Chapter 6 - Metabolism

Fats

________ are also broken down through similar catabolic reactions to release energy and make ATP.

Adenosine triphosphate

________ (ATP)- small relatively simple molecule; contains potential for quick burst of energy than can be harnessed to perform cell work.

Amino acid residue

________ provide ions or chemical groups that form covalent bonds with substrate molecules as a step of reaction process.

Adenosine

________ is a nucleoside of nitrogenous base adenine and five- carbon sugar ribose.

Coenzymes

________- organic helper molecules with a basic atomic structure made up of carbon and hydrogen.

Metabolism

________- all chemical reactions that take place inside cells, including those that use energy and those that release energy.

Bioenergetics

________- concept of energy flow through living systems (like cells)

ATP

________ is also unstable molecule that can spontaneously dissociate into ADP.

Catalyst

________- substance that helps chemical reaction to occur.

Chemical reaction goal

________ is to harvest energy in sugar molecules.

Sugar

________ (glucose) is stored as starch or glycogen.

sufficient energy

When broken, it release ________ to power cell reactions and processes.

Activators

________ can also enhance enzyme function allosterically.

smaller molecules

Synthesize sugar from ________ (requires energy)

simpler ones

On the other end of the spectrum, anabolism refers to metabolic processes that build complex molecules out of ________, such as macromolecule synthesis.

chemical reaction

This energy refers to energy associated with ________ available after entrophy is accounted for; this is usable energy-- available to do work.

Energy

________ stored in bonds of molecules is released in this pathway and harvested to be used to produce ATP.

Plants

________ use sunlight to convert to carbon dioxide gas into sugar molecules (like glucose)

phosphates

The bonds that connect the ________ (phosphoanhydride bonds) have high- energy content.

Carbs

________ consumed have origins in photosynthesis organisms like plants.

Cells

________ evolved to use products of their own reaction product to regulate its own further production.

eukaryotic cells

In ________, molecules like enzymes are compartmentalized into different organelles.

Enzymes

________ are usually proteins consisting of one or more polypeptide chains.

Heat energy

________- speeds up motion of molecules, increasing frequency and force with which they collide; also moves atoms and bonds in molecule slightly, reaching transition state.

Single cells

________ are biological systems.

Glucose synthesis

________ and glucose breakdown are examples of anabolic and catabolic pathways, respectively.

Allosteric activators

________ bind to locations on enzyme away from active site, inducing conformational change that increases affinity of enzymes active sites for its substrates.

Biological organisms energy

________ is exhchage between them and their surroundings.

Light energy

________ is temporarily stored in ATP and NDPH (nicotinamide adenine dinucleotide phosphate)

large macromolecules

There are metabolic reactions that involve breaking down complex chemicals into simpler ones, such as breaking down ________.

environmental temp

Increasing ________ can increase reaction rates.

Interaction

________ cause mild shift in enzymes structure that confirms ideal binding arrangement between enzyme nad substrate.

harvest energy

All organisms ________ from their environment and convert it to ATP to carry out cell functions.

cell environments

In some ________, enzyme activity is partly controlled by environmental factors like pH and temp.

Entropy of universe

________ is constantly increasing due to loss of usable energy with each energy transfer that occurs.

feedback inhibition

During ________, metabolic pathway products serve as inhibitors (usually allosteric) of one or more of the enzymes (usually the first committed enzyme of the pathway) involved in the pathway that produces them.

energy transfer

No ________ is efficient because some energy is lost in unusable form.

chains of amino acids

Almost all enzymes are proteins, made of ________.

Thermodynamics

________- study fo energy and energy transfer involving physical matter.

High temps

________ will cause enzymes to denature- process that changes natural properties of substance.

Enzyme substrate complex

________ can lower activation energy by controting substrate molecules to facilitate bond breaking, help reach transition state.

low energy

High entropy means high disorder and ________.

Kinetic energy

________- energy associated with objects in motion.

Enzyme inhibition

________ and activation via other molecules are other important ways that enzymes are regulated.

Endergonic reactions

________- reaction that requires input of energy instead of releasing energy.

inhibitor molecule

A(n) ________ is similar to a substrate that it can bind to active site and simply block substrate from binding.

Entropy

________ is a measure of a system's disorder.

Phosphoanhydride bonds

________- bonds that link phosphates.

Molecules

________ also have potential energy because breaking molecular bonds has the potential to release energy.

Total energy change

________ in system is called enthalpy.

bioenergetics

concept of energy flow through living systems (like cells)

metabolism

all chemical reactions that take place inside cells, including those that use energy and those that release energy

breakdown of glucose-

simple sugar

in chemical reactions of photosynthesis, primary energy currency in form of ATP-

adrenosine triphosphate

metabolic pathways

series fo interconnected biochemical reactions that convert substrate molecule or molecules thorugha series of metabolic intermediates

stored sugar can provide ATP-

36 to 38 molecules

kinetic energy

energy associated with objects in motion

potential energy

energy with potential to do work

chemical energy

potential energy within chemical bonds and released when bonds are broken

free energy

used to quantitate energy transfers; also called Gibbs free energy after Josiah Willard Gibbs (developed measurement)

this energy refers to energy associated with chemical reaction available after entrophy is accounted for; this is usable energy-

available to do work

delta G

change in free energy

exergonic reactions

reactions that have negative G and consequently release free energy

endergonic reactions

reaction that requires input of energy instead of releasing energy

activation energy

small amount of energy input necessary for all chemical reactions to occur

transition state

small energy input required to achieve contorted state; high-energy, unstable state

heat energy

speeds up motion of molecules, increasing frequency and force with which they collide; also moves atoms and bonds in molecule slightly, reaching transition state

thermodynamics

study fo energy and energy transfer involving physical matter

2 types of systems

open or closed

of work cells need to do

build complex molecules, transport material, powering beating motion of cilia, contract muscle fibers to create movement, reproduction

heat energy

energy transferred from one system to another that is not doing work

entropy

measure of randomness or disorder in system

adenosine triphosphate (ATP)

small relatively simple molecule; contains potential for quick burst of energy than can be harnessed to perform cell work

adenosine is made of three phosphate groups

alpha, beta, gamma

phosphoanhydride bonds

bonds that link phosphates

catalyst

substance that helps chemical reaction to occur

enzymes

molecules that catalyze biochemical reactions

substrates

chemical reactants to which enzyme binds

active site

location in enzyme where substrate binds

high temps will cause enzymes to denature

process that changes natural properties of substance

induced fit

expanpds upond lock and key model of enzyme substrate by describing a more dynamic interaction between enzyme and substrate

allosteric inhibition

inhibitor molecules bind to enzymes in location where binding induces conformational change that reduces affinity of enzyme for its substrate

2 helper molecules

cofactors and coenzymes

cofactors

inorganic ions like iron and magnesium

coenzymes

organic helper molecules with a basic atomic structure made up of carbon and hydrogen

6.4 ATP

Adenosine Triphosphate

Enzymes bind to substrates and catalyze reactions in four different ways

bringing substrates together in an optimal orientation, compromising the bond structures of substrates so that bonds can break down more easily, providing optimal environmental conditions for a reaction to occur, or participating directly in their chemical reaction by forming transient covalent bonds with the substrates