scholarly journals Stacking interactions of W271 and H275 of SeMV serine protease with W43 of natively unfolded VPg confer catalytic activity to protease

Virology ◽  
2008 ◽  
Vol 382 (1) ◽  
pp. 83-90 ◽  
Author(s):  
Smita Nair ◽  
P. Gayathri ◽  
M.R.N. Murthy ◽  
H.S. Savithri
Keyword(s):  
Catalytic Activity ◽  
Serine Protease ◽  
Stacking Interactions ◽  
Natively Unfolded

Engineering of serine protease for improved thermostability and catalytic activity using rational design

2019 ◽  
Vol 126 ◽  
pp. 229-237 ◽  
Author(s):  
Naeem Mahmood Ashraf ◽  
Akshaya Krishnagopal ◽  
Aadil Hussain ◽  
David Kastner ◽  
Ahmed Mahmoud Mohammed Sayed ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Serine Protease ◽  
Rational Design

scholarly journals “Natively Unfolded” VPg Is Essential forSesbaniaMosaic Virus Serine Protease Activity

2005 ◽  
Vol 280 (34) ◽  
pp. 30291-30300 ◽  
Author(s):  
Panayampalli Subbian Satheshkumar ◽  
Pananghat Gayathri ◽  
Kasaragod Prasad ◽  
Handanahal Subbarao Savithri
Keyword(s):  
Serine Protease ◽  
Protease Activity ◽  
Serine Protease Activity ◽  
Natively Unfolded

Evidence that a deferrioxamine B degrading enzyme is a serine protease

1998 ◽  
Vol 44 (6) ◽  
pp. 521-527 ◽  
Author(s):  
Ninef Zaya ◽  
Alexandra Roginsky ◽  
Jamila Williams ◽  
Domenic Castignetti
Keyword(s):  
Catalytic Activity ◽  
Serine Protease ◽  
Calcium Ions ◽  
Ferric Ion ◽  
Plant Interactions ◽  
Degrading Enzyme ◽  
Carbon And Nitrogen ◽  
Serine Peptidase ◽  
Deferrioxamine B ◽  
Low Concentrations

Siderophores are organic biomolecules synthesized by a wide variety of microbes. The molecules sequester ferric ion from environments where it is present at extremely low concentrations. Siderophores are of consequence with respect to microbial nutrition, pathogenicity, virulence, and microbe-plant interactions. How siderophores are degraded and returned to the carbon and nitrogen cycles is not well understood. The catalytic activity of an enzyme from a bacterium that degrades the siderophore deferrioxamine B has been examined. While the degradation of deferrioxamine B is sensitive to sulfhydryl and metal moiety inhibitors, the data presented is most consistent with the hypothesis that the enzyme uses a hydroxyl moiety (serine peptidase) to catalyze the degradation of deferrioxamine B. If sulfhydryl and metal inhibitors are simultaneously present at concentrations that when alone only partially inhibit the enzyme, the enzyme is unable to catalyze deferrioxamine B dissimilation. Analysis of the inhibitor experiments conducted led to the conclusion that the deferrioxamine B degrading enzyme is a serine-peptidase-like enzyme that needs calcium ions and sulfhydryl groups to be fully activated or stabilized. The knowledge of the catalytic moieties of the enzyme will be exploited to purify the enzyme.Key words: siderophores, deferrioxamine B, siderophore degradation.

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.

Design, synthesis and catalytic activity of a serine protease synthetic model

1997 ◽  
Vol 4 (4-6) ◽  
pp. 481-487 ◽  
Author(s):  
Athanassios Stavrakoudis ◽  
Ioannis N. Demetropoulos ◽  
Constantinos Sakarellos ◽  
Maria Sakarellos-Daitsiotis ◽  
Vassilios Tsikaris
Keyword(s):  
Catalytic Activity ◽  
Serine Protease ◽  
Design Synthesis ◽  
Synthetic Model

“In situ immobilization” of a multicomponent chiral catalyst (MCC) via non-covalent interactions for heterogeneous asymmetric hydrogenation reactions

2020 ◽  
Vol 7 (2) ◽  
pp. 345-349
Author(s):  
Er-Jun Hao ◽  
Gong-Xin Li ◽  
Zhen-Zhen Lv ◽  
Fu-Sheng Li ◽  
Yu-Qing Chen ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Asymmetric Hydrogenation ◽  
Stacking Interactions ◽  
In Situ Immobilization ◽  
Chiral Catalyst ◽  
Hydrogenation Reactions ◽  
Non Covalent Interactions ◽  
Dehydroamino Acid ◽  
Covalent Interactions

Novel hybrid catalysts that resulted from the anchoring of pyrene-tagged Rh(i) complexes onto graphene materials via π–π stacking interactions show excellent catalytic activity towards the hydrogenation of dehydroamino acid.

scholarly journals Targeting the Complement Serine Protease MASP-2 as a Therapeutic Strategy for Coronavirus Infections

Viruses ◽  
2021 ◽  
Vol 13 (2) ◽  
pp. 312
Author(s):  
Ben M. Flude ◽  
Giulio Nannetti ◽  
Paige Mitchell ◽  
Nina Compton ◽  
Chloe Richards ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Lung Injury ◽  
Serine Protease ◽  
Complement Activation ◽  
Lectin Pathway ◽  
Vitro Assay ◽  
Direct Inhibitors ◽  
N Proteins ◽  
Coronavirus Infections

MASP-2, mannose-binding protein-associated serine protease 2, is a key enzyme in the lectin pathway of complement activation. Hyperactivation of this protein by human coronaviruses SARS-CoV, MERS-CoV and SARS-CoV-2 has been found to contribute to aberrant complement activation in patients, leading to aggravated lung injury with potentially fatal consequences. This hyperactivation is triggered in the lungs through a conserved, direct interaction between MASP-2 and coronavirus nucleocapsid (N) proteins. Blocking this interaction with monoclonal antibodies and interfering directly with the catalytic activity of MASP-2, have been found to alleviate coronavirus-induced lung injury both in vitro and in vivo. In this study, a virtual library of 8736 licensed drugs and clinical agents has been screened in silico according to two parallel strategies. The first strategy aims at identifying direct inhibitors of MASP-2 catalytic activity, while the second strategy focusses on finding protein-protein interaction inhibitors (PPIs) of MASP-2 and coronaviral N proteins. Such agents could represent promising support treatment options to prevent lung injury and reduce mortality rates of infections caused by both present and future-emerging coronaviruses. Forty-six drug repurposing candidates were purchased and, for the ones selected as potential direct inhibitors of MASP-2, a preliminary in vitro assay was conducted to assess their interference with the lectin pathway of complement activation. Some of the tested agents displayed a dose-response inhibitory activity of the lectin pathway, potentially providing the basis for a viable support strategy to prevent the severe complications of coronavirus infections.

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