Description
Return uncompetitive apparent Vmax and Km.
Enzyme and binding models relate supplied rates, concentrations and active-site conventions under specific assumptions. A local apparent parameter, turnover or occupancy term does not identify an inhibition mechanism, fit a kinetic model or establish a validated assay.
Return uncompetitive apparent Vmax and Km.
When to use this tool
Use Uncompetitive Apparent Vmax Factor when evaluating the stated enzyme, binding, dilution or rate-basis term.
How to use the tool and how it works
- Enter vmax, km, inhibitor, kiPrime. Use the units and conventions below.
- Run the tool. Correct any format, range, or cross-field input error before interpreting the output.
- Read alphaPrime, apparentVmax, apparentKm. Use the output convention below.
Return uncompetitive apparent Vmax and Km. Require nonnegative vmax, km, inhibitor and kiPrime > 0; alphaPrime = 1+inhibitor/kiPrime, divide both parameters by alphaPrime.1
| Input field | Meaning and units | Accepted input |
|---|---|---|
| vmax | Vmax | Required. Finite number; minimum 0. |
| km | Km | Required. Finite number; minimum 0. |
| inhibitor | Inhibitor | Required. Finite number; minimum 0. |
| kiPrime | Ki Prime | Required. Finite number; strictly above 0. |
| Output field | Interpretation | Returned shape |
|---|---|---|
| alphaPrime | Alpha Prime | Required. Finite number. |
| apparentVmax | Apparent Vmax | Required. Finite number. |
| apparentKm | Apparent Km | Required. Finite number. |
{
"input": {
"vmax": 100,
"km": 10,
"inhibitor": 3,
"kiPrime": 1
},
"output": {
"alphaPrime": 4,
"apparentVmax": 25,
"apparentKm": 2.5
}
}Limitations and assumptions
- This is the supplied ideal uncompetitive-inhibition model; no mechanism identification, parameter fit or assay validation is performed.
- Inputs must satisfy both the field types and the cross-field conditions above. Invalid input causes an error; a successful false flag or documented placeholder is a different result.
- Numeric calculations use binary floating point unless exact decimal-integer arithmetic is explicitly stated. No hidden measurement tolerance or decimal rounding is added; nonfinite or out-of-contract results are rejected. Numeric signed-zero results are exported as zero.
Alternative or Complementary methods
Use calibrated observations and a complete suitable kinetic/assay model, including substrate, active-site and stoichiometric conventions, for biochemical inference.
References
Similar or alternative tools
- Enzyme Inhibition Competitive Apparent Km
Return competitive apparent Km.
- Substrate Turnover Time Factor
Return expected turnovers from a constant supplied rate.