2009-09-28_-_Lecture_10 - Biochemistry 461 FS 20089...

Info iconThis preview shows pages 1–3. Sign up to view the full content.

View Full Document Right Arrow Icon
Biochemistry 461 FS 20089 Michigan State University Introduction to Enzyme Kinetics September 28, 2009 Lecture 10 Kinetics can tell you about mechanism • Disprove mechanisms that are not consistent with the data. • Propose a reaction mechanism that is consistent with the data. • Gain insight into the role of particular amino acid residues. (E.G., “Arg XXX is not involved in substrate binding but is critical for efficient reaction catalysis.”) Why Study Enzyme Kinetics? 2
Background image of page 1

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
• Study reaction velocity as a function of: • Enzyme concentration -- usually not very informative • Temperature -- determine activation energies • pH -- acid/base catalysis Substrate Concentration(s): -- this is the central tool • Normally measure the initial rate ( ν 0 ), to avoid complications • Normally [S] >> [E] How Do You Study Enzyme Kinetics? 3 Michaelis and Menten interpreted the plots of ν 0 vs. [S] in terms of a reaction scheme centered on the enzyme-substrate complex (ES) which is sometimes called the Michaelis complex . They proposed: • The formation of an ES complex is a necessary step • The first step is S binding to E and that this step is a relatively fast and reversible step
Background image of page 2
Image of page 3
This is the end of the preview. Sign up to access the rest of the document.

This note was uploaded on 01/17/2012 for the course NSC 461 taught by Professor Benning during the Fall '11 term at Michigan State University.

Page1 / 7

2009-09-28_-_Lecture_10 - Biochemistry 461 FS 20089...

This preview shows document pages 1 - 3. Sign up to view the full document.

View Full Document Right Arrow Icon
Ask a homework question - tutors are online