Conversion of the Cleavage Specificity of Subtilisin YaB on Oxidized Insulin Chains to an Elastase-like Specificity by Replacement of Gly124 with Ala

2003 ◽  
Vol 67 (7) ◽  
pp. 1601-1604
Author(s):  
Hui-Ching MEI ◽  
Ywan-Feng LI ◽  
Chi-Cheng HSU ◽  
Ying-Chieh TSAI ◽  
Hiroshi TAKAGI
Keyword(s):  
Cleavage Specificity ◽  
Insulin Chains

Cleavage Specificity of Human Rhinovirus-2 2A Protease for Peptide Substrates

1997 ◽  
Vol 235 (3) ◽  
pp. 562-566 ◽  
Author(s):  
Q.May Wang ◽  
Wolfgang Sommergruber ◽  
Robert B. Johnson
Keyword(s):  
Human Rhinovirus ◽  
Peptide Substrates ◽  
Cleavage Specificity ◽  
2A Protease

Combination of insulin chains on an anti-insulin antibody–Sepharose column

Nature ◽  
1976 ◽  
Vol 262 (5571) ◽  
pp. 791-793 ◽  
Author(s):  
MECHTHILD KLOTZ ◽  
BERND GUTTE
Keyword(s):  
Insulin Antibody ◽  
Sepharose Column ◽  
Insulin Chains

scholarly journals Improvement of the glycoproteomic toolbox with the discovery of a unique C-terminal cleavage specificity of flavastacin for N-glycosylated asparagine

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Alexander Pralow ◽  
Marcus Hoffmann ◽  
Terry Nguyen-Khuong ◽  
Erdmann Rapp ◽  
Udo Reichl
Keyword(s):  
Cleavage Specificity

scholarly journals Active Site Mutations Change the Cleavage Specificity of Neprilysin

PLoS ONE ◽  
2012 ◽  
Vol 7 (2) ◽  
pp. e32343 ◽  
Author(s):  
Travis Sexton ◽  
Lisa J. Hitchcook ◽  
David W. Rodgers ◽  
Luke H. Bradley ◽  
Louis B. Hersh
Keyword(s):  
Active Site ◽  
Cleavage Specificity ◽  
Active Site Mutations

scholarly journals Substrate determinants in the C99 juxtamembrane domains differentially affect γ-secretase cleavage specificity and modulator pharmacology

2013 ◽  
Vol 125 (4) ◽  
pp. 610-619 ◽  
Author(s):  
Solenne Ousson ◽  
Arman Saric ◽  
Aurelie Baguet ◽  
Christophe Losberger ◽  
Stephane Genoud ◽  
...  
Keyword(s):  
Cleavage Specificity

scholarly journals Efficient Generation of a Hepatitis B Virus Cytotoxic T Lymphocyte Epitope Requires the Structural Features of Immunoproteasomes

2000 ◽  
Vol 191 (3) ◽  
pp. 503-514 ◽  
Author(s):  
Alice J.A.M. Sijts ◽  
Thomas Ruppert ◽  
Barbara Rehermann ◽  
Marion Schmidt ◽  
Ulrich Koszinowski ◽  
...  
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
T Lymphocyte ◽  
Cytotoxic T Lymphocyte ◽  
Structural Features ◽  
Core Antigen ◽  
Ctl Epitope ◽  
Cleavage Specificity ◽  
B Virus ◽  
Ifn Γ

Interferon (IFN)-γ–induced cells express the proteasome subunits low molecular weight protein (LMP)2, LMP7, and MECL-1 (multicatalytic endopeptidase complex–like 1), leading to the formation of immunoproteasomes. Although these subunits are thought to optimize MHC class I antigen processing, the extent of their role and the mechanistic aspects involved remain unclear. Herein, we study the proteolytic generation of an human histocompatibility leukocyte antigen (HLA)-Aw68–restricted hepatitis B virus core antigen (HBcAg) cytotoxic T lymphocyte (CTL) epitope that is recognized by peripheral blood lymphocytes from patients with acute self-limited but not chronic hepatitis B virus (HBV). Immunological data suggest that IFN-γ–induced rather than uninduced HeLa cells process and present the HBV CTL epitope upon infection with HBcAg-expressing vaccinia viruses. Analyses of 20S proteasome digests of synthetic polypeptides covering the antigenic HBcAg peptide demonstrate that only immunoproteasomes efficiently perform the cleavages needed for the liberation of this HBV CTL epitope. Although the concerted presence of the three immunosubunits appears essential, we find that both catalytically active LMP7 and inactive LMP7 T1A support CTL epitope generation. We conclude that LMP7 influences the structural features of 20S proteasomes, thereby enhancing the activity of the LMP2 and MECL-1 catalytic sites, which provide cleavage specificity. Thus, LMP7 incorporation is of greater functional importance for the generation of an HBV CTL epitope than cleavage specificity.

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