lecture 6 outline

lecture 6 outline - 1. Acid-Base catalysis fig 6-8 2....

Info iconThis preview shows pages 1–10. Sign up to view the full content.

View Full Document Right Arrow Icon
Lecture #6: Enzymes I. Introduction A. Overview B. Terminology Handout #18 II. How Enzymes Work A. Catalysts B. Key Points Enzymes lower the activation energy Enzymes partially stabilize the transition state Enzymes use binding energy 1 . E n z y m e s l o w e r the activation energy
Background image of page 1

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

View Full DocumentRight Arrow Icon
2. Enzymes lower the activation energy by partially stabilizing the transition state. fig 6-5 a) the enzyme pocket (active site) is complementary to the transition state. b) Binding involving weak interactions (magnetic interactions in example) provides energy that compensates for some of the energy required to reach the transition state. 3. Enzymes use binding energy to provide reaction catalysis and specificity. a) Things the binding energy is used for Handout #19 b) Optimization of weak interactions (binding) also provides enzyme specificity for its substrate. C. Catalytic groups in enzymes
Background image of page 2
Background image of page 3

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

View Full DocumentRight Arrow Icon
Background image of page 4
Background image of page 5

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

View Full DocumentRight Arrow Icon
Background image of page 6
Background image of page 7

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

View Full DocumentRight Arrow Icon
Background image of page 8
Background image of page 9

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

View Full DocumentRight Arrow Icon
Background image of page 10
This is the end of the preview. Sign up to access the rest of the document.

Unformatted text preview: 1. Acid-Base catalysis fig 6-8 2. Covalent Catalysis 3. Metal ion catalysis D. Chymotrypsin figs 6-10, 6-21 III. Enzyme Kinetics: The study of the rates of enzyme-catalyzed reactions A. Substrate concentration affects the rate of enzyme-catalyzed reactions. 1. Measuring rates 2. Determining the change in rate at different substrate concentrations B. Michaelis-Menten Kinetics: Single-substrate, enzyme catalyzed reactions 1. Michaelis-Menten equation 2. Km as a measure of an enzyme's affinity for its substrate C. Double-Reciprocal (Lineweaver Burk) Plot D. Turnover Number: kcat IV. Enzyme Inhibitors A. Reversible fig 6-15 1. Competitive inhibition 2. Uncompetitive inhibition 3. Mixed inhibition B. Irreversible inhibitors V. Regulatory Enzymes A. Allosteric Regulation fig 6-26 B. Reversible covalent modifications...
View Full Document

Page1 / 10

lecture 6 outline - 1. Acid-Base catalysis fig 6-8 2....

This preview shows document pages 1 - 10. Sign up to view the full document.

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