Results 31 to 40 of about 2,773 (218)

The malaria parasite egress protease SUB1 is a calcium-dependent redox switch subtilisin. [PDF]

open access: yes, 2014
Malaria is caused by a protozoan parasite that replicates within an intraerythrocytic parasitophorous vacuole. Release (egress) of malaria merozoites from the host erythrocyte is a highly regulated and calcium-dependent event that is critical for disease
Blackman, Michael J   +8 more
core   +1 more source

Crystal structure of subtilisin DY, a random mutant of subtilisin Carlsberg [PDF]

open access: yesEuropean Journal of Biochemistry, 1998
The crystal structure of subtilisin DY inhibited by N‐benzyloxycarbonyl‐Ala‐Pro‐Phe‐chloromethyl ketone has been solved by molecular replacement with subtilisin Carlsberg as the starting model. The model has been refined to a crystallographic R factor (= Σ∣∣Fo∣−∣Fc∣∣ / Σ∣Fo∣) of 15.1 % using X‐ray diffraction data to 0.175 nm resolution.
S, Eschenburg   +6 more
openaire   +2 more sources

Revisiting Vitis vinifera subtilase gene family: a possible role in grapevine resistance against Plasmopara viticola

open access: yesFrontiers in Plant Science, 2016
Subtilisin-like proteases, also known as subtilases, are a very diverse family of serine peptidases present in many organisms. In grapevine, there are hints of the involvement of subtilases in defence mechanisms, but their role is not yet understood. The
Joana Figueiredo   +11 more
doaj   +1 more source

Leucoagaricus gongylophorus uses leaf-cutting ants to vector proteolytic enzymes towards new plant substrate [PDF]

open access: yes, 2014
The mutualism between leaf-cutting ants and their fungal symbionts revolves around processing and inoculation of fresh leaf pulp in underground fungus gardens, mediated by ant fecal fluid deposited on the newly added plant substrate.
Boomsma, Jacobus Jan   +5 more
core   +1 more source

Merging Biocatalysis and Chemocatalysis in Flow: State‐of‐the‐Art and Future Directions for Sustainable Synthesis

open access: yesAngewandte Chemie, EarlyView.
This review highlights recent advances in integrating biocatalysis and chemocatalysis in continuous flow to create streamlined, sustainable processes. It examines chemo‐enzymatic cascades combining at least one enzymatic and one chemical step, discusses challenges such as enzyme immobilization, leaching, and reactor clogging, and presents solutions ...
Petros Siasiaridis   +2 more
wiley   +2 more sources

Kinetic evidence for two different productive substrate binding sites in subtilisins [PDF]

open access: yes, 1973
Public data made available to citizens must meet certain characteristics to guarantee it can be easily reused to generate new information or services and, ultimately, to increase the transparency of public bodies.
Bosshard, Hans Rudolf
core   +3 more sources

Non-canonical proteolytic activation of human prothrombin by subtilisin from Bacillus subtilis may shift the procoagulant\ue2\u80\u93anticoagulant equilibrium toward thrombosis [PDF]

open access: yes, 2017
Blood coagulation is a finely regulated physiological process culminating with the factor Xa (FXa)-mediated conversion of the prothrombin (ProT) zymogen to active -thrombin (T).
Acquasaliente, Laura   +5 more
core   +1 more source

Restricting detergent protease action to surface of protein fibres by chemical modification [PDF]

open access: yes, 2006
Due to their excellent properties, such as thermostability, activity over a broad range of pH and efficient stain removal, proteases from Bacillus sp. are commonly used in the textile industry including industrial processes and laundry and represent ...
A Abuchowski   +33 more
core   +1 more source

The Structure of Subtilisin Novo

open access: yesJournal of Biological Chemistry, 1968
The amino acid composition of subtilisin Novo has been determined. The compositions of all of the 14 expected tryptic peptides from subtilisin Novo were obtained or deduced. A total of 281 residues was found by analysis of the protein, in good agreement with the total of 275 residues in the expected 14 tryptic peptides.
S A, Olaitan, R J, DeLange, E L, Smith
openaire   +2 more sources

Cross genome comparisons of serine proteases in Arabidopsis and rice

open access: yesBMC Genomics, 2006
Background Serine proteases are one of the largest groups of proteolytic enzymes found across all kingdoms of life and are associated with several essential physiological pathways.
Sowdhamini R, Tripathi Lokesh P
doaj   +1 more source

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