Browse
Submit Data
Databases
API
Help

Dataset Information

21 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Enzymatic degradation of chlorodiamino-s-triazine.

ABSTRACT: 2-Chloro-4,6-diamino-s-triazine (CAAT) is a metabolite of atrazine biodegradation in soils. Atrazine chlorohydrolase (AtzA) catalyzes the dechlorination of atrazine but is unreactive with CAAT. In this study, melamine deaminase (TriA), which is 98% identical to AtzA, catalyzed deamination of CAAT to produce 2-chloro-4-amino-6-hydroxy-s-triazine (CAOT). CAOT underwent dechlorination via hydroxyatrazine ethylaminohydrolase (AtzB) to yield ammelide. This represents a newly discovered dechlorination reaction for AtzB. Ammelide was subsequently hydrolyzed by N-isopropylammelide isopropylaminohydrolase to produce cyanuric acid, a compound metabolized by a variety of soil bacteria.

SUBMITTER: Seffernick JL

PROVIDER: S-EPMC124118 | biostudies-literature | 2002 Sep

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Publications

Enzymatic degradation of chlorodiamino-s-triazine.

Seffernick Jennifer L JL Shapir Nir N Schoeb Michael M Johnson Gilbert G Sadowsky Michael J MJ Wackett Lawrence P LP

Applied and environmental microbiology 20020901 9

2-Chloro-4,6-diamino-s-triazine (CAAT) is a metabolite of atrazine biodegradation in soils. Atrazine chlorohydrolase (AtzA) catalyzes the dechlorination of atrazine but is unreactive with CAAT. In this study, melamine deaminase (TriA), which is 98% identical to AtzA, catalyzed deamination of CAAT to produce 2-chloro-4-amino-6-hydroxy-s-triazine (CAOT). CAOT underwent dechlorination via hydroxyatrazine ethylaminohydrolase (AtzB) to yield ammelide. This represents a newly discovered dechlorination ...[more]

PMID: 12200330

Similar Datasets

BET, thermal degradation, and FTIR spectras of triazine polyamine polymers.

Project description:Here we show effect of the polyamine polymer chain length to BET isotherms. According to IUPAC classification [1], all three polymers are fitting type 1 physical adsorption isotherm with H3 hysteresis (except for EDA having H2 hysteresis). Moreover, TG and TGA analysis of polymers triazine-ethylenediamine (EDA) and triazine-triethylenetetramine (TETA) are provided. Due to the similarities of the structure, main decomposition temperatures are close to each other (between 593 K and 873 K). In order to understand change of FTIR spectra with adsorption and stripping Au(III), fresh, Au(III) adsorbed and recycled spectras of polymers measured. For further discussions about the effect of chain length to adsorption of Au(III) onto triazine polyamine polymer particles "Au (III) Uptake by Triazine Polyamine Polymers: Mechanism, Kinetic and Equilibrium Studies" Can et al. [2] (article in press).

| S-EPMC5331151 | biostudies-literature

Enzymatic degradation of multiwalled carbon nanotubes.

Project description:Because of their unique properties, carbon nanotubes and, in particular, multiwalled carbon nanotubes (MWNTs) have been used for the development of advanced composite and catalyst materials. Despite their growing commercial applications and increased production, the potential environmental and toxicological impacts of MWNTs are not fully understood; however, many reports suggest that they may be toxic. Therefore, a need exists to develop protocols for effective and safe degradation of MWNTs. In this article, we investigated the effect of chemical functionalization of MWNTs on their enzymatic degradation with horseradish peroxidase (HRP) and hydrogen peroxide (H(2)O(2)). We investigated HRP/H(2)O(2) degradation of purified, oxidized, and nitrogen-doped MWNTs and proposed a layer-by-layer degradation mechanism of nanotubes facilitated by side wall defects. These results provide a better understanding of the interaction between HRP and carbon nanotubes and suggest an eco-friendly way of mitigating the environmental impact of nanotubes.

| S-EPMC3113459 | biostudies-literature

Lateral transfer of genes for hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) degradation.

Project description:Recent studies demonstrated that degradation of the military explosive hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) by species of Rhodococcus, Gordonia, and Williamsia is mediated by a novel cytochrome P450 with a fused flavodoxin reductase domain (XplA) in conjunction with a flavodoxin reductase (XplB). Pulse field gel analysis was used to localize xplA to extrachromosomal elements in a Rhodococcus sp. and distantly related Microbacterium sp. strain MA1. Comparison of Rhodococcus rhodochrous 11Y and Microbacterium plasmid sequences in the vicinity of xplB and xplA showed near identity (6,710 of 6,721 bp). Sequencing of the associated 52.2-kb region of the Microbacterium plasmid pMA1 revealed flanking insertion sequence elements and additional genes implicated in RDX uptake and degradation.

| S-EPMC2681654 | biostudies-literature

UV and temperature effects on chloroacetanilide and triazine herbicides degradation and cytotoxicity.

Project description:The purpose of this study was to explore the stability and toxicity of the herbicides and their degradation byproduct after exposure to different environmental factors. Triazines (atrazine, propazine, simazine) and chloroacetanilides (acetochlor, alachlor, metolachlor) which are commonly used herbicides were evaluated for cytotoxicity in different UV (254 nm and 365 nm) and temperature (4 °C, 23 °C, and 40 °C) conditions as well as degradation rates. Atrazine with the highest LD50 (4.23 μg mL-1) was less toxic than the other tested triazine herbicides Chloroacetanilides tested were more toxic than tested triazines, with LD50 0.08-1.42 μg mL-1 vs 1.44-4.23 μg mL-1, respectively. Alachlor with LD50 0.08 μg mL-1 showed the strongest toxic response as compared with other tested herbicides. Temperatures only did not alter cytotoxicity of the tested herbicides, except for acetochlor and alachlor showing about 45 % more cell death after exposure to 40 °C for 2 h. At all 3 tested temperatures, 2 h of UV treatments did not affect cytotoxic effects of the tested herbicides, except for acetochlor and alachlor. At 4 °C, acetochlor toxicity was attenuated about 63 % after UV 365 nm exposure; but alachlor toxicity was enhanced after either UV 254 or 365 nm exposure for about 40 % and 24 %, respectively. At 23 °C, acetochlor toxicity was enhanced about 35 % after UV 254 nm exposure, but attenuated about 48 % after UV 365 nm exposure. Alachlor toxicity was enhanced about 34 % after UV 254 nm and 23 °C exposure. In combination of UV 254 nm and 40 °C, acetochlor toxicity was lowered by 63 % and alachlor toxicity was no change as compared with 4 °C, no UV group. After co-treatment with UV 365 nm and 40 °C both acetochlor and alachlor toxicity was enhanced 55 % and 80 %, respectively. Through degradation analysis by LC-MS/MS, alachlor showed the most dramatic degradation (only 0.58 %-10.58 % remaining) after heat and UV treatments.

| S-EPMC8461356 | biostudies-literature

Organochlorinated pesticides expedite the enzymatic degradation of DNA.

Project description:Extracellular DNA in the environment may play important roles in genetic diversity and biological evolution. However, the influence of environmental persistent organic contaminants such as organochlorinated pesticides (e.g., hexachlorocyclohexanes [HCHs]) on the enzymatic degradation of extracellular DNA has not been elucidated. In this study, we observed expedited enzymatic degradation of extracellular DNA in the presence of α-HCH, β-HCH and γ-HCH. The HCH-expedited DNA degradation was not due to increased deoxyribonuclease I (DNase I) activity. Our spectroscopic and computational results indicate that HCHs bound to DNA bases (most likely guanine) via Van der Waals forces and halogen bonds. This binding increased the helicity and accumulation of DNA base pairs, leading to a more compact DNA structure that exposed more sites susceptible to DNase I and thus expedited DNA degradation. This study provided insight into the genotoxicity and ecotoxicity of pesticides and improved our understanding of DNA persistence in contaminated environments.

| S-EPMC6391446 | biostudies-other

Hydrolysis and enzymatic degradation of Novichok nerve agents.

Project description:Several parameters of the Novichok nerve agents A230, A232 and A234 were determined. Hydrolysis rates were approximately one to three orders of magnitude slower than G-type nerve agents and approximately zero to two orders of magnitude slower than V-type nerve agents. A230 was the most labile Novichok compound followed by A232 then A234. Activation energies (Ea) and frequency factors (A) were determined for all three compounds. The organophosphorus acid anhydrolase (OPAA) enzyme had catalytic efficiencies on the Novichok compounds ranging between 104 and 105 M-1 min-1 with the highest k cat/Km value for A230, then A232 and lastly, A234.

| S-EPMC7002793 | biostudies-literature

Mechanism of enzymatic degradation of beta-sheet crystals.

Project description:The anti-parallel beta pleated sheet is a fundamental secondary structure in proteins and a major component in silk fibers generated by silkworms and spiders, with a key role to stabilize these proteins via physical cross-links. Importantly, these beta-sheets are fully degradable and nontoxic structures in biology, in contrast for example to beta-amyloid structures formed in disease states. Thus, insight into mechanism of enzymatic degradation would be instructive as a route to elucidating differences among these stable yet different structural features in biological systems. We report on the mechanism of enzymatic degradation of anti-parallel beta pleated sheets with Bombyx mori silk structures, leading to fibrils and subsequently to nanofilaments (2nm thickness and 160nm length). These nanofilaments play a role as nucleators of the crystalline regions, an important feature of the system that can be exploited to design silk-based biomaterials with predictable biodegradability and mechanical properties. The potential toxicity of degradation products from these proteolytic enzymes was also assessed in vitro and no cell toxicity found in vitro for the protease found in vivo in the human body. The degradation mechanism of beta-sheet silk crystals provides additional insight into the significant differences in biological impact between the anti-parallel beta-sheet silk biomaterials reported in this work vs. amyloid structures in disease states, adding to prior descriptions of chemical and structural differences that are more extensively documented.

| S-EPMC2819634 | biostudies-literature

Xanthan: enzymatic degradation and novel perspectives of applications.

Project description:The extracellular heteropolysaccharide xanthan, synthesized by bacteria of the genus Xanthomonas, is widely used as a thickening and stabilizing agent across the food, cosmetic, and pharmaceutical sectors. Expanding the scope of its application, current efforts target the use of xanthan to develop innovative functional materials and products, such as edible films, eco-friendly oil surfactants, and biocompatible composites for tissue engineering. Xanthan-derived oligosaccharides are useful as nutritional supplements and plant defense elicitors. Development and processing of such new functional materials and products often necessitate tuning of xanthan properties through targeted structural modification. This task can be effectively carried out with the help of xanthan-specific enzymes. However, the complex molecular structure and intricate conformational behavior of xanthan create problems with its enzymatic hydrolysis or modification. This review summarizes and analyzes data concerning xanthan-degrading enzymes originating from microorganisms and microbial consortia, with a particular focus on the dependence of enzymatic activity on the structure and conformation of xanthan. Through a comparative study of xanthan-degrading pathways found within various bacterial classes, different microbial enzyme systems for xanthan utilization have been identified. The characterization of these new enzymes opens new perspectives for modifying xanthan structure and developing innovative xanthan-based applications. KEY POINTS: • The structure and conformation of xanthan affect enzymatic degradation. • Microorganisms use diverse multienzyme systems for xanthan degradation. • Xanthan-specific enzymes can be used to develop xanthan variants for novel applications.

| S-EPMC10881899 | biostudies-literature

Enzymatic degradation of cellulose in soil: A review.

Project description:Cellulose degradation is a critical process in soil ecosystems, playing a vital role in nutrient cycling and organic matter decomposition. Enzymatic degradation of cellulosic biomass is the most sustainable and green method of producing liquid biofuel. It has gained intensive research interest with future perspective as the majority of terrestrial lignocellulose biomass has a great potential to be used as a source of bioenergy. However, the recalcitrant nature of lignocellulose limits its use as a source of energy. Noteworthy enough, enzymatic conversion of cellulose biomass could be a leading future technology. Fungal enzymes play a central role in cellulose degradation. Our understanding of fungal cellulases has substantially redirected in the past few years with the discovery of a new class of enzymes and Cellulosome. Efforts have been made from time to time to develop an economically viable method of cellulose degradation. This review provides insights into the current state of knowledge regarding cellulose degradation in soil and identifies areas where further research is needed.

| S-EPMC10792583 | biostudies-literature

UV Pretreatment Impairs the Enzymatic Degradation of Polyethylene Terephthalate.

Project description:The biocatalytic degradation of polyethylene terephthalate (PET) emerged recently as a promising alternative plastic recycling method. However, limited activity of previously known enzymes against post-consumer PET materials still prevents the application on an industrial scale. In this study, the influence of ultraviolet (UV) irradiation as a potential pretreatment method for the enzymatic degradation of PET was investigated. Attenuated total reflection Fourier transform infrared (ATR-FTIR) and 1H solution nuclear magnetic resonance (NMR) analysis indicated a shortening of the polymer chains of UV-treated PET due to intra-chain scissions. The degradation of UV-treated PET films by a polyester hydrolase resulted in significantly lower weight losses compared to the untreated sample. We also examined site-specific and segmental chain dynamics over a time scale of sub-microseconds to seconds using centerband-only detection of exchange, rotating-frame spin-lattice relaxation (T 1 ? ), and dipolar chemical shift correlation experiments which revealed an overall increase in the chain rigidity of the UV-treated sample. The observed dynamic changes are most likely associated with the increased crystallinity of the surface, where a decreased accessibility for the enzyme-catalyzed hydrolysis was found. Moreover, our NMR study provided further knowledge on how polymer chain conformation and dynamics of PET can mechanistically influence the enzymatic degradation.

| S-EPMC7199389 | biostudies-literature

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