Breaking the Backbone: Central Arginine Residues Induce Membrane Exit and Helix Distortions within a Dynamic Membrane Peptide

Protein methylation is an important and reversible post-translational modification that regulates many biological processes in cells. It occurs mainly on lysine and arginine residues and involves many important biological processes, including transcriptional activity, signal transduction, and the regulation of gene expression. Protein methylation and its regulatory enzymes are related to a variety of human diseases, so improved identification of methylation sites is useful for designing drugs for a variety of related diseases. In this review, we systematically summarize and analyze the tools used for the prediction of protein methylation sites on arginine and lysine residues over the last decade.

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Functional characterization and structural modelling of peptidoglycan degrading β-N-acetyl-glucosaminidase from a dental isolate of Serratia marcescens

Combinatorial Chemistry & High Throughput Screening ◽

10.2174/1386207323999201103204234 ◽

2020 ◽

Vol 23 ◽

Author(s):

Aditi Rathee ◽

Anil Panwar ◽

Seema Kumari ◽

Sanjay Chhibber ◽

Ashok Kumar

Keyword(s):

Functional Characterization ◽

Major Change ◽

Crystal Form ◽

Bound State ◽

Dynamics Simulation ◽

Gram Positive ◽

Structural Cell ◽

Stability Structure ◽

Arginine Residues ◽

The Stability

Introduction:: Enzymatic degradation of peptidoglycan, a structural cell wall component of Gram-positive bacteria, has attracted considerable attention being a specific target for many known antibiotics. Methods:: Peptidoglycan hydrolases are involved in bacterial lysis through peptidoglycan degradation. β-N-acetylglucosaminidase, a peptidoglycan hydrolase, acts on O-glycosidic bonds formed by N-acetylglucosamine and N-acetyl muramic acid residues of peptidoglycan. Aim of present study was to study the action of β-N-acetylglucosaminidase, on methicillin- resistant Staphylococcus aureus (MRSA) and other Gram-negative bacteria. Results:: We investigated its dynamic behaviour using molecular dynamics simulation and observed that serine and alanine residues are involved in catalytic reaction in addition to aspartic acid, histidine, lysine and arginine residues. When simulated in its bound state, the RMSD values were found lesser than crystal form in the time stamp of 1000 picoseconds revealing its stability. Structure remained stably folded over 1000 picoseconds without undergoing any major change further confirming the stability of complex. Conclusion:: It can be concluded that enzymes belonging to this category can serve as a tool in eradicating Gram-positive pathogens and associated infections.

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Gas-lift anaerobic dynamic membrane bioreactors for high strength synthetic wastewater treatment: Effect of biogas sparging velocity and HRT on treatment performance

Chemical Engineering Journal ◽

10.1016/j.cej.2016.02.003 ◽

2016 ◽

Vol 305 ◽

pp. 46-53 ◽

Cited By ~ 30

Author(s):

Mustafa Evren Ersahin ◽

Juan B. Gimenez ◽

Hale Ozgun ◽

Yu Tao ◽

Henri Spanjers ◽

...

Keyword(s):

Wastewater Treatment ◽

Treatment Effect ◽

High Strength ◽

Membrane Bioreactors ◽

Synthetic Wastewater ◽

Dynamic Membrane ◽

Treatment Performance ◽

Gas Lift

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Arginine Residues at the Active Site of Avian Liver Phosphoenolpyruvate Carboxykinase

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)94068-8 ◽

1989 ◽

Vol 264 (6) ◽

pp. 3317-3324

Author(s):

K C Cheng ◽

T Nowak

Keyword(s):

Active Site ◽

Phosphoenolpyruvate Carboxykinase ◽

Arginine Residues

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Whole-body arginine dimethylation is associated with all-cause mortality in adult renal transplant recipients

Amino Acids ◽

10.1007/s00726-021-02965-1 ◽

2021 ◽

Author(s):

Adrian Post ◽

Alexander Bollenbach ◽

Stephan J. L. Bakker ◽

Dimitrios Tsikas

Keyword(s):

Renal Transplant ◽

Excretion Rate ◽

Whole Body ◽

Renal Transplant Recipients ◽

Transplant Recipients ◽

Kidney Donors ◽

Body Protein ◽

All Cause Mortality ◽

Arginine Residues ◽

Excretion Rates

AbstractArginine residues in proteins can be singly or doubly methylated post-translationally. Proteolysis of arginine-methylated proteins provides monomethyl arginine, asymmetric dimethylarginine (ADMA) and symmetric dimethylarginine (SDMA). ADMA and SDMA are considered cardiovascular risk factors, with the underlying mechanisms being not yet fully understood. SDMA lacks appreciable metabolism and is almost completely eliminated by the kidney, whereas ADMA is extensively metabolized to dimethylamine (DMA), with a minor ADMA fraction of about 10% being excreted unchanged in the urine. Urinary DMA and ADMA are useful measures of whole-body asymmetric arginine-dimethylation, while urinary SDMA serves as a whole-body measure of symmetric arginine-dimethylation. In renal transplant recipients (RTR), we previously found that higher plasma ADMA concentrations and lower urinary ADMA and SDMA concentrations were associated with a higher risk of all-cause mortality. Yet, in this RTR collective, no data were available for urinary DMA. For the present study, we additionally measured the excretion rate of DMA in 24-h collected urine samples of the RTR and of healthy kidney donors in the cohort, with the aim to quantitate whole-body asymmetric (ADMA, DMA) and symmetric (SDMA) arginine-dimethylation. We found that lower DMA excretion rates were associated with higher all-cause mortality, yet not with cardiovascular mortality. In the healthy donors, kidney donation was associated with considerable decreases in ADMA (by − 39%, P < 0.0001) and SDMA (by − 21%, P < 0.0001) excretion rates, yet there was no significant change in DMA (by − 9%, P = 0.226) excretion rate. Our results suggest that protein-arginine dimethylation is altered in RTR compared to healthy kidney donors and that it is pronouncedly shifted from symmetric to asymmetric arginine-dimethylation, with whole-body protein-arginine dimethylation being almost unaffected.

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