Year 12 Biology

5 carbon atoms.

The hindrance of an enzyme by binding to an allosteric site, changing the shape of the active site to prevent substrate binding.

Ribonucleic acid, a single strand of nucleotides.

Short single-stranded chains of nucleotides that are complementary to the template strand.

A reaction where two or more smaller molecules combine to form a larger one, gaining energy.

The reactant undergoing an enzyme-facilitated reaction.

trpE, trpD, trpC, trpB, and trpA.

They usually occupy the active site of an enzyme and are classified as competitive inhibitors.

RNA is single stranded.

DNA and RNA.

Enzymes frequently team up to catalyze reactions continuously.

The section of DNA just upstream of the coding region and downstream of the promoter and operator.

The process where different exons may be spliced, resulting in a single gene producing multiple different mRNA strands.

It allows a single gene to give rise to many different mRNA strands and code for many different proteins.

In a 5' to 3' direction.

A reaction where a larger molecule breaks down into two or more smaller molecules, losing energy.

The pocket-like area where the substrate binds.

By bringing reactants closer to the state they need to be in to react.

A regulatory gene located upstream.

A series of reactions where one enzyme catalyzes a substrate into a product.

It plays a critical role in regulating gene expression in prokaryotes.

Disulphide bonds.

They are chemical messengers used to communicate and induce changes in cells.

The process whereby a sequence of DNA is used as a template to produce a complementary sequence of mRNA.

A phosphate group, a five-carbon sugar, and a nitrogenous base.

RNA contains ribose sugar instead of deoxyribose and uses uracil instead of thymine.

A cluster of linked genes that share a common promoter and operator and are transcribed at the same time.

The process where a sequence of DNA is used as a template to produce a complementary sequence of mRNA.

Molecules need to collide with enough kinetic energy.

Deoxyribonucleic acid (DNA) and ribonucleic acid (RNA).

The expression of structural genes coding for proteins involved in the production of the amino acid tryptophan.

The process of cutting out introns and joining exons in pre-mRNA.

They receive signals from the environment.

Polymers of nucleotide monomers.

Acetylcholine receptors and hormone receptors.

Unbonded nucleotides on the ends of the DNA strand resulting from a staggered cut.

Initiation, elongation, and termination.

It provides the rules for how genetic information is transcribed and translated into functional proteins.

To speed up biochemical reactions by lowering activation energy.

It involves reading and converting the information in the mRNA molecule into a polypeptide chain.

The reaction rate will increase.

Pathways where the amount of product is controlled by one enzyme within the pathway.

Into groups of three.

The result of a straight cut across double-stranded DNA by an endonuclease, resulting in no overhanging nucleotides.

A series of enzyme-catalyzed biochemical reactions where the product of one reaction becomes the substrate of the next.

It acts as a limiting factor or limiting reagent.

It undergoes a conformational change.

Entirely within the nucleus.

A change in the 3D shape of macromolecules such as proteins.

Replication or amplification of DNA.

The process where an mRNA sequence is read to produce a corresponding amino acid sequence to build a polypeptide.

Formed when 2 or more polypeptide chains with tertiary structure join together.

The immediate product of transcription of a DNA sequence that requires modifications before translation.

The production of functional gene products such as proteins or non-coding strands of RNA.

Polypeptides.

A protein signaling molecule that regulates physiological behavior.

Enzyme activity is affected by temperature; too much heat can cause denaturation and stop functioning.

A protein produced by plasma cells during immune response that is specific to an antigen and combats pathogens.

It can disrupt the pathway by non-competitively and reversibly inhibiting an enzyme, halting its function.

Monomers.

The content of this page is not provided, so specific details cannot be summarized.

The modification of pre-mRNA into mRNA for translation.

Disulphide bonds between cysteine amino acids.

Blood sugar levels.

Transcription of structural genes necessary for tryptophan synthesis is prevented.

It occurs when all enzyme active sites are continuously occupied by substrate molecules.

A sequence of amino acids, ultimately forming a polypeptide chain.

The amino acid methionine.

The enzyme that removes introns and joins exons during RNA processing.

They are essential coenzymes in cellular energy transfer.

Chemical reactions speed up due to greater kinetic energy of molecules.

ATP loses a phosphate group and becomes ADP.

Transcription of genes.

It stabilizes the mRNA molecule and prevents degradation.

Organic (carbon-based) molecules.

A non-protein group bound to a protein, such as a vitamin or ion.

It may lead to an accumulation of Substrate 1, necessitating the recommencement of the pathway.

Different codons (3 bases) correspond to different amino acids.

The process where an mRNA sequence is read to produce a corresponding amino acid sequence to build a polypeptide.

Deoxyribose (DNA) and Ribose (RNA).

They assist enzymes in catalyzing reactions.

The enzyme can no longer catalyze its specific reaction or its function is greatly reduced.

To carry genetic information and synthesize proteins.

Higher enzyme concentrations lead to higher reaction rates due to more available active sites.

Breaks down starch into maltose.

A region on an enzyme that is not the active site.

The initial amount of energy required for a chemical reaction.

It stabilizes mRNA and allows binding to ribosomes during translation.

It causes specific folding of the mRNA via hydrogen bonds, forming a terminator hairpin loop.

Serves as the main structural component of ribosomes within cells.

Inhibitors form strong, unbreakable bonds with enzymes, preventing them from binding with substrates or catalyzing reactions indefinitely.

The ribosome pauses due to the absence of tRNA-bound tryptophan.

A form of bulk transport and active transport.

An enzyme-substrate complex.

They regulate the production of specific products based on the body's requirements.

They are involved in the immune system by recognizing and destroying pathogens.

1. Vesicle is transported to the plasma membrane. 2. Vesicle membrane fuses with plasma membrane. 3. Secretory products are released into the extracellular environment.

They act as organic catalysts that lower the activation energy of reactions.

RNA that is a key structural component of ribosomes, which assemble proteins.

A common promoter and operator.

It changes the shape of the active site, preventing substrate binding.

At the same time.

A primer.

Transcription and translation.

Carries genetic information from the nucleus to the ribosomes for protein synthesis.

Two tryptophan amino acids.

Delivers specific amino acids to the ribosome after recognizing specific nucleotide sequences on mRNA.

A sequence of three nucleotides coding for one amino acid.

Non-coding regions of DNA that do not code for proteins.

Increases heart rate and expands airways.

A sequence of three nucleotides coding for one amino acid.

It exits the nucleus through a nuclear pore and travels to a ribosome in the cytosol or attached to the rough endoplasmic reticulum.

The process by which contents of a vesicle are released from a cell.

20 amino acids.

No, not all proteins will have a Quaternary structure.

The result of a staggered cut through double-stranded DNA by an endonuclease, resulting in overhanging nucleotides.

The type of sugar molecule present.

Transcription, RNA processing, and Translation.

All the proteins that are expressed by a cell or organism at a given time.

The termination of translation.

DNA forms double strands, while RNA forms single strands.

Temperature, pH, or enzyme concentration.

Catalase.

A sequence of three nucleotides in mRNA that signals the end of translation.

Polymerases add nucleotides to DNA or RNA, leading to the copying of entire genes.

Promoter region, introns, exons, termination sequences, and operator regions.

Catalyzes the formation of mRNA from DNA.

RNA polymerase moves along the DNA template, adding complementary RNA nucleotides to form pre-mRNA.

The breakdown of bonds that create tertiary and quaternary structures, causing loss of function.

The 3D structure of the protein.

A group of multiple structural genes controlled by a single promoter and operator.

The arrangement of multiple polypeptide chains.

RNA polymerase can move downstream, allowing for transcription of the gene.

A symmetrical, bell-shaped curve.

To carry genetic information from the nucleus to the ribosomes.

The reaction rate remains constant, resulting in a plateau.

The nitrogenous bases present.

DNA is copied into pre-mRNA.

To speed up chemical reactions by reducing activation energy.

A sequence of three nucleotides in mRNA that signals the start of translation.

36 - 38°C.

Through a process called phosphorylation, where a phosphate group is added.

The point at which the maximum function of an enzyme occurs.

A reaction where two monomers join to form a larger molecule, producing water as a by-product.

The chain of amino acids.

They inhibit or decrease the expression of structural genes.

Each strand runs in opposite directions; one runs 3' to 5' and the other runs 5' to 3'.

Yes, enzymes can regain functionality when reheated as significant denaturation does not occur at low temperatures.

A tough protein found in skin, hair, and nails.

They become inactive.

It is involved in the production of the amino acid tryptophan, which is used in protein production.

Sticky ends and blunt ends.

They create a staggered cut with overhanging, unpaired nucleotides.

Regions of DNA that code for proteins and are retained during RNA processing.

It continues along the DNA template.

An energy input.

When high levels of tryptophan are present.

Ligases are enzymes that join two fragments of DNA or RNA together by catalyzing the formation of phosphodiester bonds.

It inhibits tryptophan synthesis, conserving energy for the cell.

It enables the membrane to fuse with vesicles.

Storage of iron.

Reversible inhibitors bind weakly and can be removed, while irreversible inhibitors form strong bonds that cannot be broken.

A short, single strand of nucleic acids that acts as a starting point for polymerase enzymes to attach.

Over 1,000 times daily.

'TATAAA', known as the TATA box.

They slow down the reactions but do not permanently stop them.

Reversible inhibitors bind weakly and impair temporarily, while irreversible inhibitors bind strongly and impair permanently.

The control of gene expression, typically by switching transcription on or off.

It serves as the binding site for repressor proteins to inhibit gene expression.

Optimal pH of 8.

They ensure that an inserted gene is oriented correctly when manipulating DNA.

Molecules that block an enzyme's active site, preventing substrate binding.

They maintain cellular homeostasis by regulating biochemical pathways.

They bind to a site other than the active site, causing a conformational change that prevents substrate binding.

Metabolic pathway.

Proteins that influence the expression of structural genes.

Transcription of the trp structural genes is started to increase tryptophan availability.

A chain of amino acids linked together.

It binds to the operator region to block RNA polymerase when tryptophan levels are high.

Ribosomes, rough endoplasmic reticulum, Golgi apparatus, and transport and secretory vesicles.

An organic molecule, typically a protein, that catalyzes specific reactions.

By increasing substrate concentration, which increases the chances of substrate binding to the enzyme.

Substances that block an enzyme’s active site.

Increased tryptophan production is facilitated.

Kinetic energy increases, leading to more enzyme-substrate complexes.

The functional 3D shape of a protein formed by further folding of secondary structures.

Extreme conditions such as high temperatures or extreme pH levels.

The bonding of multiple polypeptide chains together.

Optimal pH around 1.5 – 2.

They cut in the middle of the recognition site, resulting in a straight cut with no overhanging nucleotides.

An antiterminator hairpin loop.

A phosphate group, a five-carbon sugar, and a nitrogen-containing base.

A molecule that is the smallest building block of a polymer.

They produce proteins involved in the structure or function of a cell, such as enzymes and transport proteins.

Initiation, elongation, and termination.

The phosphate of the following nucleotide.

A process where transcription begins but is stopped early before proteins are made, in response to tRNA-bound tryptophan.

To move large molecules or groups of molecules into or out of the cell.

At the end of the leader region of the trp operon.

Enzyme concentrations are usually lower than substrate concentrations.

It is processed into mRNA, which carries the message for protein synthesis.

By complementary base pairs.

They can remain in the cell for use or be exported out of the cell via exocytosis.

Enzyme activity sharply declines until denaturation causes complete loss of function.

A segment of DNA responsible for producing proteins that control the expression of other genes.

EcoRI.

To recognize specific codons on the mRNA strand and add the corresponding amino acid to the polypeptide chain during protein synthesis.

They work together to enable muscle contractions.

The nitrogenous base.

Enzymes are specific, not used up in reactions, can work in both directions, and can catalyze each step of metabolic pathways.

The chemical properties of each R group.

They lower the activation energy.

A point may be reached where all substrates are utilized, leading to a decrease in reaction rate.

Another term for non-competitive inhibition, where an inhibitor binds to an allosteric site.

The process where coenzymes are recycled after assisting in reactions by accepting more energy.

Yes, it can be reused to produce more polypeptides.

Formation of alpha-helices and beta-pleated sheets through hydrogen bonds between amino acids.

Enzyme activity slows until freezing occurs, causing reversible loss of function.

Restriction endonuclease digestion.

A short region of DNA that interacts with repressor proteins to alter the transcription of an operon.

The 5’ end of mRNA binds to the ribosome; the start codon (AUG) is recognized; tRNA with anticodon (UAC) delivers methionine.

Because both the substrate and inhibitor compete for binding to the active site.

They are complementary in shape.

An organic molecule, typically a protein, that catalyzes (speeds up) specific reactions.

The stop codon on mRNA.

The chemical bond linking two amino acids.

It is released by the ribosome into the cytosol or endoplasmic reticulum.

Primary, Secondary, Tertiary, and Quaternary.

Channel proteins and carrier proteins.

Hydrophobic proteins.

A mechanism for gene regulation that stops transcription when tryptophan levels are high.

Regions of coding DNA that are transcribed and translated into the final protein.

An enzyme that cuts strands of DNA by breaking the phosphodiester bond between nucleotides.

It prevents gene expression by binding to its operator.

To prevent overproduction of products within the pathway.

A large molecule made up of small, repeated monomer subunits.

Downstream (towards the 3’ end) of the regulatory gene that controls them.

Coenzymes are organic, non-protein molecules that assist enzyme function.

Polypeptide chains or proteins.

RNA polymerase synthesizes RNA from a DNA template.

Consists of two strands of nucleotides bonded together via complementary base pairing.

Two consecutive trp codons.

Regions of non-coding DNA that are removed during RNA processing.

The end of transcription.

A process that causes irreversible loss of function due to conformational changes.

No, operator regions are typically only found in prokaryotic genes.

Increasing substrate concentration while keeping enzyme concentration constant increases reaction rate.

DNA ligase (joins DNA fragments) and RNA ligase (joins RNA fragments).

A molecule that assists enzyme functioning, which can be organic or inorganic.

Primary, Secondary, Tertiary, and Quaternary.

It prevents mRNA dissociation from the template strand.

The phosphate group of the nucleotide.

At a cell's ribosomes via condensation reaction, forming peptide bonds.

Waste, preventing toxin build-up.

Polypeptides or proteins.

The sequence of amino acids in a polypeptide chain.

The wider range of conditions under which an enzyme can function effectively.

The process of reading the information stored within a gene to create a functional product, typically a protein.

Endonucleases that target specific recognition sites on DNA.

AluI.

A central carbon atom, carboxyl group, amino group, an R-group, and a hydrogen atom.

It reduces the availability of Substrate 2 for the subsequent reaction catalyzed by Enzyme 2, regulating the production rate of Substrate 3.

Transcription factors bind to the promoter region, and RNA polymerase binds to initiate transcription.

Regulatory proteins such as repressor and activator proteins.

It continues transcribing the structural genes for tryptophan synthesis.

Alpha helix and beta sheet.

DNA polymerase synthesizes a new DNA strand from nucleotides.

Non-competitive inhibitors bind elsewhere and alter the structure of the active site.

Each polypeptide chain is folded and modified into a fully functional protein.

It inhibits transcription by preventing RNA polymerase from moving downstream.

The polypeptide chains must fold correctly into shape.

Even though they are genetically identical, they produce different proteins based on their specific functions.

Extreme pH levels can lead to denaturation of enzymes.

The sequence of DNA to which RNA polymerase binds.

mRNA is fed through the ribosome; codons are matched to tRNA anticodons; tRNA delivers amino acids, forming peptide bonds.

'Loaded' ATP carries three phosphate groups, while 'unloaded' ADP has two phosphate groups.

Enzymes can denature, leading to a conformational change in the active site.

It serves as a binding site for RNA polymerase to initiate transcription.

A protein signaling molecule that regulates physiological behavior.

The termination sequence of a gene.

Enzymes move slower, collide less frequently, and may experience little to no activity.

The active site is blocked by the inhibitor, preventing the substrate from binding.

In prokaryotes, transcription occurs directly in the cytoplasm, while in eukaryotes, it occurs in the nucleus.

They assist enzyme functioning and must be recycled after undergoing a reaction.

A segment of DNA that codes for proteins involved in the structure or function of a cell or organism.

A specific target sequence of DNA where restriction endonucleases act.

Reaction rate increases with increasing enzyme concentration until reaching a plateau.

Pathways where the amount of product is controlled by the inhibition of enzymes.

The coenzyme binds to the active site, donates energy or molecules, and is changed but not immediately reused.

Control the entry and exit of substances from a cell.

There is no inhibition due to tryptophan abundance.

They initiate or increase the expression of structural genes.

Support cell and tissue shape.

No, prokaryotic genes do not contain introns.

In elastic connective tissues such as the skin.

A protein found in connective tissues such as the skin.

It increases the reaction rate up to a certain point.

It increases gene expression.