Analysis of acetohydroxyacid synthase1 gene in chickpea conferring resistance to imazamox herbicide

Genome ◽  
2014 ◽  
Vol 57 (11/12) ◽  
pp. 593-600 ◽  
Author(s):  
Parul Jain ◽  
Bunyamin Tar’an
Keyword(s):  
Enzyme Activity ◽  
Weed Management ◽  
Ligand Docking ◽  
Treatment Results ◽  
Enzyme Activity Assay ◽  
Canadian Prairies ◽  
Docking Analysis ◽  
Hydrophobic Cluster Analysis ◽  
Competition Ability ◽  
Resistant Genotypes

Chickpea (Cicer arietinum L.) production in the Canadian prairies is challenging due to a lack of effective weed management mainly because of poor competition ability of the crop and limited registered herbicide options. Chickpea genotype with resistance to imidazolinone (IMI) herbicides has been identified. A point mutation in the acetohydroxyacid synthase1 (AHAS1) gene at C581 to T581, resulting in an amino acid substitution from Ala194 to Val194 (position 205, standardized to arabidopsis), confers the resistance to imazamox in chickpea. However, the molecular mechanism leading to the resistance is not fully understood. In many plant species, contrasting transcription levels of AHAS gene has been implicated in the resistant and susceptible genotypes in response to IMI. The objectives of this research were to compare the AHAS gene expression and AHAS enzyme activity in resistant and susceptible chickpea cultivars in response to imazamox herbicide treatment. Results from RT–qPCR indicated that there is no significant change in the transcript levels of AHAS1 between the susceptible and the resistant genotypes in response to imazamox treatment. Protein hydrophobic cluster analysis, protein-ligand docking analysis, and AHAS enzyme activity assay all indicated that the resistance to imazamox in chickpea is due to the alteration of interaction of the AHAS1 enzyme with the imazamox herbicide.

Expression and Enzyme Activity Assay of pfu with Molecular Chaperone

2010 ◽  
Vol 31 (6) ◽  
pp. 499-503
Author(s):  
Hai-Jun ZHANG ◽  
Jun YANG ◽  
Xiao-Guang LIU ◽  
Xiang-Yang HU
Keyword(s):  
Enzyme Activity ◽  
Molecular Chaperone ◽  
Activity Assay ◽  
Enzyme Activity Assay

Antibacterial Flavonoids Against Oral Bacteria of Enterococcus Faecalis ATCC 29212 from Sarang Semut (Myrmecodia pendans) and Its Inhibitor Activity Against Enzyme MurA

2019 ◽  
Vol 16 (3) ◽  
pp. 290-296 ◽  
Author(s):  
Dikdik Kurnia ◽  
Eti Apriyanti ◽  
Cut Soraya ◽  
Mieke H. Satari
Keyword(s):  
Enzyme Activity ◽  
Enterococcus Faecalis ◽  
Ethyl Acetate Fraction ◽  
Antibacterial Activities ◽  
Oral Bacteria ◽  
Diffusion Method ◽  
Enzyme Activity Assay ◽  
Antibacterial Compounds ◽  
Ic50 Values ◽  
Positive Controls

Background: A significant number of antibiotics are known to inhibit peptidoglycan synthesis in the cross-linking stage, while the drug fosfomycin is the only one known to inhibit MurA. Escalated antibiotic resistance has had an impact on the efficacy of fosfomycin, thus demanding the discovery of suitable substitutes with improved potential for MurA inhibition. The aim of this work is to isolate antibacterial compounds from Sarang Semut (Myrmecodia pendans) and to evaluate their antibacterial activity against pathogenic oral bacteria of Enterococcus faecalis ATCC 29212 and inhibitory activity against MurA enzyme. Methods: The antibacterial compounds from Sarang Semut were isolated by a bioactivity-guided separation method with various solvents and combination of column chromatography on normal and reverse phases. The compounds with concentrations of 1000 and 5000 ppm were assessed against E. faecalis ATCC 29212 by agar well diffusion method, with chlorhexidine and fosfomycin being used as positive controls. Results: Two antibacterial compounds isolated from Sarang Semut were identified as two new flavonoids derivates of 1 (10 mg) and 2 (4 mg). Both compounds were tested for antibacterial activities against E. faecalis. MIC values of compounds 1 and 2 were 8.15 and 8.05 mm at 1000 ppm and 8.62 and 8.55 mm at 5000 ppm, respectively. MBC values were 156 and 625 ppm for 1 and 625 and 2500 ppm for 2, respectively. In an inhibitory murA enzyme activity assay, compounds 1 and 2 were shown to inhibit the enzyme activity by IC50 values of 21.7 and 151.3 ppm. Conclusion: The study demonstrated that ethyl acetate fraction of Sarang Semut contained antibacterial flavonoids as active constituents that showed activity against E. faecalis. These results showed the plant’s potential in herbal medicine and the development of new antibacterial agent for pathogenic dental caries.

Effect of nitric oxide on Sertoli cell microtubule of piglets

2009 ◽  
Vol 6 (3) ◽  
pp. 257-263 ◽  
Author(s):  
Yang Li ◽  
Wang Xian-zhong ◽  
Yang Meng-bo ◽  
Zhang Jia-hua
Keyword(s):  
Nitric Oxide ◽  
Enzyme Activity ◽  
Protein Kinase ◽  
Cell Viability ◽  
Sodium Nitroprusside ◽  
Sertoli Cell ◽  
Sertoli Cells ◽  
High Concentration ◽  
Treatment Results ◽  
Anti Oxidant

AbstractTo illustrate the effect of nitric oxide (NO) on the microtubules of Sertoli cells (SC), SCs of piglets were treated with sodium nitroprusside (SNP). Changes in cell viability, anti-oxidant activity, enzyme activity and p38 mutagen-activated protein kinase (p38MAPK) activation were detected. The results were as follows. A low concentration of NO can keep SC microtubule and cell viability normal, and a high concentration of NO could increase p38MAPK activation, decrease anti-oxidant activity and transferrin secretion, and destroy the structure and distribution of the microtubules. The results suggest that SNP treatment results in an increase in NO in SCs and decreased cell anti-oxidant activity. The high concentration of NO destroys cell microtubules by activating p38MAPK.

scholarly journals Structural and biochemical characterization of bifunctional XynA

2020 ◽  
Author(s):  
Wei Xie ◽  
Qi Yu ◽  
Yun Liu ◽  
Ruoting Cao ◽  
Ruiqing Zhang ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Enzyme Activity ◽  
Catalytic Mechanism ◽  
Biochemical Characterization ◽  
Cellulase Activity ◽  
Cost Savings ◽  
Site Directed Mutagenesis ◽  
Enzyme Activity Assay ◽  
Great Cost ◽  
Terminal Domain

AbstractXylan and cellulose are the two major constituents in numerous types of lignocellulosic biomass, representing a promising resource for biofuels and other biobased industries. The efficient degradation of lignocellulose requires the synergistic actions of cellulase and xylanase. Thus, bifunctional enzyme incorporated xylanase/cellulase activity has attracted considerable attention since it has great cost savings potential. Recently, a novel GH10 family enzyme XynA identified from Bacillus sp. is found to degrade both cellulose and xylan. To understand its molecular catalytic mechanism, here we first solve the crystal structure of XynA at 2.3 Å. XynA is characterized with a classic (α/β)8 TIM-barrel fold (GH10 domain) flanked by the flexible N-terminal domain and C-terminal domain. Circular dichroism, protein thermal shift and enzyme activity assays reveal that conserved residues Glu182 and Glu280 are both important for catalytic activities of XynA, which is verified by the crystal structure of XynA with E182A/E280A double mutant. Molecular docking studies of XynA with xylohexaose and cellohexaose as well as site-directed mutagenesis and enzyme activity assay demonstrat that Gln250 and His252 are indispensible to cellulase and bifunctional activity, separately. These results elucidate the structural and biochemical features of XynA, providing clues for further modification of XynA for industrial application.

Impact of enzyme activity assay on indication in liver transplantation for ornithine transcarbamylase deficiency

2012 ◽  
Vol 105 (3) ◽  
pp. 404-407 ◽  
Author(s):  
Taiichi Wakiya ◽  
Yukihiro Sanada ◽  
Taizen Urahashi ◽  
Yoshiyuki Ihara ◽  
Naoya Yamada ◽  
...  
Keyword(s):  
Liver Transplantation ◽  
Enzyme Activity ◽  
Ornithine Transcarbamylase ◽  
Ornithine Transcarbamylase Deficiency ◽  
Activity Assay ◽  
Enzyme Activity Assay

Resistance in Smallflower Umbrella Sedge (Cyperus difformis L.) to Acetolactate Synthase-Inhibiting Herbicides in Rice - First Case in India

2021 ◽  
pp. 1-22
Author(s):  
Vijay K. Choudhary ◽  
Seshadri S. Reddy ◽  
Subhash K. Mishra ◽  
Bhumesh Kumar ◽  
Yogita Gharde ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Acetolactate Synthase ◽  
Activity Assay ◽  
Enzyme Activity Assay ◽  
Synthetic Auxin ◽  
Cyperus Difformis ◽  
First Case ◽  
Whole Plant ◽  
Plant Bioassay ◽  
Direct Seeded

Abstract Smallflower umbrella sedge is one of the problematic weeds in direct-seeded rice in India. Bispyribac-sodium (acetolactate synthase-inhibiting herbicide) is a commonly used in rice, but recently growers have reported lack of smallflower umbrella sedge control with this herbicide. An extensive survey was carried out in two rice growing states, Chhattisgarh and Kerala, where 53 putative bispyribac-sodium resistant (BR) biotypes were collected. Studies were conducted to confirm resistance to bispyribac-sodium and to test the efficacy of newly developed synthetic auxin herbicide florpyrauxifen-benzyl on putative BR biotypes. Whole-plant bioassay revealed that bispyribac-sodium is no longer effective. Of 53 putative BR biotypes, 17 biotypes survived recommended label rate of 25 g ai ha−1. Effective bispyribac-sodium rate required to control 50% of the plants in most of the BR biotypes (ED50) ranged from 19 to 96 g ha−1 whereas it was 10 g ha−1 in susceptible biotype. In two highly resistant biotypes, ED50 was beyond the maximum tested rate, 200 g ha−1. This suggests 2 to >20-fold resistance in BR biotypes. Acetolactate synthase (ALS) enzyme activity assay suggests altered target site as mechanism of resistance to bispyribac-sodium. This study confirms the first case of evolved resistance in smallflower umbrella sedge for bispyribac-sodium in India. However, the newly developed synthetic auxin, florpyrauxifen-benzyl effectively controlled all BR biotypes at the field use rate 31.25 g ae ha−1.

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