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michaelis–menten kinetics tool  (GraphPad Software Inc)


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    GraphPad Software Inc michaelis–menten kinetics tool
    Michaelis–Menten Kinetics Tool, supplied by GraphPad Software Inc, 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/michaelis%E2%80%93menten+kinetics+tool/michaelis+menten+kinetics/pm39920612-74-17-21
    Average 90 stars, based on 1 article reviews
    michaelis–menten kinetics tool - by Bioz Stars, 2026-09
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    Article Title: Differential Mechanisms of Soybean-Derived ACE2-Activating Peptides IVPQ and IAVPT in ACE2-Mediated Endothelial Protection.
    Article Snippet: This study aimed to investigate the modulatory effects of soybean-derived peptides IVPQ and IAVPT, which were initially identified as potent ACE2-activating peptides, on Ang II-induced endothelial dysfunction in human umbilical vein endothelial cells (HUVECs) and the underlying mechanisms via ACE2 activation.. IVPQ and IAVPT ameliorated Ang II-induced malignant migration and NO reduction in HUVECs via the activation of the ACE2/Ang-(1−7)/MasR axis, resulting in Ang II degradation and decreased Ang II signaling.. These protective effects were attenuated by ACE2 knockdown to different degrees, which was possibly due to different mechanisms of activating ACE2, where IAVPT directly activated ACE2 at a concentration of 1.0 × 10−4 M and IVPQ upregulated ACE2 likely through effects on ACE2 mRNA stability.

    Article Title: Angiotensin-Converting Enzyme 2 Activation Is Not a Common Feature of Angiotensin-Converting Enzyme Inhibitory Peptides.
    Article Snippet: Angiotensin-converting enzyme (ACE) catalyzes the formation of angiotensin II (Ang II), a vasoconstrictor, whereas its homologue ACE2 degrades Ang II into angiotensin (1−7) (Ang (1−7)), a vasodilator.. Given the similarities in structure and their interconnected roles in the regulation of cardiovascular system, this study aims to investigate if ACE-inhibitory (ACEi) peptides can also activate ACE2.. About 200 potent ACEi peptides were subjected to molecular docking, 20 peptides were selected for cell and in vitro enzymatic activity studies, and 5 peptides were fed orally to spontaneously hypertensive rats at a dose of 15 mg/kg body weight/day for 7 days.



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    on-line michaelis-menten kinetics tool  (GraphPad Software Inc)
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    Discovery of SBI-797812, a small molecule NAMPT activator. a Compiled melting temperature (Tm) data for human NAMPT treated with chemical compounds ( N = 57,004) and tested with the PTS assay protocol (green). NAMPT ligands produced an upward Tm shift. DMSO was the Neg Control (blue). CHS-828 (20 μM) was the Pos Control (red). b Structures of NAMPT activators and inhibitors. c Pivotal role of the 4-pyridyl nitrogen in SBI-797812 for NAMPT activation. NAMPT (30 nM), NAM (10 μM), PRPP (50 μM), ATP (2 mM) were incubated 1 h at 37 °C with vehicle or 2 μM SBI-797812, GNI-50, or SBI-796950. NMN was detected using the fluorescence assay. Data are expressed as means ± s.d.; n = 4. *, p < 0.0001 compared to Vehicle. One-way ANOVA with Dunnett’s multiple comparisons test was used. d Dose-dependent activation of human NAMPT by SBI-797812. NMN production assay was performed as above but with 25 μM NAM and varying SBI-797812. NMN levels were normalized for basal NMN production without SBI-797812. Three replicates were run for each SBI-797812 concentration. <t>Michaelis-Menten</t> curve fit was produced with GraphPad Prism software. e NAMPT(G217R) mutant was resistant to both SBI-797812 and FK-866. NAMPT(G217R) (50 nM) was incubated with NAM (10 μM), PRPP (50 μM), ATP (2 mM) and (where indicated) 1 μM SBI-797812 and/or 1 μM FK-866. Reactions were performed for 1 h at 37 °C. NMN was detected with the fluorescence assay. Data are expressed as means ± s.d.; n = 4. * p < 0.0001 compared to NAMPT(G217R). One-way ANOVA with Dunnett’s multiple comparisons test was used. f FK-866 and CHS-828 blocked binding of SBI-797812 to NAMPT. SBI-797812 was added to T8MD-Tween buffer with ATP or the same buffer containing NAMPT, NAMPT + FK-866, or NAMPT + CHS-828. Samples were incubated at 37 °C for 10 min and applied to a spin column to separate NAMPT-bound SBI-797812 from unbound SBI-797812. SBI-797812 (in column eluent) was measured by LC-MS-TOF. Data are expressed as means ± s.d.; n = 4. * p < 0.0001 compared to “No NAMPT”. One-way ANOVA with Dunnett’s multiple comparisons test was used. For Fig. 1c–f, source data are provided as a Source Data file
    On Line Michaelis Menten Kinetics Tool, supplied by GraphPad Software Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Discovery of SBI-797812, a small molecule NAMPT activator. a Compiled melting temperature (Tm) data for human NAMPT treated with chemical compounds ( N = 57,004) and tested with the PTS assay protocol (green). NAMPT ligands produced an upward Tm shift. DMSO was the Neg Control (blue). CHS-828 (20 μM) was the Pos Control (red). b Structures of NAMPT activators and inhibitors. c Pivotal role of the 4-pyridyl nitrogen in SBI-797812 for NAMPT activation. NAMPT (30 nM), NAM (10 μM), PRPP (50 μM), ATP (2 mM) were incubated 1 h at 37 °C with vehicle or 2 μM SBI-797812, GNI-50, or SBI-796950. NMN was detected using the fluorescence assay. Data are expressed as means ± s.d.; n = 4. *, p < 0.0001 compared to Vehicle. One-way ANOVA with Dunnett’s multiple comparisons test was used. d Dose-dependent activation of human NAMPT by SBI-797812. NMN production assay was performed as above but with 25 μM NAM and varying SBI-797812. NMN levels were normalized for basal NMN production without SBI-797812. Three replicates were run for each SBI-797812 concentration. Michaelis-Menten curve fit was produced with GraphPad Prism software. e NAMPT(G217R) mutant was resistant to both SBI-797812 and FK-866. NAMPT(G217R) (50 nM) was incubated with NAM (10 μM), PRPP (50 μM), ATP (2 mM) and (where indicated) 1 μM SBI-797812 and/or 1 μM FK-866. Reactions were performed for 1 h at 37 °C. NMN was detected with the fluorescence assay. Data are expressed as means ± s.d.; n = 4. * p < 0.0001 compared to NAMPT(G217R). One-way ANOVA with Dunnett’s multiple comparisons test was used. f FK-866 and CHS-828 blocked binding of SBI-797812 to NAMPT. SBI-797812 was added to T8MD-Tween buffer with ATP or the same buffer containing NAMPT, NAMPT + FK-866, or NAMPT + CHS-828. Samples were incubated at 37 °C for 10 min and applied to a spin column to separate NAMPT-bound SBI-797812 from unbound SBI-797812. SBI-797812 (in column eluent) was measured by LC-MS-TOF. Data are expressed as means ± s.d.; n = 4. * p < 0.0001 compared to “No NAMPT”. One-way ANOVA with Dunnett’s multiple comparisons test was used. For Fig. 1c–f, source data are provided as a Source Data file

    Journal: Nature Communications

    Article Title: Boosting NAD + with a small molecule that activates NAMPT

    doi: 10.1038/s41467-019-11078-z

    Figure Lengend Snippet: Discovery of SBI-797812, a small molecule NAMPT activator. a Compiled melting temperature (Tm) data for human NAMPT treated with chemical compounds ( N = 57,004) and tested with the PTS assay protocol (green). NAMPT ligands produced an upward Tm shift. DMSO was the Neg Control (blue). CHS-828 (20 μM) was the Pos Control (red). b Structures of NAMPT activators and inhibitors. c Pivotal role of the 4-pyridyl nitrogen in SBI-797812 for NAMPT activation. NAMPT (30 nM), NAM (10 μM), PRPP (50 μM), ATP (2 mM) were incubated 1 h at 37 °C with vehicle or 2 μM SBI-797812, GNI-50, or SBI-796950. NMN was detected using the fluorescence assay. Data are expressed as means ± s.d.; n = 4. *, p < 0.0001 compared to Vehicle. One-way ANOVA with Dunnett’s multiple comparisons test was used. d Dose-dependent activation of human NAMPT by SBI-797812. NMN production assay was performed as above but with 25 μM NAM and varying SBI-797812. NMN levels were normalized for basal NMN production without SBI-797812. Three replicates were run for each SBI-797812 concentration. Michaelis-Menten curve fit was produced with GraphPad Prism software. e NAMPT(G217R) mutant was resistant to both SBI-797812 and FK-866. NAMPT(G217R) (50 nM) was incubated with NAM (10 μM), PRPP (50 μM), ATP (2 mM) and (where indicated) 1 μM SBI-797812 and/or 1 μM FK-866. Reactions were performed for 1 h at 37 °C. NMN was detected with the fluorescence assay. Data are expressed as means ± s.d.; n = 4. * p < 0.0001 compared to NAMPT(G217R). One-way ANOVA with Dunnett’s multiple comparisons test was used. f FK-866 and CHS-828 blocked binding of SBI-797812 to NAMPT. SBI-797812 was added to T8MD-Tween buffer with ATP or the same buffer containing NAMPT, NAMPT + FK-866, or NAMPT + CHS-828. Samples were incubated at 37 °C for 10 min and applied to a spin column to separate NAMPT-bound SBI-797812 from unbound SBI-797812. SBI-797812 (in column eluent) was measured by LC-MS-TOF. Data are expressed as means ± s.d.; n = 4. * p < 0.0001 compared to “No NAMPT”. One-way ANOVA with Dunnett’s multiple comparisons test was used. For Fig. 1c–f, source data are provided as a Source Data file

    Article Snippet: The values for V max and K m (ATP hydrolysis) were deduced using the on-line Michaelis-Menten kinetics tool at http://www.graphpad.com/quickcalcs/ttest1/?Format=SEM .

    Techniques: Produced, Activation Assay, Incubation, Fluorescence, Concentration Assay, Software, Mutagenesis, Binding Assay, Liquid Chromatography with Mass Spectroscopy