Enzymes and Catalysis

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Questions and Answers

In the context of enzymatic reactions, which of the following scenarios would LEAST favour an increase in reaction velocity?

  • Elevating the substrate concentration to a point significantly exceeding the enzyme's $K_m$ value.
  • Increasing the concentration of a competitive inhibitor while maintaining constant substrate concentration. (correct)
  • Increasing the temperature within the enzyme's optimal range, provided substrate is not limiting.
  • Introducing a cofactor that enhances the conformational fit of the substrate to the active site.

An enzyme subjected to non-competitive inhibition retains its capacity to bind the substrate with unaltered affinity, but its catalytic efficiency is compromised.

True (A)

Describe the mechanistic implications of an enzyme exhibiting 'ping-pong' kinetics, with particular attention to the role of modified enzyme intermediates during the reaction coordinate.

Ping-pong kinetics involve an enzyme mechanism where one or more substrates bind to the enzyme, releasing one or more products before any other substrates bind. This results in a modified form of the enzyme that is then involved in the subsequent steps of the reaction.

In enzyme kinetics, the turnover number, often denoted as $k_{cat}$, signifies the ______ under saturating conditions, reflecting the enzyme's maximal catalytic efficiency.

<p>number of substrate molecules converted per enzyme molecule per unit time</p> Signup and view all the answers

Match the following regulatory mechanisms with their specific effects on enzyme activity:

<p>Allosteric Activation = Enhances enzyme activity by binding a modulator. Competitive Inhibition = Reduces enzyme activity by blocking substrate binding. Covalent Modification (Phosphorylation) = May either activate or inhibit enzyme activity depending on the specific enzyme. Feedback Inhibition = Inhibits an enzyme in a metabolic pathway by the end product of that pathway.</p> Signup and view all the answers

Which statement accurately differentiates between anabolic and catabolic biochemical pathways?

<p>Anabolic pathways consume energy to synthesize complex molecules from simpler precursors, whereas catabolic pathways liberate energy by breaking down complex molecules. (C)</p> Signup and view all the answers

In the induced fit model of enzyme-substrate interaction, the enzyme's active site remains perfectly rigid and complementary to the substrate throughout the binding process, ensuring optimal specificity.

<p>False (B)</p> Signup and view all the answers

Explain the thermodynamic basis for why enzymes are capable of accelerating biochemical reactions, with specific reference to the transition state theory and the Arrhenius equation.

<p>Enzymes accelerate reactions by stabilizing the transition state, which effectively lowers the activation energy ($E_a$). According to the Arrhenius equation ($k = Ae^{-E_a/RT}$), a decrease in $E_a$ results in an exponential increase in the rate constant ($k$), thereby increasing the reaction rate.</p> Signup and view all the answers

The phenomenon where an enzyme's catalytic activity is modulated by the binding of a molecule to a site other than the active site is termed ______ regulation.

<p>allosteric</p> Signup and view all the answers

Match the following descriptions to the correct type of enzyme inhibition:

<p>Competitive Inhibition = Inhibitor binds only to the active site. Uncompetitive Inhibition = Inhibitor binds only to the enzyme-substrate complex. Noncompetitive Inhibition = Inhibitor binds to either the enzyme or the enzyme-substrate complex with equal affinity. Mixed Inhibition = Inhibitor binds to either the enzyme or the enzyme-substrate complex, but not with equal affinity.</p> Signup and view all the answers

Considering the implications of extreme pH values on enzyme structure and function, which of the following statements accurately describes the molecular mechanism of pH-induced denaturation?

<p>Extreme pH values alter the ionization state of amino acid residues, disrupting ionic and hydrogen bonds that stabilize the tertiary structure. (C)</p> Signup and view all the answers

An enzyme's optimal temperature is invariably situated marginally below its point of thermal denaturation, ensuring maximal activity while precluding structural compromise.

<p>False (B)</p> Signup and view all the answers

Explain the role of cofactors and coenzymes in enzyme catalysis, differentiating between their binding affinities and chemical contributions to the reaction mechanism.

<p>Cofactors (metal ions or coenzymes) bind to enzymes to facilitate catalysis. Metal ions typically bind tightly and provide structural support or participate in redox reactions. Coenzymes (organic molecules, often derived from vitamins) can bind loosely or tightly; they act as carriers of chemical groups or electrons during the reaction.</p> Signup and view all the answers

In the context of DNA replication, the enzyme responsible for alleviating torsional stress ahead of the replication fork by inducing transient breaks in the DNA backbone is known as ______.

<p>topoisomerase</p> Signup and view all the answers

Match each DNA replication enzyme with its primary function:

<p>Helicase = Unwinds the DNA double helix at the replication fork. Primase = Synthesizes RNA primers to initiate DNA synthesis. DNA Polymerase = Catalyzes the addition of new nucleotides to the growing DNA strand. Ligase = Joins Okazaki fragments on the lagging strand by forming phosphodiester bonds.</p> Signup and view all the answers

Given the semi-conservative nature of DNA replication, what outcome would MOST reasonably be expected following three rounds of replication initiated from a single double-stranded DNA molecule?

<p>Half of the DNA molecules will contain one original strand and one new strand, while the other half will consist entirely of newly synthesized strands. (C)</p> Signup and view all the answers

The exclusive function of DNA ligase is to rectify mismatched base pairs arising during DNA replication, thereby ensuring genomic fidelity.

<p>False (B)</p> Signup and view all the answers

Describe the mechanism by which exonuclease activity contributes to the fidelity of DNA replication, with specific reference to the 3'-to-5' and 5'-to-3' exonuclease activities of DNA polymerase I in E. coli.

<p>The 3'-to-5' exonuclease activity of DNA polymerase I acts as a proofreading function, removing incorrectly incorporated nucleotides from the 3' end of the growing strand. The 5'-to-3' exonuclease activity removes RNA primers and replaces them with DNA.</p> Signup and view all the answers

During DNA replication, ______ are short sequences of DNA synthesized on the lagging strand, which are subsequently joined together by DNA ligase.

<p>Okazaki fragments</p> Signup and view all the answers

Match the following components with their roles during protein synthesis:

<p>mRNA = Carries the genetic code from the DNA to the ribosome. tRNA = Transports amino acids to the ribosome for protein assembly. Ribosome = The site of protein synthesis; facilitates the binding of tRNA and mRNA. Aminoacyl-tRNA synthetase = Enzyme that charges tRNA molecules with their corresponding amino acids.</p> Signup and view all the answers

In considering the central dogma of molecular biology, which molecular process is MOST directly affected by the presence of non-coding introns within a pre-mRNA transcript?

<p>Post-transcriptional modification and splicing. (A)</p> Signup and view all the answers

The presence of a stop codon (UAA, UAG, or UGA) in the mRNA transcript directly recruits a tRNA molecule charged with a specific amino acid to terminate translation.

<p>False (B)</p> Signup and view all the answers

Delineate the mechanistic differences between Rho-dependent and Rho-independent transcription termination in prokaryotes, emphasizing the structural elements involved and the energetic requirements of each process.

<p>Rho-dependent termination involves the Rho protein binding to the mRNA and moving towards the RNA polymerase, causing it to dissociate from the DNA template. Rho-independent termination relies on the formation of a hairpin loop structure in the mRNA, followed by a string of uracil residues, which causes the RNA polymerase to stall and dissociate.</p> Signup and view all the answers

The initiation of translation in eukaryotes typically begins with the binding of the initiator tRNA carrying ______ to the start codon AUG.

<p>methionine</p> Signup and view all the answers

Match each of the following terms related to gene expression with its description:

<p>Promoter = A region of DNA where RNA polymerase can bind to initiate transcription. Enhancer = A DNA sequence that can increase the transcription of a gene, often located far from the promoter. Silencer = A DNA sequence that can decrease the transcription of a gene. Transcription Factor = A protein that binds to specific DNA sequences, controlling the rate of transcription.</p> Signup and view all the answers

Concerning the regulation of gene expression, which epigenetic mechanism would MOST directly impact the accessibility of DNA for transcriptional machinery?

<p>DNA methylation patterns. (B)</p> Signup and view all the answers

Eukaryotic gene expression exclusively relies on transcriptional control mechanisms, precluding any significant roles for post-translational modifications in regulating protein activity.

<p>False (B)</p> Signup and view all the answers

Describe the functional consequences of histone acetylation and deacetylation on gene expression, with specific reference to the enzymes involved and the resulting chromatin structure.

<p>Histone acetylation (catalyzed by histone acetyltransferases, HATs) leads to a more open chromatin structure (euchromatin) and increased gene expression by neutralizing the positive charge of histones. Histone deacetylation (catalyzed by histone deacetylases, HDACs) leads to a more condensed chromatin structure (heterochromatin) and decreased gene expression.</p> Signup and view all the answers

In the context of eukaryotic cells, the ______ refers to the overall structural organization of chromatin, which can impact gene expression by influencing the accessibility of DNA.

<p>epigenome</p> Signup and view all the answers

Match the following terms related to the Lac Operon with their description:

<p>lacZ = Encodes β-galactosidase, which cleaves lactose into glucose and galactose. lacY = Encodes lactose permease, which facilitates the transport of lactose into the cell. lacA = Encodes transacetylase, which transfers an acetyl group to β-galactosides. lacI = Encodes the Lac repressor protein, which inhibits transcription of the operon in the absence of lactose.</p> Signup and view all the answers

Within the framework of the lac operon, what would be the MOST immediate consequence of a loss-of-function mutation in the gene encoding the LacI repressor protein?

<p>Constitutive expression of the lac operon, irrespective of lactose availability. (D)</p> Signup and view all the answers

The catabolite activator protein (CAP) exerts its positive control over the lac operon solely by directly binding to the lac operator, occluding RNA polymerase binding in the of glucose.

<p>False (B)</p> Signup and view all the answers

Explain the regulatory mechanisms involved in attenuation of the trp operon in E. coli, emphasizing the role of the leader peptide and the ribosome in modulating transcription termination.

<p>Attenuation of the trp operon involves a leader sequence that encodes a short peptide with tryptophan residues. If Trp levels are high, the ribosome translates the leader peptide rapidly, causing a terminator hairpin to form, stopping transcription. If Trp levels are low, the ribosome stalls, allowing an antiterminator hairpin to form, which allows transcription to continue.</p> Signup and view all the answers

In the absence of lactose, the LacI repressor protein binds to the ______ region of the lac operon, thereby preventing RNA polymerase from initiating transcription.

<p>operator</p> Signup and view all the answers

Flashcards

Enzymes

Biological catalysts that speed up reactions by lowering activation energy. They are not used up in the reaction and are reused many times.

Anabolic Reactions

Reactions that build complex molecules from simple ones.

Catabolic Reactions

Reactions that break down complex molecules into simple ones.

Induced Fit Model

Substrate binds weakly, inducing an enzyme shape change. Active site becomes more complementary.

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Competitive Inhibition

Inhibitor similar to substrate occupies active site, preventing substrate binding.

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Non-Competitive Inhibition

Inhibitor binds at allosteric site, causing enzyme shape change and denaturing it.

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Temperature Effect on Enzymes

Rate increases with temperature, but too high denatures the enzyme.

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pH Effect on Enzymes

Outside viable range causes denaturing.

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Co-factors role

Modify enzyme shape to ensure active site is complementary.

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DNA

Double-stranded polymer of repeated nucleotides. Nucleotides are made of a phosphate group, deoxyribose sugar, and a nitrogenous base.

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DNA Base Pairings

A-T, C-G

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Helicase

Enzyme that breaks hydrogen bonds between base pairs to unzip DNA.

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Primase

Allows DNA replication to begin

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DNA Polymerase

Attaches new DNA bases to template strands, proofreading and correcting.

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Exonuclease

Removes RNA primers and refills gaps with DNA.

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Ligase

Rejoins strands into a double helix by attaching sugar-phosphate backbone.

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Semi-Conservative Replication

One strand is original, one is new.

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Gene

Section of DNA which codes for a specific protein.

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Transcription

RNA polymerase moves along the template strand and adds complementary mRNA bases (Uracil instead of thymine).

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Genetic Code

Each triplet (codon) codes for a specific amino acid.

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tRNA Function

tRNA brings amino acids to the ribosome.

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Protein folding

Polypeptide folds to produce a protein

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Gene Expression

Process that determines which genes are transcribed and when genes are expressed.

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Epigenetic Tags

Environmental factors affecting gene expression.

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Histones Role in Eukaryotes

Unnecessary genes are wrapped tightly around histones

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Operon

A set of genes with a promoter, coding for a specific enzyme.

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Lac Operon Function

Breaks down lactose to form glucose.

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Lactose absent effect on lac operon

The RNA polymerase joins to the promoter, but cannot transcribe lacZ, lacY or lacA, so no enzymes are made

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Lactose present effect on lac operon

When lactose is present, it binds to the repressor, causing a conformational change.The repressor detaches from the operator

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LacI

LacI codes for the production of the repressor

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LacZ

LacZ codes for lactase

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Study Notes

Enzymes

  • Enzymes serve as biological catalysts
  • They facilitate alternative reaction pathways with reduced activation energy
  • This enhances the reaction rate, making life-sustaining reactions viable
  • Enzymes remain unchanged and reusable throughout reactions
  • Enzymes catalyze anabolic reactions (simple to complex)
  • Enzymes catalyze catabolic reactions (complex to simple)
  • Enzymes catalyze complex reaction pathways

Induced Fit Model

  • Substrate weakly binds to the enzyme's active site
  • The active site becomes more complementary
  • This initiates conformational changes in the enzyme's shape

Inhibition

  • Competitive inhibition occurs when an inhibitor, resembling the substrate, occupies the active site
  • This prevents the substrate from binding
  • Competitive inhibition is temporary or permanent, and can be overcome by increasing substrate concentration
  • Non-competitive inhibition involves the inhibitor binding to an allosteric site
  • Non-competitive inhibition causes a conformational change in the enzyme and its active site
  • The substrate is no longer complementary to the active site
  • The enzyme is permanently denatured in non-competitive inhibition

Factors Affecting Enzyme Function

  • Increased temperature leads to an increased reaction rate, but excessively high temperatures denature the enzyme
  • Denaturing occurs outside the viable pH range
  • Each enzyme has an optimum pH range that varies
  • Substrate and enzyme concentration: concentration increases to a plateau
  • Other concentration becomes limiting

Co-factors

  • Certain enzymes require co-factors to function
  • Co-factors modify the enzyme shape to ensure the active site is complementary
  • Inorganic co-factors predominantly consist of metal ions
  • Organic co-enzymes are mainly vitamins

DNA Replication

  • DNA is a double-stranded polymer of repeated nucleotides
  • Nucleotides consist of a phosphate group, deoxyribose sugar (pentose), and nitrogenous bases
  • A-T and C-G represent complementary base pairings
  • Adenine, Thymine, Cytosine, and Guanine are bases
  • Nucleotides split into triplets or codons, which code for an amino acid
  • Helicase disrupts hydrogen bonds between base pairs, unzipping the DNA into a replication fork and producing two template strands
  • Primase synthesizes RNA primase, which initiates DNA replication
  • DNA polymerase attaches new DNA bases to the template strands, elongates them, and proofreads/corrects errors
  • Exonuclease eliminates RNA primers, and polymerase refills gaps with DNA
  • Ligase rejoins strands into a double helix by connecting the sugar-phosphate backbone
  • DNA Replication is semi-conservative: one strand is original, while the other is new

Protein Synthesis/Gene Expression

  • DNA encodes proteins by sections known as genes
  • Genes code for specific proteins
  • Proteins are either structural or globular
  • RNA polymerase moves along the template strand
  • Complementary mRNA bases are added
  • NB uracil, not thymine
  • Strands separate just ahead and closes just behind to avoid exposing DNA
  • mRNA exits the nucleus via nuclear pores and relocates to the ribosome
  • Non-coding introns are excised from the DNA to produce mature RNA (spliceosome)

Translation

  • Each triplet/codon specifies an amino acid
  • tRNA transports amino acids from the cytoplasm to the ribosome
  • tRNA possesses an anticodon matching triplets; it binds only to a specific amino acid
  • Once a base is brought, the ribosome proceeds to link amino acids together with a peptide bond
  • Polypeptide chain folds to produce a protein, occurs in endoplasmic reticulum
  • Translation commences with an AUG (methionine) codon
  • Translation terminates with stop codons (UAA, UAG, UGA)

Gene Expression

  • Gene expression dictates which genes undergo transcription
  • Gene regulation determines the timing of gene expression
  • This process ensures only relevant genes are active in a cell
  • Regulated by metabolic, environmental, and physiological factors
  • Gene expression does not alter the DNA sequence
  • Epigenetic tags influence the selection of genes for expression

Eukaryotic Cells

  • Epigenome constitutes the secondary structure of DNA
  • Unnecessary genes are tightly wrapped around histones
  • Necessary genes are relaxed and exposed for transcription
  • Environmental factors influence epigenetic tags
  • Gene expression guides cell differentiation from stem cells

Prokaryotic Cells - Lac Operon

  • An operon is a set of genes with a promoter that code for a specific enzyme
  • The lac operon facilitates lactose breakdown to form glucose
  • Lactase enzyme production is contingent upon the presence of lactose
  • If there is no lactose, the repressor attaches to the operator
  • RNA polymerase binds to the promoter, but cannot transcribe lacZ, lacY, or lacA, thus preventing enzyme synthesis
  • When lactose is available, it binds to the repressor, inducing a conformational shift
  • The repressor detaches from the operator
  • RNA polymerase transcribes lacZ, lacY, and lacA, resulting in enzyme production
  • LacI codes for the repressor production
  • LacZ codes for lactase
  • LacY enhances membrane permeability to facilitate lactose entry
  • LacA codes for a supporting enzyme

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