Exam Four: Part Four Flashcards

1
Q

what is METABOLISM?

A

CHEMICAL PROCESS that occurs within all living things to MAINTAIN LIFE
ex. converting food into energy

use of NUTRIENTS (sources of energy/molecular building blocks)

PROCESSING:
- we break them down to help RELEASE ENERGY to be stored in their chemical bonds
- creation of certain BUILDING BLOCKS to build MACROMOLECULES needed for life

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2
Q

what are ENZYMES?

A

all of the work being done inside the cell is being done by ENZYMES:

  • energy is required for a REACTION to proceed
    • helps BREAK OLD chemical bonds of reactants
    • forms NEW chemical bonds in the product

they are CATALYSTS;
- LOWER THE ENERGY OF ACTIVATION
- INCREASE THE REACTION RATE–chemical reactions occur more frequently and we get more product
- NOT PERMANENTLY CHANGED
(always RECYCLED)

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3
Q

definition of REACTION RATE + ACTIVATION ENERGY

A

REACTION RATE:
the FREQUENCY of COLLISIONS with SUFFICIENT ENERGY to make a PRODUCT depends on the NUMBER OF REACTANTS with ENOUGH ENERGY

  • needs ENOUGH ENERGY
  • WITH PROPER ORIENTATION
    = REACTION

ACTIVATION ENERGY:
MINIMUM ENERGY required to start a reaction

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4
Q

what is an ENZYME’S STRUCTURE?

A

most enzymes are PROTEINS
- encoded with GENETIC MATERIAL
- transcribed into mRNA
- after, then translated into a protein!

PROTEIN – is FOLDED and MODIFIED
through the TERTIARY STRUCTURE/3-D SHAPE
- no shape. no reaction

ACTIVE SITES:
- POCKET where substrate fits and reaction occurs
- very SPECIFIC, only binds to a specific molecule
SUBSTRATES:
substances are affected by the enzyme at the active site

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5
Q

how do we NAME ENZYMES?

A

substrate + chemical reaction type + “ase”

  • substrate - sucrose
  • reaction - breaks down sucrose to glucose and fructose
  • name - sucrase
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6
Q

what are Co-FACTORS and CO-ENZYMES?

A

sometimes ENZYMES need a second - NON-PROTEIN COMPONENT to work
- needed both for enzymes to function

COFACTORS:
- made from MINERALS (Zn, Mg, or Fe)

COENZYMES;
- anything made of an ORGANIC MOLECULE
- made from VITAMINS or NUCLEOTIDES

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7
Q

what are two IMPORTANT COENZYMES?

A

Nicotinamide adenine dinucleotide [NAD+]
& Nicotinamide adenine dinucleotide phosphate [NADP+]
- functions as ELECTRON CARRIERS
- both DINUCLEOTIDES

COENZYME A [CoA]
- important role in METABOLISM

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8
Q

what are some ENVIRONMENTAL EFFECTS on ENZYME ACTION?

A
  • TEMPERATURE
  • pH
  • SUBSTRATE CONCENTRATION
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9
Q

describe ENZYME ACTION

A

ENZYMES are EXTREMELY EFFICIENT:
- can catalyze reactions up to 10 BILLION TIMES faster than w/o enzyme
- can react with 1-10,000 substrate molecules per second

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10
Q

what is TURNOVER NUMBER?

A

the MAXIMUM NUMBER of substrate molecules that can be processed by enzymes into product in ONE SEC for a given enzyme concentration
- where the enzyme is FULLY SATURATED WIHTHIN SUBSTRATE

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11
Q

describe TEMPERATURE and its effect on ENZYME ACTION

A
  • OPTIMUM TEMPERATURE:
    • the temperature at which the MAXIMUM REACTION RATE is achieved
      • (most optimal at 35-40 degrees C)
  • TEMPERATURE IS LOWER THAN OPTIMUM
    • reactions may SLOW OR STOP–INACTIVE
    • LESS MOVEMENT within the reaction
  • TEMPERATURE IS HIGHER THAN OPTIMUM
    • proteins are DENATURED = irreversibly inactivated by heat (even if the temperature is lowered)
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12
Q

describe pH and its effects on ENZYME ACTION

A
  • OPTIMUM pH
    • most function best at NEUTRAL pH 7.0
  • TOO ACIDIC
    • too many HYDROGEN MOLECULES may be collected within the ACTIVE SITE
      • cannot bind effectively to SUBSTRATE
  • TOO ALKALINE
    • can also result in DENATURATION
    • exceptions;
      • STOMACH enzymes; pH 1-2
      • LIVER enzymes; pH 9-10
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13
Q

describe SUBSTRATE CONCENTRATION and its effect on ENZYME ACTION

A
  • SUBSTRATE CONCENTRATION:
    if HIGH
    - SATURATION:
    - substrate CONTINUOUSLY fills the active site of the enzyme
    - MAXIMAL REACTION RATE
    if LOW;
    - NORMAL condition
    - many INACTIVE molecules at any given time
    - SLOWER REACTION RATE

**Increasing concentration does not AFFECT REACTION RATE

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14
Q

what is REGULATION?

A
  • an enormous amount of energy and resources are dedicated to metabolic pathways
  • cells have to REGULATE THE ACTIVITIES of the enzyme very precisely

USAGE OF METHODS;
- COMPETITIVE INHIBITION
- ALLOSTERIC INHIBITION
- ALLOSTERIC ACTIVATION

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15
Q

what is an INHIBITOR?

A

a MOLECULE that attaches to the enzyme and INTERFERES with its ability to do its JOB

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16
Q

describe COMPETITIVE INHIBITION

A
  • where the INHIBITOR COMPETES with the SUBSTRATE for the enzyme’s ACTIVE SITE

TWO TYPES:

REVERSIBLE COMP. INHIBITION
- competition can be OVERCOME by increasing SUBSTRATE CONCENTRATION
- inhibitor can leave

*SULFA DRUGS–type of REVERSIBLE INHIBITOR

IRREVERSIBLE COMP. INHIBITION
- increasing the SUBSTRATE CONCENTRATION DOES NOT OVERCOME the inhibitor

*example–PENICILIN (prevents synthesis of BACTERIAL CELL WALLS–kills BACTERIA–modifies PEPTIDOGLYCAN SYNTHESIS)

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17
Q

describe ALLOSTERIC INHIBITION

A

binding of inhibitor to a site other than the active site called the ALLOSTERIC SITE
- this CHANGES THE SHAPE of the ACTIVE SITE—enzyme can no longer do its job
- is REVERSIBLE

18
Q

describe ALLOSTERIC ACTIVATION

A

helps turn on/ACTIVATE the ENZYME
- ex. oxygen binding to HEMOGLOBIN

19
Q

describe FEEDBACK INHIBITION

A
  • a certain TYPE of ALLOSTERIC INHIBITION
  • stops the cell from MAKING MORE OF A PRODUCT than what is NECESSARY
  • inhibits the FIRST ENZYME in the PATHWAY
  • binds to ALLOSTERIC SITE
20
Q

what are RIBOZYMES?

A
  • identification of RNAs possessing CATALYTIC ACTIVITY
  • RNA SPLICING
21
Q

what are the TWO TYPES OF METABOLIC REACTIONS?

A
  • CATABOLISM
  • ANABOLISM
22
Q

describe CATABOLISM

A
  • BREAKDOWN of complex organic compounds to simpler ones
    • process of HYDROLYSIS
      • breakdown of polymers

EXERGONIC REACTION; produces MORE ENERGY than they consume
- energy + heat

  • provides the ENERGY and BUILDING BLOCKS FOR ANABOLISM
23
Q

describe ANABOLISM

A
  • BUILDING OF complex organic molecules from simpler ones
    • DEHYDRATION SYNTHESIS
      • building polymers
  • consumes energy; ENDERGONIC
24
Q

describe ENERGY PRODUCTION within a cell

A

transfer of ELECTRONS between molecules during CATABOLISM allows cells to transfer and use ENERGY IN INCREMENTAL STEPS (small packages) rather than in a SINGLE BIG BURST

25
describe OXIDATION-REDUCTION/REDOXreactions
where in a REACTION; - one MOLECULE LOSES an ELECTRON (OXIDATION) and another MOLECULE GAINS an ELECTRON (REDUCTION) - COUPLED REACTION CELLULAR OXIDATION REACTIONS; - here we see, an ELECTRON and HYDROGEN are removed at the SAME TIME - these BREAKDOWN COMPLEX ORGANIC MOLECULES --extracts energy from nutrient molecules (STEPWISE MANNER) - traps ENERGY in FORM OF ATP
26
describe ATP
The main ENERGY MOLECULE of the CELL (ADENOSINE TRIPHOSPHATE) - other carrier of energy in living cells (NAD) NAD + e + H = NADH NADP + e + H = NADPH
27
describe how we make ATP
1. SUBSTRATE LEVEL (SLP) - we see an ENZYME TRANSFER a PHOSPHATE from the substrate to ADP **known as PHOSPHORYLATION--addition of phosphate to a molecule 2. OXIDATIVE PHOSPHORYLATION - see the ELECTRON TRANSPORT CHAIN (ETC)--CELLULAR RESPIRATION 3. PHOTOPHOSPHORYLATIOn - process of PHOTOSYNTHESIS; light energy ia converted into CHEMICAL ENERGY in form of ATP and NADH - Synthesizes organic MOLECULES
28
describe CATABOLISM (cont.)
BREAKDOWN of COMPLEX organic compounds to SIMPLER ones - do not want to breakdown complex compounds in ONE REACTION - LARGE amount of energy released would result in LARGE amount of HEAT that would DAMAGE CELLS
29
what is CARBOHYDRATE CATABOLISM?
- our CARBOHYDRATES--primary source of energy - GLUCOSE: most common carbohydrate --must make ENERGY from GLUCOSE through the process of GLYCOLYSIS;
30
describe the process of GLYCOLYSIS
- BREAKDOWN of 6-CARBON GLUCOSE into TWO 3-CARBON PYRUVIC ACIDS (known as PYRUVATE) - has to have an INVESTMENT of 2 ATP to make more - breaking of 6C to 2 x 3C - UNIVERSAL PATHWAY INPUT: 2 ATP OUTPUT/YIELD: 4 ATP 2 NADH NET GAIN: 2 ATP 2 NADH
31
what is an ALTERNATIVE PATHWAY to GLYCOLYSIS (1)?
the ENTER-DOUDOROFF PATHWAY (ED) - similar beginning; glucose --- pyruvate - discovered within PROKARYOTES INPUT: 1 ATP OUTPUT: 2 ATP 1 NADH 1 NADPH NET GAIN: 1 ATP 1 NADH 1 NADPH
32
what is another ALTERNATE PATHWAY for GLYCOLYSIS?
the PENTOSE PHOSPHATE PATHWAY - production of 5 CARBON SUGARS that make up DNA and RNA (EXCESS CARBON SUGARS are FEED BACK TO GLYCOLYSIS) - major source of NADPH - NO ATP IS PRODUCED
33
what are the TWO OPTIONS AFTER GLYCOLYSIS?
- FERMENTATION - RESPIRATION WHY? - we still have a byproduct of PYRUVATE from the process of GLYCOLYSIS--deemed TOXIC; must be broken by one of these options
34
describe CELLULAR RESPIRATION
THREE-STEP PROCESS to complete PROCESSING ENERGY SOURCES: 1. TRANSITION STEP - the OXIDATION of 2 PYRUVATE, which is then turned into 2 ACETYL COA - release of CO2 & 2 NADH - this happens within the MITOCHONDRIA 2. KREBS CYCLE - our 2 ACETYL COA will enter - CO2 is released; TWO CYCLES; 2 ATP 2 FADH 6 NADH 3. ELECTRON TRANSPORT CHAIN - important in terms of helping RECYCLE NADH & FADH - electrons are STORED and TRAVEL with NADH--must END UP SOMEWHERE - ELECTRONS transferred into PROTEIN COMPLEXES + ELECTRON CARRIERS PROTON MODIF FORCE: - this creates a specific PROTON GRADIENT (HYDROGEN)---gradient formed by the accumulation of H+ on the outside of the cell membrane - gradient goes through ATP SYNTHASE--creating ADP into ATP (addition of a P) makes NADH/H+ ---NAD+ (recycled 3 ATP) makes FADH2 ---- FAD+ (recycled 2 ATP)
35
aerobic respiration
- extremely EFFICIENT PROCESS of making ATP - creation of 38 ATP - PROKARYOTES - creation of 36 ATP - EUKARYOTES the BREAKDOWN of GLUCOSE from START to END IN the PRESENCE OF OXYGEN (this is what separates it from ANAEROBIC RESPIRATION)
36
describe FERMENTATION
- PROCESSES PYRUVIC ACID to other less toxic organic molecules --ACTS AS TERMINAL ELECTRON ACCEPTORS-- OXYGEN IS NOT PRESENT--ANAEROBIC TYPE - DOES NOT NEED KREBS CYCLE OR ELECTRON TRANSPORT CHAIN - only ATP generated is through GLYCOLYSIS - only 2 ATP generated TWO TYPES - LACTIC ACID FERMENTATION - ALCOHOL FERMENTATION seen in a lot of common processes; alcohol, acetic acid, cheese products etc..
37
what are the ADDITIONAL SOURCES OF ENERGY?
- sources of energy can come from FATS AND PROTEINS - use of LIPASE: breaks down LIPIDS to GLYCEROL + FATTY ACIDS goes into glycolysis, krebs cycle, and ETC PROTEINS - degraded by EXTERNAL PROTEASES - cuts the protein at SPECIFIC AMINO ACID RESIDUES - broken into SMALLER PEPTIDES - taken into the CELL--broken into INDIVIDUAL AMINO ACIDS--which are then DEAMINATED to REMOVE AMINE GROUP - goes into KREBS CYCLE - can help to IDENTIFY BACTERIA
38
describe ANABOLISM
its BIOSYNTHESIS - the BUILDUP of SMALL MOLECULES into LARGER MOLECULES - makes POLYMERS through process of DEHYDRATION SYNTHESIS - this requires ENERGY
39
use of CHLOROPLASTS
CHLOROPLASTS - where PHOTOSYNTHESIS OCCURS - has a TRIPLE MEMBRANE (outer, inner, and the THYLAKOID) - has the actual PIGMENT CHLOROPHYLL within PROKARYOTES - has INTERNAL FOLDING within PM--has chlorophyll
40
describe the production of energy in LIGHT REACTIONS and DARK REACTIONS
PHOTOPHOSPHORYLATION - has LIGHT REACTIONS (LIGHT DEPENDENT) conversion of LIGHT ENERGY from the SUN into CHEMICAL ENERGY ATP - happens within the THYLAKOID; light hits the chlorophyll sending electrons into the ETC, continues to hit nearby chlorophylls etc... - PRODUCTS: oxygen, NADPH, and ATP PHOTOSYNTHESIS - has DARK REACTIONS (LIGHT DEPENDENT) - makes FOOD for the plant - uses chemical energy ATP to convert CO2 to SUGAR - happens within the STROMA - goes through CALVIN CYCLE--creation of a 3 carbon simple sugar - PRODUCTS: NADP+, GLUCOSE(starch)