Enzyme Kinetics (Michaelis-Menten) Solver mechanism

Model scope

The two displayed equations are algebraically correct within their assumptions. Verdict is NEEDS_REVIEW because the claimed v(t) output, fitting algorithm, regression weighting, R² definition, physical-domain constraints, and reciprocal-data handling are unspecified. The existing educational/non-medical label is appropriate, but the interface should also state that fitted parameters are model-dependent and that Lineweaver-Burk fits may be statistically inferior to nonlinear fits.

• The Michaelis-Menten formula v=Vmax[S]/(Km+[S]) is standard for a single-substrate reaction under steady-state, initial-rate conditions, but those applicability constraints are not stated.
• The Lineweaver-Burk transformation is algebraically correct for nonzero [S] and v, but ordinary least-squares fitting in reciprocal space is statistically biased because it disproportionately weights low-velocity measurements; the fitting method is unspecified.
• The output 'v(t) curve' is ambiguous and not supported by the supplied formula, which computes v as a function of substrate concentration [S], not time t. A time curve requires a substrate-depletion or reaction-progress model.
• The fitting procedure, parameter constraints, treatment of replicate data and weighting, and definition of R² are unspecified, so Vmax, Km, and R² are not uniquely determined from the specification.

Units and conventions

• [S] and Km must use the same concentration unit.
• v and Vmax must use the same velocity unit, such as micromoles per minute.
• For the Lineweaver-Burk equation, 1/[S] and Km/Vmax must have reciprocal-concentration units, while 1/v and 1/Vmax must have reciprocal-velocity units.
• The examples assume nonnegative substrate concentration, positive Km, positive Vmax, and measured initial velocity before substantial substrate depletion.
• All reciprocal-fit data points require [S] != 0 and v != 0.

Inspectable vector

One of 4 source-bound review vectors:

{
  "inputs": {
    "mode": "direct",
    "Vmax": "100 micromol/min",
    "Km": "20 micromol/L",
    "sampled_substrate_concentrations": [
      "0 micromol/L",
      "20 micromol/L",
      "80 micromol/L"
    ]
  },
  "expected_outputs": {
    "sampled_points": {
      "0 micromol/L": "0 micromol/min",
      "20 micromol/L": "50 micromol/min",
      "80 micromol/L": "80 micromol/min"
    },
    "curve_features": {
      "root": "[S]=0 micromol/L, v=0",
      "half_maximum": "[S]=Km=20 micromol/L, v=50 micromol/min",
      "horizontal_asymptote": "v approaches 100 micromol/min as [S] approaches infinity",
      "finite_vertical_asymptote": "none for physical [S]>=0"
    },
    "R_squared": "not applicable for direct parameters"
  },
  "working": "At [S]=0: v=100*0/(20+0)=0/20=0 micromol/min. At [S]=20: v=100*20/(20+20)=2000/40=50 micromol/min. At [S]=80: v=100*80/(20+80)=8000/100=80 micromol/min. At [S]=Km, v=Vmax*Km/(Km+Km)=Vmax/2=50 micromol/min. As [S] becomes very large, Km/[S] approaches 0, so v approaches Vmax=100 micromol/min."
}

Failure boundary

BREAK_CLAIMED · SELF_FLAGGED

The specification exposes undefined-result paths at [S]=0 in the Lineweaver-Burk transform and at Km+[S]=0 in the Michaelis-Menten expression. Negative or unit-inconsistent inputs can also produce invalid or materially different results unless explicitly rejected or normalized.

Other records

Sources and evidence

These pointers bind the page to evidence. They do not grant authority or collapse verification into deployment.

• VERIFIED_LEDGER.json
• evidence-tranche6/tranche6-results.json
• BOUNDARY_HAZARD_CATALOG.json