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fluorogenic substrate mca-apk-dnp  (Bachem)

 
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    Bachem fluorogenic substrate mca-apk-dnp
    Fluorogenic Substrate Mca Apk Dnp, supplied by Bachem, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/pro+fluorogenic+substrate/fluorogenic+substrate++7+methoxycoumarin+4+yl+acetyl+pro+leu+gly+leu+3++2++4++dinitrophenyl++l+2+3+diaminopropionyl+ala+arg+nh2/pm37041017-180-4-7
    Average 90 stars, based on 1 article reviews
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    Synthesized:

    Article Title: Exploring the catalytic mechanism of ATPase at the molecular level by tandem mass spectrometry
    Article Snippet: The nucleotide adenosine-5′-triphosphate (ATP) is the coenzyme selected by nature to provide energy for its cellular processes through the ATP hydrolysis reaction.. Although the crystal structures and the general working principles of numerous ATP hydrolases (ATPases) are generally known, this omnipresent ATP conversion reaction is not fully understood at the level of local interactions.. Questions such as “How does the peptide environment of the active sites of ATPases affect their association with ATP and the consecutive reaction of ATP?” and “Why is the conversion of ATP to ADP preferred over other reactions at the active site?” await detailed answers at the molecular level.

    other:

    Article Title: An ACE2-Fc decoy produced in glycoengineered plants neutralizes ancestral and newly emerging SARS-CoV-2 variants and demonstrates therapeutic efficacy in hamsters
    Article Snippet: The enzymatic activity of wild-type and mutant ACE2-Fc was determined using 50 μM 7-methoxycoumarin-4-yl-acetyl-Ala-Pro-Lys-2,4-dinitrophenyl (Bachem, Bubendorf, Switzerland) as substrate.

    Article Title: Intranasal soluble ACE2 improves survival and prevents brain SARS-CoV-2 infection.
    Article Snippet: For ACE2 activity, a fluorogenic substrate Mca-APK-Dnp (Bachem) was used, and the plates were read using a fluorescence plate reader FLX800 (BioTek Instruments) at an excitation wavelength of 320 nm and an emission wavelength of 400 nm.

    Article Title: The Thromboxane Levels in Ovarian Follicular Fluid Are Inversely Correlated With Oocyte Maturation: Implications of PAR-2/-3 Cooperation and Thromboxane Participation in Follicle Development.
    Article Snippet: It has been reported the presence of components from the coagulation thrombin‐generating pathway and prostaglandins (PGs) in human ovarian follicular fluid (FF) but with unclear functions.. Moreover, thrombin can induce COX‐2 expression linking to PG synthesis in several cell types.. Therefore, this study sought to explore the thromboxane (TX) generation in FF and the correlation between FF TX levels and oocyte maturation.

    Article Title: Design, synthesis and biological evaluation of arylsulfonamides as ADAMTS7 inhibitors
    Article Snippet: After the addition of 200 μM solution of the fluorogenic substrate Mca-Lys-Pro-Leu-Gly-LeuDap(Dnp)-Ala-Arg-NH2 (Bachem) in DMSO (final concentration 2 μM), the hydrolysis was monitored every 15 sec for 20 min recording the increase in fluorescence (λex = 325 nm, λem = 400 nm) with a Molecular Devices SpectraMax Gemini XPS plate reader.

    Article Title: Sanguinarine targets the catalytic domain of MMP-9: Molecular dynamics and in vitro studies in MDA-MB 468 breast cancer cells
    Article Snippet: Matrix metalloproteinase 9 (MMP9) belongs to a group of endopeptidases.. It is functionally involved in the proteolytic degradation of extracellular matrix proteins in various pathophysiological conditions.. MMP9 is overexpressed in several cancers and is crucial for metastatic progression of triple negative breast cancer (TNBC).

    Article Title: Design, synthesis and biological evaluation of arylsulfonamides as ADAMTS7 inhibitors
    Article Snippet: After the addition of 200 μM solution of the fluorogenic substrate Mca-Lys-Pro-Leu-Gly-Leu-Dap(Dnp)-Ala-Arg-NH 2 (Bachem) in DMSO (final concentration 2 μM), the hydrolysis was monitored every 15 s for 20 min recording the increase in fluorescence ( λ ex = 325 nm, λ em = 400 nm) with a molecular devices SpectraMax Gemini XPS plate reader.

    Article Title: An ACE2-Fc decoy produced in glycoengineered plants neutralizes ancestral and newly emerging SARS-CoV-2 variants and demonstrates therapeutic efficacy in hamsters.
    Article Snippet: The enzymatic activity of wild-type and mutant ACE2-Fc was determined using 50 μM 7-methoxycoumarin-4yl-acetyl-Ala-Pro-Lys-2,4-dinitrophenyl (Bachem, Bubendorf, Switzerland) as substrate.



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    Enzyme activity profiles of DPPIV family proteases. (A) To compare the peptidase activities of hDPP4, hDPP9, C. elegans DPF‐3, and the catalytic mutant DPF‐3 (S784A), the <t>fluorogenic</t> <t>tripeptide</t> <t>substrate</t> <t>H‐Met‐Gly‐Pro‐AMC</t> was used over a range of concentrations (0.5–64 μ m ). hDPP4 displayed robust, concentration‐dependent activity, reaching 100% normalized fluorescence at 64 μ m substrate. In contrast, wild‐type DPF‐3 showed substantially lower activity, achieving only ~25% of the maximal signal at the highest substrate concentration. hDPP9 activity was negligible under these conditions, and the S784A mutation abrogated DPF‐3 activity completely, confirming loss of catalytic function. (B, C) Michaelis–Menten analysis of DPF‐3 (B) and hDPP4 (C) revealed distinct kinetic parameters. Nonlinear regression yielded for DPF‐3 a V max of 33 193 AU min −1 and a K m of 245.6 μ m . hDPP4 exhibited a higher catalytic efficiency, with V max = 56 027 AU min −1 and K m = 461.5 μ m . The higher V max of hDPP4, despite its higher K m , underscores its greater turnover capacity on this substrate. (D, E) Dose–response curves for the hDPP8/9 inhibitor 1G244 and the hDPP4 inhibitor vildagliptin were generated against DPF‐3 and hDPP4 using substrate concentrations near each enzyme's K m . For DPF‐3, 1G244 inhibited activity with an IC 50 = 499.5 n m , whereas vildagliptin was more potent (IC 50 = 142.1 n m ) (D). DPP4 was more sensitive to both 1G244 (IC 50 = 43.3 n m ) and vildagliptin (IC 50 = 14.8 n m ) (E), indicating differential inhibitor specificities within the DPPIV family. Each graph represents the mean data from triplicate experiments, and the error bars represent the standard deviation.
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    Enzyme activity profiles of DPPIV family proteases. (A) To compare the peptidase activities of hDPP4, hDPP9, C. elegans DPF‐3, and the catalytic mutant DPF‐3 (S784A), the <t>fluorogenic</t> <t>tripeptide</t> <t>substrate</t> <t>H‐Met‐Gly‐Pro‐AMC</t> was used over a range of concentrations (0.5–64 μ m ). hDPP4 displayed robust, concentration‐dependent activity, reaching 100% normalized fluorescence at 64 μ m substrate. In contrast, wild‐type DPF‐3 showed substantially lower activity, achieving only ~25% of the maximal signal at the highest substrate concentration. hDPP9 activity was negligible under these conditions, and the S784A mutation abrogated DPF‐3 activity completely, confirming loss of catalytic function. (B, C) Michaelis–Menten analysis of DPF‐3 (B) and hDPP4 (C) revealed distinct kinetic parameters. Nonlinear regression yielded for DPF‐3 a V max of 33 193 AU min −1 and a K m of 245.6 μ m . hDPP4 exhibited a higher catalytic efficiency, with V max = 56 027 AU min −1 and K m = 461.5 μ m . The higher V max of hDPP4, despite its higher K m , underscores its greater turnover capacity on this substrate. (D, E) Dose–response curves for the hDPP8/9 inhibitor 1G244 and the hDPP4 inhibitor vildagliptin were generated against DPF‐3 and hDPP4 using substrate concentrations near each enzyme's K m . For DPF‐3, 1G244 inhibited activity with an IC 50 = 499.5 n m , whereas vildagliptin was more potent (IC 50 = 142.1 n m ) (D). DPP4 was more sensitive to both 1G244 (IC 50 = 43.3 n m ) and vildagliptin (IC 50 = 14.8 n m ) (E), indicating differential inhibitor specificities within the DPPIV family. Each graph represents the mean data from triplicate experiments, and the error bars represent the standard deviation.
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    Enzyme activity profiles of DPPIV family proteases. (A) To compare the peptidase activities of hDPP4, hDPP9, C. elegans DPF‐3, and the catalytic mutant DPF‐3 (S784A), the <t>fluorogenic</t> <t>tripeptide</t> <t>substrate</t> <t>H‐Met‐Gly‐Pro‐AMC</t> was used over a range of concentrations (0.5–64 μ m ). hDPP4 displayed robust, concentration‐dependent activity, reaching 100% normalized fluorescence at 64 μ m substrate. In contrast, wild‐type DPF‐3 showed substantially lower activity, achieving only ~25% of the maximal signal at the highest substrate concentration. hDPP9 activity was negligible under these conditions, and the S784A mutation abrogated DPF‐3 activity completely, confirming loss of catalytic function. (B, C) Michaelis–Menten analysis of DPF‐3 (B) and hDPP4 (C) revealed distinct kinetic parameters. Nonlinear regression yielded for DPF‐3 a V max of 33 193 AU min −1 and a K m of 245.6 μ m . hDPP4 exhibited a higher catalytic efficiency, with V max = 56 027 AU min −1 and K m = 461.5 μ m . The higher V max of hDPP4, despite its higher K m , underscores its greater turnover capacity on this substrate. (D, E) Dose–response curves for the hDPP8/9 inhibitor 1G244 and the hDPP4 inhibitor vildagliptin were generated against DPF‐3 and hDPP4 using substrate concentrations near each enzyme's K m . For DPF‐3, 1G244 inhibited activity with an IC 50 = 499.5 n m , whereas vildagliptin was more potent (IC 50 = 142.1 n m ) (D). DPP4 was more sensitive to both 1G244 (IC 50 = 43.3 n m ) and vildagliptin (IC 50 = 14.8 n m ) (E), indicating differential inhibitor specificities within the DPPIV family. Each graph represents the mean data from triplicate experiments, and the error bars represent the standard deviation.
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    Enzyme activity profiles of DPPIV family proteases. (A) To compare the peptidase activities of hDPP4, hDPP9, C. elegans DPF‐3, and the catalytic mutant DPF‐3 (S784A), the fluorogenic tripeptide substrate H‐Met‐Gly‐Pro‐AMC was used over a range of concentrations (0.5–64 μ m ). hDPP4 displayed robust, concentration‐dependent activity, reaching 100% normalized fluorescence at 64 μ m substrate. In contrast, wild‐type DPF‐3 showed substantially lower activity, achieving only ~25% of the maximal signal at the highest substrate concentration. hDPP9 activity was negligible under these conditions, and the S784A mutation abrogated DPF‐3 activity completely, confirming loss of catalytic function. (B, C) Michaelis–Menten analysis of DPF‐3 (B) and hDPP4 (C) revealed distinct kinetic parameters. Nonlinear regression yielded for DPF‐3 a V max of 33 193 AU min −1 and a K m of 245.6 μ m . hDPP4 exhibited a higher catalytic efficiency, with V max = 56 027 AU min −1 and K m = 461.5 μ m . The higher V max of hDPP4, despite its higher K m , underscores its greater turnover capacity on this substrate. (D, E) Dose–response curves for the hDPP8/9 inhibitor 1G244 and the hDPP4 inhibitor vildagliptin were generated against DPF‐3 and hDPP4 using substrate concentrations near each enzyme's K m . For DPF‐3, 1G244 inhibited activity with an IC 50 = 499.5 n m , whereas vildagliptin was more potent (IC 50 = 142.1 n m ) (D). DPP4 was more sensitive to both 1G244 (IC 50 = 43.3 n m ) and vildagliptin (IC 50 = 14.8 n m ) (E), indicating differential inhibitor specificities within the DPPIV family. Each graph represents the mean data from triplicate experiments, and the error bars represent the standard deviation.

    Journal: Febs Letters

    Article Title: The Caenorhabditis elegans DPF ‐3 and human DPP4 have tripeptidyl peptidase activity

    doi: 10.1002/1873-3468.70219

    Figure Lengend Snippet: Enzyme activity profiles of DPPIV family proteases. (A) To compare the peptidase activities of hDPP4, hDPP9, C. elegans DPF‐3, and the catalytic mutant DPF‐3 (S784A), the fluorogenic tripeptide substrate H‐Met‐Gly‐Pro‐AMC was used over a range of concentrations (0.5–64 μ m ). hDPP4 displayed robust, concentration‐dependent activity, reaching 100% normalized fluorescence at 64 μ m substrate. In contrast, wild‐type DPF‐3 showed substantially lower activity, achieving only ~25% of the maximal signal at the highest substrate concentration. hDPP9 activity was negligible under these conditions, and the S784A mutation abrogated DPF‐3 activity completely, confirming loss of catalytic function. (B, C) Michaelis–Menten analysis of DPF‐3 (B) and hDPP4 (C) revealed distinct kinetic parameters. Nonlinear regression yielded for DPF‐3 a V max of 33 193 AU min −1 and a K m of 245.6 μ m . hDPP4 exhibited a higher catalytic efficiency, with V max = 56 027 AU min −1 and K m = 461.5 μ m . The higher V max of hDPP4, despite its higher K m , underscores its greater turnover capacity on this substrate. (D, E) Dose–response curves for the hDPP8/9 inhibitor 1G244 and the hDPP4 inhibitor vildagliptin were generated against DPF‐3 and hDPP4 using substrate concentrations near each enzyme's K m . For DPF‐3, 1G244 inhibited activity with an IC 50 = 499.5 n m , whereas vildagliptin was more potent (IC 50 = 142.1 n m ) (D). DPP4 was more sensitive to both 1G244 (IC 50 = 43.3 n m ) and vildagliptin (IC 50 = 14.8 n m ) (E), indicating differential inhibitor specificities within the DPPIV family. Each graph represents the mean data from triplicate experiments, and the error bars represent the standard deviation.

    Article Snippet: Enzymatic activities of hDPP4 and DPF‐3 were measured using the fluorogenic tripeptide substrate H‐Met‐Gly‐Pro‐AMC (7‐amino‐4‐methylcoumarin, Catalog number: ES017, R&D Systems).

    Techniques: Activity Assay, Mutagenesis, Concentration Assay, Fluorescence, Generated, Standard Deviation