scholarly journals On the role of protein structural dynamics in the catalytic activity and thermostability of serine protease subtilisin Carlsberg

2009 ◽  
Vol 103 (1) ◽  
pp. 77-84 ◽  
Author(s):  
Miraida Pagán ◽  
Ricardo J. Solá ◽  
Kai Griebenow
Keyword(s):  
Catalytic Activity ◽  
Serine Protease ◽  
Structural Dynamics ◽  
Subtilisin Carlsberg ◽  
Protein Structural Dynamics

scholarly journals Lopap, a prothrombin activator from Lonomia obliqua belonging to the lipocalin family: recombinant production, biochemical characterization and structure–function insights

2006 ◽  
Vol 398 (2) ◽  
pp. 295-302 ◽  
Author(s):  
Cleyson Valença Reis ◽  
Sonia Aparecida Andrade ◽  
Oscar Henrique Pereira Ramos ◽  
Celso Raul Romero Ramos ◽  
Paulo Lee Ho ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Serine Protease ◽  
Calcium Binding ◽  
Biochemical Characterization ◽  
Structural Features ◽  
Reading Frame ◽  
Molecular Features ◽  
Recombinant Production ◽  
Lonomia Obliqua

Using a cDNA library made from Lonomia obliqua caterpillar bristles, we identified a transcript with a 603 bp open reading frame. The deduced protein corresponds to Lopap, a prothrombin activator previously isolated by our group from the bristles of this species. The mature protein is composed by 185 amino acids and shares similarity with members of the lipocalin family. The cDNA encoding the mature form was amplified by PCR, subcloned into pAE vector and used to transform Escherichia coli BL21(DE3) cells. As for the native Lopap, the recombinant fusion protein shows enzymatic activity, promotes prothrombin hydrolysis, generates fragments similar to prethrombin-2 and fragment 1.2 as intermediates, and generates thrombin as the final product. In addition, structural bioinformatics studies indicated several interesting molecular features, including the residues that could be responsible for Lopap's serine protease-like activity and the role of calcium binding in this context. Such catalytic activity has never been found in other members of the lipocalin family. This is the first report describing the recombinant production and biochemical characterization of a Lonomia obliqua lipocalin, as well as the structural features that could be responsible for its serine protease-like catalytic activity.

scholarly journals Examining the role of protein structural dynamics in drug resistance in Mycobacterium tuberculosis

2017 ◽  
Vol 8 (12) ◽  
pp. 8384-8399 ◽  
Author(s):  
Daniel J. Shaw ◽  
Rachel E. Hill ◽  
Niall Simpson ◽  
Fouad S. Husseini ◽  
Kirsty Robb ◽  
...  
Keyword(s):  
Drug Resistance ◽  
Mycobacterium Tuberculosis ◽  
Antimicrobial Resistance ◽  
Ir Spectroscopy ◽  
Structural Dynamics ◽  
2D Ir ◽  
Protein Structural Dynamics

2D-IR spectroscopy reveals a role for protein structural dynamics in antimicrobial-resistance.

scholarly journals Myelin Basic Protein dynamics from out-of-equilibrium functional state to degraded state in myelin

2019 ◽  
Author(s):  
M. Di Gioacchino ◽  
A. Bianconi ◽  
M. Burghammer ◽  
G. Ciasca ◽  
F. Bruni ◽  
...  
Keyword(s):  
Myelin Basic Protein ◽  
Protein Dynamics ◽  
Functional State ◽  
Structural Dynamics ◽  
Basic Protein ◽  
Physiological State ◽  
X Ray ◽  
Intrinsically Disordered ◽  
Protein Structural Dynamics

ABSTRACTLiving matter is a quasi-stationary out-of-equilibrium system; in this physical condition, structural fluctuations at nano- and meso-scales are needed to understand the physics behind its biological functionality. Myelin has a simple ultrastructure whose fluctuations show correlated disorder in its functional out-of-equilibrium state. However, there is no information on the relationship between this correlated disorder and the dynamics of the intrinsically disordered Myelin Basic Protein (MBP) which is expected to influence the membrane structure and overall functionality. In this work, we have investigated the role of this protein structural dynamics in the myelin ultrastructure fluctuations in and out-of-equilibrium conditions, by using synchrotron Scanning micro X Ray Diffraction and Small Angle X ray Scattering. We have induced the crossover from out-of-equilibrium functional state to in-equilibrium degeneration changing the pH far away from physiological condition. While the observed compression of the cytosolic layer thickness probes the unfolding of the P2 protein and of the cytoplasmic P0 domain (P0cyt), the intrinsic large MBP fluctuations preserve the cytosol structure also in the degraded state. Thus, the transition of myelin ultrastructure from correlated to uncorrelated disordered state, is significantly affected by the unfolding of the P2 and P0 proteins, which in this latter state do not act in synergistic manner with MBP to determine the membrane functionality.STATEMENT OF SIGNIFICANCEA better comprehension of myelin degenerative process and the role of protein dynamics in this biological membrane is a topic issue in today’s scientific community. The myelin ultrastructural fluctuations exhibit correlated disorder in its functional state, that becomes uncorrelated as it degenerates. In this work we elucidate the interplay of protein structural dynamics and myelin ultrastructure in the transition from its functional state to the degraded state. The results highlight that the intrinsically disordered Myelin Basic Protein (MBP) allows to preserve the myelin structure following both the small correlated fluctuations in physiological state and the large disordered fluctuations in degraded conditions, where the myelin functionality is close to being lost and the MBP remains the single active protein.

Correction: Structural modeling and role of HAX-1 as a positive allosteric modulator of human serine protease HtrA2

2020 ◽  
Vol 477 (2) ◽  
pp. 459-459
Author(s):  
Lalith K. Chaganti ◽  
Shubhankar Dutta ◽  
Raja Reddy Kuppili ◽  
Mriganka Mandal ◽  
Kakoli Bose
Keyword(s):  
Serine Protease ◽  
Structural Modeling ◽  
Allosteric Modulator ◽  
Positive Allosteric Modulator

Catalytic Activity of Binary and Triple Systems Based on Redox Inactive Metal Compound, LiSt and Additives of Monodentate Ligands-Modifiers: DMF, HMPA and PhOH, in Selective Ethylbenzene Oxidation with Dioxygen

2016 ◽  
Vol 10 (3) ◽  
pp. 259-270
Author(s):  
Ludmila Matienko ◽  
◽  
Larisa Mosolova ◽  
Vladimir Binyukov ◽  
Gennady Zaikov ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Triple System ◽  
Metal Compound ◽  
Ethylbenzene Oxidation ◽  
Catalytic Systems ◽  
Triple Systems ◽  
Lithium Compound ◽  
Mechanism Of Catalysis ◽  
Monodentate Ligands

Mechanism of catalysis with binary and triple catalytic systems based on redox inactive metal (lithium) compound {LiSt+L2} and {LiSt+L2+PhOH} (L2=DMF or HMPA), in the selective ethylbenzene oxidation by dioxygen into -phenylethyl hydroperoxide is researched. The results are compared with catalysis by nickel-lithium triple system {NiII(acac)2+LiSt+PhOH} in selective ethylbenzene oxidation to PEH. The role of H-bonding in mechanism of catalysis is discussed. The possibility of the stable supramolecular nanostructures formation on the basis of triple systems, {LiSt+L2+PhOH}, due to intermolecular H-bonds, is researched with the AFM method.

scholarly journals Carbohydrate-controlled serine protease inhibitor (serpin) production in Bifidobacterium longum subsp. longum

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
S. Duboux ◽  
M. Golliard ◽  
J. A. Muller ◽  
G. Bergonzelli ◽  
C. J. Bolten ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Serine Protease ◽  
Serine Proteases ◽  
Intestinal Tract ◽  
Defense Mechanism ◽  
Inflammatory Diseases ◽  
Bifidobacterium Longum ◽  
Serine Protease Inhibitor ◽  
Innate Defense

AbstractThe Serine Protease Inhibitor (serpin) protein has been suggested to play a key role in the interaction of bifidobacteria with the host. By inhibiting intestinal serine proteases, it might allow bifidobacteria to reside in specific gut niches. In inflammatory diseases where serine proteases contribute to the innate defense mechanism of the host, serpin may dampen the damaging effects of inflammation. In view of the beneficial roles of this protein, it is important to understand how its production is regulated. Here we demonstrate that Bifidobacterium longum NCC 2705 serpin production is tightly regulated by carbohydrates. Galactose and fructose increase the production of this protein while glucose prevents it, suggesting the involvement of catabolite repression. We identified that di- and oligosaccharides containing galactose (GOS) and fructose (FOS) moieties, including the human milk oligosaccharide Lacto-N-tetraose (LNT), are able to activate serpin production. Moreover, we show that the carbohydrate mediated regulation is conserved within B. longum subsp. longum strains but not in other bifidobacterial taxons harboring the serpin coding gene, highlighting that the serpin regulation circuits are not only species- but also subspecies- specific. Our work demonstrates that environmental conditions can modulate expression of an important effector molecule of B. longum, having potential important implications for probiotic manufacturing and supporting the postulated role of serpin in the ability of bifidobacteria to colonize the intestinal tract.

scholarly journals Role of CO2 During Oxidative Dehydrogenation of Propane Over Bulk and Activated-Carbon Supported Cerium and Vanadium Based Catalysts

2021 ◽  
Author(s):  
Petar Djinović ◽  
Janez Zavašnik ◽  
Janvit Teržan ◽  
Ivan Jerman
Keyword(s):  
Catalytic Activity ◽  
Activated Carbon ◽  
Oxidative Dehydrogenation ◽  
Active Phase ◽  
Lattice Oxygen ◽  
Chemisorbed Oxygen ◽  
Catalytically Active ◽  
Temperature Programmed ◽  
Propane Cracking

AbstractCeO2, V2O5 and CeVO4 were synthesised as bulk oxides, or deposited over activated carbon, characterized by XRD, HRTEM, CO2-TPO, C3H8-TPR, DRIFTS and Raman techniques and tested in propane oxidative dehydrogenation using CO2. Complete oxidation of propane to CO and CO2 is favoured by lattice oxygen of CeO2. The temperature programmed experiments show the ~ 4 nm AC supported CeO2 crystallites become more susceptible to reduction by propane, but less prone to re-oxidation with CO2 compared to bulk CeO2. Catalytic activity of CeVO4/AC catalysts requires a 1–2 nm amorphous CeVO4 layer. During reaction, the amorphous CeVO4 layer crystallises and several atomic layers of carbon cover the CeVO4 surface, resulting in deactivation. During reaction, V2O5 is irreversibly reduced to V2O3. The lattice oxygen in bulk V2O5 favours catalytic activity and propene selectivity. Bulk V2O3 promotes only propane cracking with no propene selectivity. In VOx/AC materials, vanadium carbide is the catalytically active phase. Propane dehydrogenation over VC proceeds via chemisorbed oxygen species originating from the dissociated CO2. Graphic Abstract

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