperazine rings with the LH2-specific Arg661. Treatment of 344SQ WT cells with 13 resulted in a dose-dependent reduction in their migration potential, whereas the compound did not impede the migration of the same cell line with an LH2 knockout (LH2KO).

| S-EPMC10577891 | biostudies-literature

Ambient gold-catalyzed O-vinylation of cyclic 1,3-diketone: A vinyl ether synthesis.

Project description:Gold-catalyzed O-vinylation of cyclic 1,3-diketones has been achieved for the first time, which provides direct access to various vinyl ethers. A catalytic amount of copper triflate was identified as the significant additive in promoting this transformation. Both aromatic and aliphatic alkynes are suitable substrates with good to excellent yields.

| S-EPMC3869262 | biostudies-literature

Analysis of Transglucosylation Products of Aspergillus niger α-Glucosidase that Catalyzes the Formation of α-1,2- and α-1,3-Linked Oligosaccharides.

Project description:According to whole-genome sequencing, Aspergillus niger produces multiple enzymes of glycoside hydrolases (GH) 31. Here we focus on a GH31 α-glucosidase, AgdB, from A. niger . AgdB has also previously been reported as being expressed in the yeast species, Pichia pastoris ; while the recombinant enzyme (rAgdB) has been shown to catalyze tranglycosylation via a complex mechanism. We constructed an expression system for A. niger AgdB using Aspergillus nidulans . To better elucidate the complicated mechanism employed by AgdB for transglucosylation, we also established a method to quantify glucosidic linkages in the transglucosylation products using 2D NMR spectroscopy. Results from the enzyme activity analysis indicated that the optimum temperature was 65 °C and optimum pH range was 6.0-7.0. Further, the NMR results showed that when maltose or maltopentaose served as the substrate, α-1,2-, α-1,3-, and small amount of α-1,1-β-linked oligosaccharides are present throughout the transglucosylation products of AgdB. These results suggest that AgdB is an α-glucosidase that serves as a transglucosylase capable of effectively producing oligosaccharides with α-1,2-, α-1,3-glucosidic linkages.

| S-EPMC8311119 | biostudies-literature

1,3-Diketone-Modified Nucleotides and DNA for Cross-Linking with Arginine-Containing Peptides and Proteins.

Project description:Linear or branched 1,3-diketone-linked thymidine 5'-O-mono- and triphosphate were synthesized through CuAAC click reaction of diketone-alkynes with 5-azidomethyl-dUMP or -dUTP. The triphosphates were good substrates for KOD XL DNA polymerase in primer extension synthesis of modified DNA. The nucleotide bearing linear 3,5-dioxohexyl group (HDO) efficiently reacted with arginine-containing peptides to form stable pyrimidine-linked conjugates, whereas the branched 2-acetyl-3-oxo-butyl (PDO) group was not reactive. Reaction with Lys or a terminal amino group formed enamine adducts that were prone to hydrolysis. This reactive HDO modification in DNA was used for bioconjugations and cross-linking with Arg-containing peptides or proteins (e.g. histones).

| S-EPMC8362068 | biostudies-literature

Macroscopic Superlow Friction of Steel and Diamond-Like Carbon Lubricated with a Formanisotropic 1,3-Diketone.

Project description:Energy dissipation due to friction and wear is reducing the energy efficiency and reliability of mechanical systems. Thus, great efforts are being made to minimize friction for technical applications. In our present work, we investigate the tribological behavior of stainless steel 100Cr6 with a-C:H and a-C:H:Si coating lubricated with a surface-active formanisotropic 1,3-diketone. The results show that superlow friction can be achieved on the macroscale using a steel 100Cr6 self pairing (COF ∼ 0.005) and with 100Cr6 in combination with a-C:H coating (COF ∼ 0.008). Furthermore, the replacement of steel with a-C:H coating leads to a considerable decrease of wear. The reduced COF arises from the chemical interaction of the lubricant with the surface and nascent iron ions. It was found that interfacial parameters correlate with tribological results. In addition, the alignment of the formanisotropic molecules in the tribological contact at thin-film lubrication leads to an anisotropic viscosity with a minimum shear resistance in sliding direction. Atomistic simulation of tribochemical interactions was conducted to derive a friction model based on the thin-film lubrication theory. This investigation indicates the potential to substantially reduce friction and wear using this fluid in real technical applications.

| S-EPMC6645003 | biostudies-literature

Enantioselective dichlorination of allylic alcohols.

Project description:The development of an enantioselective allylic alcohol dichlorination catalyzed by dimeric cinchona alkaloid derivatives and employing aryl iododichlorides as chlorine sources is reported. Reaction optimization, exploration of the substrate scope, and a model for stereoinduction are presented.

| S-EPMC3107004 | biostudies-literature

Toward the Total Synthesis of Ryanodol via Oxidative Alkyne-1,3-Diketone Annulation: Construction of a Ryanoid Tetracycle.

Project description:A synthetic strategy conceived with the intent of establishing a novel approach to the de novo construction of ryanoids is described that is based on a recently developed metallacycle-mediated intramolecular oxidative alkyne-1,3-diketone coupling reaction. In short, a one-pot annulation/oxidation sequence is shown to be capable of establishing a densely oxygenated polycyclic intermediate that could be converted to a composition of matter that contains the ABCD tetracyclic ring system present in the ryanoid family of natural products.

| S-EPMC6199674 | biostudies-literature

A natural love of natural products.

Project description:Recent research on the chemistry of natural products from the author's group that led to the receipt of the ACS Ernest Guenther Award in the Chemistry of Natural Products is reviewed. REDOR NMR and synthetic studies established the T-taxol conformation as the bioactive tubulin-binding conformation, and these results were confirmed by the synthesis of compounds which clearly owed their activity or lack of activity to whether or not they could adopt the T-taxol conformation. Similar studies with the epothilones suggest that the current tubulin-binding model needs to be modified. Examples of natural products discovery and biodiversity conservation in Suriname and Madagascar are also presented, and it is concluded that natural products chemistry will continue to make significant contributions to drug discovery.

| S-EPMC2660139 | biostudies-other

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data