BCHE 395-12 Enzyme Kinetics I

So need to plot inial rates vs s v0 inial velocity

Info iconThis preview shows page 1. Sign up to view the full content.

View Full Document Right Arrow Icon
This is the end of the preview. Sign up to access the rest of the document.

Unformatted text preview: Kine*cs: Simple, First Order Chemical Reac*ons •  Start with rates of first order chemical reac*on •  S à༎ P with reac*on rate constant k –  k = 1/*me •  Reac*on rate is dependent ONLY on the concentra*on of one reactant [S] •  V = k[S] Enzyme Kine*cs: S ⇌ P •  Since V is dependent on [S] we can measure rates at different [S] •  Problem: [S] is changing through the assay à༎ gets used up! •  So, need to plot ini:al rates vs. [S] •  V0 = ini:al velocity Lines are the V (velocity of reac*on) Enzyme Kine*cs: S ⇌ P •  V0 vs. [S] –  [E] constant •  Vary [S] à༎ Measure V0 and plot •  Vmax is plateau •  So much [S], enzyme working at maximum velocity w༇ w༇ w༇ w༇ w༇ w༇ w༇ Enzyme Kine*cs; Enzyme Catalyzed Reac*on •  Hyperbolic shape of curve à༎ implies a limited number of sites in the enzyme where reac*on takes place •  Once sites are filled, reac*on cannot proceed any faster at constant [E] – Enzyme SATURATION Enzyme Kine*cs: S ⇌ P •  V0 vs. [S] •  Michaelis- Menton enzymes (M- M)à༎ •  Enzymes that have characteris*c hyperbolic V0...
View Full Document

This note was uploaded on 03/02/2014 for the course BIOCHEMIST 395 taught by Professor Potenza during the Spring '14 term at NMSU.

Ask a homework question - tutors are online