Identification and magnetic immobilization of a pyrophilous aspartic protease from Antarctic psychrophilic fungus

2018 ◽  
Vol 42 (6) ◽  
pp. e12691 ◽  
Author(s):  
Bei Gao ◽  
Lei He ◽  
Dongzhi Wei ◽  
Lujia Zhang
Keyword(s):  
Aspartic Protease ◽  
Psychrophilic Fungus ◽  
Magnetic Immobilization

Memapsin 2, a drug target for Alzheimer's disease

2003 ◽  
Vol 70 ◽  
pp. 213-220 ◽  
Author(s):  
Gerald Koelsch ◽  
Robert T. Turner ◽  
Lin Hong ◽  
Arun K. Ghosh ◽  
Jordan Tang
Keyword(s):  
Crystal Structure ◽  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Transition State ◽  
Amyloid Precursor Protein ◽  
Therapeutic Target ◽  
Drug Target ◽  
Aspartic Protease ◽  
Precursor Protein ◽  
Memapsin 2

Mempasin 2, a ϐ-secretase, is the membrane-anchored aspartic protease that initiates the cleavage of amyloid precursor protein leading to the production of ϐ-amyloid and the onset of Alzheimer's disease. Thus memapsin 2 is a major therapeutic target for the development of inhibitor drugs for the disease. Many biochemical tools, such as the specificity and crystal structure, have been established and have led to the design of potent and relatively small transition-state inhibitors. Although developing a clinically viable mempasin 2 inhibitor remains challenging, progress to date renders hope that memapsin 2 inhibitors may ultimately be useful for therapeutic reduction of ϐ-amyloid.

Isolation and characterization of an Aspartic Protease from Salpichroa origanifolia Fruits

2015 ◽  
Vol 22 (4) ◽  
pp. 379-390 ◽  
Author(s):  
Gabriela Rocha ◽  
W. Obregon ◽  
Fernando Munoz ◽  
M. Guevara ◽  
Graciela Fernandez ◽  
...  
Keyword(s):  
Aspartic Protease ◽  
Isolation And Characterization

Mucor strictus Hagem, a psychrophilic fungus, andMucor falcatus sp.n.

1967 ◽  
Vol 33 (1) ◽  
pp. 189-195 ◽  
Author(s):  
Maria A. A. Schipper
Keyword(s):  
Psychrophilic Fungus

Kinetic and thermodynamic study of aspartic protease extracted from Withania Coagulans

2020 ◽  
pp. 104960
Author(s):  
Salman Ahmadi ◽  
Mahmoud Salehi ◽  
Solmaz Ausi
Keyword(s):  
Aspartic Protease ◽  
Thermodynamic Study ◽  
Withania Coagulans ◽  
Kinetic And Thermodynamic Study

Genome-wide identification of the aspartic protease gene family and their response under powdery mildew stress in wheat

2020 ◽  
Vol 47 (11) ◽  
pp. 8949-8961
Author(s):  
Yanlin Yang ◽  
Deshun Feng
Keyword(s):  
Powdery Mildew ◽  
Gene Family ◽  
Aspartic Protease ◽  
Protease Gene ◽  
Genome Wide

Structure-Based Design of Inhibitors of the Aspartic Protease Endothiapepsin by Exploiting Dynamic Combinatorial Chemistry

2014 ◽  
Vol 53 (12) ◽  
pp. 3259-3263 ◽  
Author(s):  
Milon Mondal ◽  
Nedyalka Radeva ◽  
Helene Köster ◽  
Ahyoung Park ◽  
Constantinos Potamitis ◽  
...  
Keyword(s):  
Combinatorial Chemistry ◽  
Aspartic Protease ◽  
Dynamic Combinatorial Chemistry

Structure-Based Design and Synthesis of Macroheterocyclic Peptidomimetic Inhibitors of the Aspartic Protease β-Site Amyloid Precursor Protein Cleaving Enzyme (BACE)

2006 ◽  
Vol 49 (15) ◽  
pp. 4544-4567 ◽  
Author(s):  
Stephen Hanessian ◽  
Gaoqiang Yang ◽  
Jean-Michel Rondeau ◽  
Ulf Neumann ◽  
Claudia Betschart ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Aspartic Protease ◽  
Precursor Protein ◽  
Design And Synthesis ◽  
Peptidomimetic Inhibitors

Polygalacturonase isolated from the culture of the psychrophilic fungus Sclerotinia borealis

1997 ◽  
Vol 43 (5) ◽  
pp. 417-424 ◽  
Author(s):  
Toshihide Takasawa ◽  
Keiko Sagisaka ◽  
Koichi Yagi ◽  
Kyoko Uchiyama ◽  
Atsushi Aoki ◽  
...  
Keyword(s):  
Culture Medium ◽  
Enzyme Reaction ◽  
Wheat Seedling ◽  
Maximum Activity ◽  
Reducing Sugar ◽  
Pectic Acid ◽  
Snow Mold ◽  
Viscosity Change ◽  
Optimum Ph ◽  
Psychrophilic Fungus

A polygalacturonase was isolated from the culture medium of Sclerotinia borealis, a psychrophilic fungus that grows on lawn and wheat seedling under the snow in winter and induces the snow mold disease. Pectic acid was a better substrate of this enzyme than pectin when the activity was determined by measuring the reducing sugar produced. However, when the activity was measured by viscosity change, the viscosity of pectin decreased more rapidly than that of pectic acid. The results of viscosity change apparently indicate that the polygalacturonase catalyzes pectin hydrolysis as an endo-type enzyme. Highly methyl-esterified pectin was a poor substrate, as determined by measurements of reducing sugar production and viscosity change. It is suggested from the results that the methoxy group of pectin affects the polygalacturonase reaction. A reaction mechanism was proposed for the polygalacturonase reaction. Molecular mass of this enzyme was 40 kDa and its isoelectric point was pH 7.5. Optimum pH of the enzyme reaction was 4.5 and its optimum temperature was 40–50 °C. Thirty percent of the maximum activity was observed at 5 °C, but it was only slightly active above 60 °C. The activity was preserved for more than 2 years at 5 °C and pH 4.5, but it was lost when kept at room temperature overnight or heated at 50 °C for 30 min. The amino acid sequence of the N-terminal region of the psychrophilic polygalacturonase of Sclerotinia borealis is compared with those of polygalacturonases of mesophilic fungi. The function of this enzyme against the target plants is discussed with reference to the reaction of polygalacturonases of mesophilic fungi.Key words: polygalacturonase, pectin-hydrolyzing enzyme, psychrophilic fungi, snow mold disease, Sclerotinia borealis.

Additional interaction of allophenylnorstatine-containing tripeptidomimetics with malarial aspartic protease plasmepsin II

2007 ◽  
Vol 17 (11) ◽  
pp. 3048-3052 ◽  
Author(s):  
Koushi Hidaka ◽  
Tooru Kimura ◽  
Yumi Tsuchiya ◽  
Mami Kamiya ◽  
Adam J. Ruben ◽  
...  
Keyword(s):  
Aspartic Protease ◽  
Plasmepsin Ii ◽  
Additional Interaction
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