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Lecture

# Michaelis-Menton kinetics, turnover number, unit, specific activity

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School
Department
Life Science
Course
LIFE 212
Professor
Semester
Fall

Description
19 September Michaelis-Menton Kinetics Describes irreversible catalytic reactions Km = Michaelis-Menton rate constant (k2+kcat) Km = k1 Reaction rates vary with changes to [substrate] and [enzyme] Fast reaction → smaller Km Enz I Report Plotted A475s [dopachrome, mM] A Calculate C Generate standard curve (y = mx + b) Correlation co-efficient Calc. μmoles dopachrome Dopachrome Plot A475s μmoles mL Used in Enz II lab Enz II Report Part A Calc. Optimum [Enzyme] req. to convert 2 μmoles of DOPA to Dopachrome in 3 to 5 minutes (= 2 mM Dopa) micromoles Calc min Part B Determined pH effects on Velocity (at 1.5 min) A 475vs velocity mM Dopa/micromole Dopachrome μmols Plot velocity ( min ) vs pH Part C Det. Temperature effects on Velocity A 475vs Velocity mM Dopa micromole Dopachrome μmols Plot velocity ( ) vs temperature min μM Velocity is commonly expressed as min Enz III Report 1. Det. A 475 [Product (mM)] & μmols In 0.5 min increments For serial dilution series: 5 different [Substrate] 2. Plot Product (Y axis) vs Minutes (X axis) Put all curves on same graph Calc. slope m = Velocity y2 – y1 (x1, y1) (x2, y2) M = x2−x1
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