n) Enzymatic proteins- catalyst- facilitate a reaction to increase the reaction rate(1) need this because temperatures are so varying that certain reactions do not happen(2) a substrate (or ligand) binds to an active binding site on an enzymatic protein and are converted to some other substance(3) reduce activation energy in the presence of an enzyme(a) enzyme will bind to and hold the substrate ligand in an appropriate orientation- less energy is required to make it into something else(b) some of the energy to bind that substance is transferred to the catalysist(4) enzymes can convert 1000 substrates per 1 second to product(5) activity(a) usually referred to as a velocity: conversion substrate to product per unit time(b) times when we want these to move quickly and other times we want it done at a lower rate(c) most enzymes never reach saturation- work more in subsaturation, so that you can control the rate of the reaction(d) we do not stock pile things in the cell(e) control of enzyme activity in cell (temperature, pressure, pH is not effective here)(i) control substrate concentration- relatively effective for short term(ii) change the Km(iii) change in enzyme concentration- ultimately most affective long term(f) there can an alternative binding site that can cause an allosteric change, regulatory proteins can bind to the binding site and through the ripple effect can cause the active binding site to change, making it less or more efficient (high/low affinity for the substrate)(g) Active, regulatory and structural ligands exist. Regulatory ligand can be:(i) positive modulators- increasing the affinity for a substrate(ii) negative modulator- decreases affinity for substrate (curve shifts to the right, increase in Km decreases the affinity but Vmax remains the same- not as active at any given substrate concentration)(h) have up to ten modulators for regulatory sites, multiple binding sites – the active binding sites are constantly changing(i) substrate ligand is altered but a regulatory ligand is never altered(6) need on average 1 gram of ATP a minute for our metabolism to survive with using enzymesIII. ThermodynamicsB. 1st law- energy can not be created or destroyed1. we get most energy from the sun, however we can not derive much from the suna) we derive our energy from the oxidative process of converting organic products to energyBY 330 1st Edition Lecture 5Outline of Last Lecture 3. Protein (continued)Outline of Current Lecture 3. Protein (continued)III. Thermodynamics A. 1st law of thermodynamicsCurrent Lecturen) Enzymatic proteins- catalyst- facilitate a reaction to increase the reaction rate(1) need this because temperatures are so varying that certain reactions do not happen(2) a substrate (or ligand) binds to an active binding site on an enzymatic protein and are converted to some other substance(3) reduce activation energy in the presence of an enzyme (a) enzyme will bind to and hold the substrate ligand in an appropriate orientation- less energy is required to make it into something else(b) some of the energy to bind that substance is transferred to the catalysist(4) enzymes can convert 1000 substrates per 1 second to product(5) activity (a) usually referred to as a velocity: conversion substrate to product per unit time(b) times when we want these to move quickly and other times we want it done at a lower rate These notes represent a detailed interpretation of the professor’s lecture. GradeBuddy is best used as a supplement to your own notes, not as a substitute.Usually a hyperbolic curve, until it reaches Vmax or it is saturated (c) most enzymes never reach saturation- work more in subsaturation, so that you can control the rate of the reaction(d) we do not stock pile things in the cell(e) control of enzyme activity in cell (temperature, pressure, pH is not effective here) (i) control substrate concentration- relatively effective for short term (ii) change the Km (iii) change in enzyme concentration- ultimately most affective long term(f) there can an alternative binding site that can cause an allosteric change, regulatory proteins can bind to the binding site and through the ripple effect can cause the active binding site to change, making it less or more efficient (high/low affinity for the substrate) (g) Active, regulatory and structural ligands exist. Regulatory ligand can be:(i) positive modulators- increasing the affinity for a substrate(ii) negative modulator- decreases affinity for substrate (curveshifts to the right, increase in Km decreases the affinity but Vmax remains the same- not as active at any given substrate concentration)Positive modulator- decreases Km½ vmax ; km= [substrate] @1/2 the VmsxNegative modulator - inceases Km, same Vmax and decreases affinityEnzyme activity [Substrate](h) have up to ten modulators for regulatory sites, multiple binding sites – the active binding sites are constantly changing(i) substrate ligand is altered but a regulatory ligand is never altered (6) need on average 1 gram of ATP a minute for our metabolism to survive with using enzymesIII. ThermodynamicsB. 1st law- energy can not be created or destroyed 1. we get most energy from the sun, however we can not derive much from the suna) we derive our energy from the oxidative process of converting organic products to