scholarly journals Ghrelin proteolysis by insulin-degrading enzyme

2021 ◽  
Author(s):  
David D. Bocach ◽  
Kierstin L. Jones ◽  
Jonathan M. Bell ◽  
Qiuchen Zheng ◽  
Noel D. Lazo ◽  
...  
Keyword(s):  
Kinetic Parameters ◽  
Chelating Agent ◽  
Target Sequence ◽  
Enzyme Specificity ◽  
Peptide Substrate ◽  
Recombinant Human Insulin ◽  
Insulin Degrading Enzyme ◽  
Degrading Enzyme ◽  
Fluorogenic Peptide Substrate ◽  
Fluorogenic Peptide

Here we report proteolysis of synthetic acylated human ghrelin by recombinant human insulin-degrading enzyme (IDE). Kinetic parameters and sites of proteolytic cleavage were evaluated. Ghrelin proteolysis by IDE was inhibited by ethylenediaminetetraacetate (EDTA), a metal chelating agent. Ghrelin proteolysis appears at least somewhat specific to M16 family proteases such as IDE, as the M13 protease neprilysin (NEP) did not exhibit ghrelin proteolysis in this study. A quenched fluorogenic peptide substrate comprising the primary sites of IDE-mediated ghrelin proteolysis (Mca-QRVQQRKESKK(Dnp)-OH; Mca: 7-methoxycoumarin-3-carboxylic acid; Dnp: 2,4-dinitrophenyl) was developed and used to evaluate enzyme specificity and kinetic parameters of proteolysis. Like acyl ghrelin, Mca-QRVQQRKESKK(Dnp)-OH was efficiently cleaved by IDE central to the target sequence. We anticipate that this quenched fluorogenic peptide substrate will be of value to future studies of ghrelin proteolysis by IDE and potentially other peptidases.

A New fluorogenic Peptide Substrate for Vitamin K-Dependent Blood Coagulation Factor, Bovine Protein C1

1981 ◽  
Vol 90 (5) ◽  
pp. 1387-1395 ◽  
Author(s):  
Yasuo OHNO ◽  
Hisao KATO ◽  
Takashi MORITA ◽  
Sadaaki IWANAGA ◽  
Katsumi TAKADA ◽  
...  
Keyword(s):  
Blood Coagulation ◽  
Vitamin K ◽  
Coagulation Factor ◽  
Peptide Substrate ◽  
Fluorogenic Peptide Substrate ◽  
Fluorogenic Peptide

Purification of Human Matrilysin Produced inEscherichia coliand Characterization Using a New Optimized Fluorogenic Peptide Substrate

1995 ◽  
Vol 324 (1) ◽  
pp. 59-64 ◽  
Author(s):  
Anthony R. Welch ◽  
Christopher M. Holman ◽  
Michelle F. Browner ◽  
Michael R. Gehring ◽  
Chen-Chen Kan ◽  
...  
Keyword(s):  
Peptide Substrate ◽  
Fluorogenic Peptide Substrate ◽  
Fluorogenic Peptide

scholarly journals A highly sensitive peptide substrate for detecting two Aβ-degrading enzymes: Neprilysin and insulin-degrading enzyme

2010 ◽  
Vol 190 (1) ◽  
pp. 57-62 ◽  
Author(s):  
Po-Ting Chen ◽  
Tai-Yan Liao ◽  
Chaur-Jong Hu ◽  
Shu-Ting Wu ◽  
Steven S.-S. Wang ◽  
...  
Keyword(s):  
Peptide Substrate ◽  
Insulin Degrading Enzyme ◽  
Degrading Enzyme ◽  
Degrading Enzymes ◽  
Highly Sensitive

scholarly journals A Selective Fluorogenic Peptide Substrate for the Human Mitochondrial ATP‐Dependent Protease Complex ClpXP

ChemBioChem ◽  
2020 ◽  
Vol 21 (14) ◽  
pp. 2037-2048
Author(s):  
Zhou Sha ◽  
Jennifer Fishovitz ◽  
Susan Wang ◽  
Sujatha Chilakala ◽  
Yan Xu ◽  
...  
Keyword(s):  
Peptide Substrate ◽  
Fluorogenic Peptide Substrate ◽  
Fluorogenic Peptide

scholarly journals A new fluorogenic substrate for plasmin

1979 ◽  
Vol 183 (3) ◽  
pp. 555-559 ◽  
Author(s):  
P A Pierzchala ◽  
C P Dorn ◽  
M Zimmerman
Keyword(s):  
Plasminogen Activator ◽  
Hela Cells ◽  
Kinetic Constants ◽  
Assay Method ◽  
Peptide Substrate ◽  
Fluorogenic Substrate ◽  
Direct Assay ◽  
Wide Range ◽  
Fluorogenic Peptide Substrate ◽  
Fluorogenic Peptide

A new fluorogenic peptide substrate for plasmin, 7-(N-succinoylalanylphenylalanyl-lysylamido)-4-methylcoumarin trifluoroacetate salt, was prepared that can be used in a simple and direct assay. The results obtained by the assay method are linear over a wide range of enzyme concentrations and sensitive enough to detect as little as 10(-5) CTA units of plasmin. By making use of the inhibitor Trasylol and the differences in kinetic constants, plasmin can be specifically assayed even in the presence of the plasminogen activator thrombin, as well as in culture fluids from HeLa cells.

Design and Synthesis of a Quenched Fluorogenic Peptide Substrate for Human Cytomegalovirus Proteinase

1995 ◽  
Vol 6 (4) ◽  
pp. 255-261 ◽  
Author(s):  
B.K. Handa ◽  
E. Keech ◽  
E.A. Conway ◽  
A. Broadhurst ◽  
A. Ritchie
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Natural Substrate ◽  
Peptide Substrate ◽  
Protein Precursor ◽  
Design And Synthesis ◽  
Fluorogenic Peptide Substrate ◽  
Fluorogenic Peptide

A fluorogenic peptide substrate for HCMV proteinase was synthesized by solid-phase peptide synthesis. The amino acid sequence of this substrate is derived from the maturation cleavage site (M site) of the natural substrate, the assembly protein precursor. The minimum sequence for efficient cleavage requires at least seven residues (P4-P3′). A systematic modification of the peptide substrate was carried out to identify positions suitable for the introduction of the fluorescent donor and the quencher acceptor groups.

scholarly journals Fluorogenic Peptide Substrate for Quantification of Bacterial Enzyme Activities

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Ismail H. Al-Abdullah ◽  
Karine Bagramyan ◽  
Shiela Bilbao ◽  
Meirigeng Qi ◽  
Markus Kalkum
Keyword(s):  
Enzyme Activities ◽  
Peptide Substrate ◽  
Bacterial Enzyme ◽  
Fluorogenic Peptide Substrate ◽  
Fluorogenic Peptide
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