Module 10: Biomolecules

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Vocabulary practice flashcards covering enzyme classification, kinetics, mechanisms, and inhibition, alongside nucleic acid structures, replication, transcription, and translation.

38 Terms

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Enzyme

A protein that acts as a biological catalyst to increase reaction rates by up to 102010^{20} times and lower activation energy without being consumed.

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Carbonic anhydrase

An enzyme that catalyses the reaction CO2+H2O→H2CO3CO_2 + H_2O \rightarrow H_2CO_3 to remove carbon dioxide from cells, forming up to 36 million molecules per minute.

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Absolute specificity

The catalytic property where an enzyme will catalyse only one specific reaction of only one substance, such as urease hydrolysing urea.

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Relative specificity

The catalytic property where an enzyme catalyses the reactions of any structurally related substances, such as proteases hydrolysing various proteins.

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Stereochemical specificity

The catalytic property where an enzyme only catalyses reactions of a single 3D stereochemical isomer, such as D-amino acid oxidase reacting only with D-amino acids.

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International Enzyme Commission (IEC) system

A systematic nomenclature scheme that categorises enzymes into six classes based on the reaction catalysed, systematically naming the substrate, the functional group acted on, and the reaction type.

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Active site

The specific 3D region of an enzyme determined by its polypeptide conformation where substrate binding and catalytic reactions occur.

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Enzyme-substrate (E-S) complex

The temporary molecular association formed when a substrate binds to the active site of an enzyme prior to chemical conversion into products.

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<p>Lock-and-key model</p>

Lock-and-key model

A mechanism of enzyme action stating that the active site has a rigid, pre-formed 3D shape that fits only a substrate of the exact corresponding shape.

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<p>Induced-fit model</p>

Induced-fit model

A mechanism of enzyme action stating that the enzyme has a flexible active site that modifies and adapts its conformation to match the shape of the incoming substrate.

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Co-factor

A small non-protein molecule or inorganic ion that an enzyme requires in order to function properly.

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Co-enzyme

An organic non-protein molecule that functions as a co-factor to aid enzyme catalytic activity.

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<p>Apoenzyme</p>

Apoenzyme

The inactive protein component that remains after all co-factors or co-enzymes have been removed from an enzyme.

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Irreversible inhibition

Permanent inhibition in which an inhibitor forms a permanent bond to a specific functional group of an enzyme, permanently stopping its catalytic activity.

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<p>Competitive inhibition</p>

Competitive inhibition

A form of reversible inhibition where an inhibitor with a molecular structure similar to the substrate directly competes with the substrate for binding at the active site.

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<p>Non-competitive inhibition</p>

Non-competitive inhibition

A form of reversible inhibition where an inhibitor binds to a site other than the active site, altering the 3D shape of the enzyme and active site so the substrate can no longer bind.

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Assay

A medical procedure used to quantify the concentration or activity of a specific substance, such as an enzyme, in body fluids for disease diagnosis.

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Nucleotide

The basic monomer unit of nucleic acids, consisting of a heterocyclic nitrogenous base, a monosaccharide, and a phosphate group.

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Pyrimidines

Single-ring heterocyclic amine bases occurring in nucleic acids, specifically cytosine (C), thymine (T), and uracil (U).

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Purines

Two-ring heterocyclic amine bases occurring in nucleic acids, specifically adenine (A) and guanine (G).

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<p>Primary structure of DNA</p>

Primary structure of DNA

The specific linear sequence of heterocyclic bases attached to an alternating sugar-phosphate backbone.

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<p>Secondary structure of DNA</p>

Secondary structure of DNA

The double helix conformation consisting of two anti-parallel nucleotide strands coiled in a right-hand spiral held together by hydrogen bonds between complementary bases.

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<p>Complementary base pairing</p>

Complementary base pairing

The specific hydrogen bonding arrangement in DNA where adenine pairs with thymine via two hydrogen bonds and guanine pairs with cytosine via three hydrogen bonds.

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DNA replication

The process of unwinding the DNA double helix and synthesising two identical daughter DNA molecules using complementary deoxyribonucleotides.

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Replication fork

The Y-shaped active point where the DNA double helix strands begin separating and unwinding, catalysed by helicase.

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Leading strand

The newly synthesized DNA strand formed continuously in the 5′5' to 3′3' direction toward the advancing replication fork.

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Lagging strand

The newly synthesized DNA strand formed discontinuously away from the replication fork as short Okazaki fragments.

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Semiconservative replication

The mechanism of DNA duplication that yields two daughter DNA molecules, each containing one intact parental template strand and one newly formed strand.

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<p>Transcription</p>

Transcription

The process by which RNA polymerase unwinds DNA and links complementary ribonucleotides to synthesize a strand of messenger RNA (mRNA) from a DNA template.

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Messenger RNA (mRNA)

A single-stranded RNA molecule that carries genetic coding information from nuclear DNA to ribosomes in the cytoplasm for protein synthesis.

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Ribosomal RNA (rRNA)

The structural RNA that constitutes approximately 65%65\% of a ribosome's mass.

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Transfer RNA (tRNA)

An RNA molecule responsible for delivering specific amino acids from the cytoplasm to the ribosome to assemble growing polypeptide chains.

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Codon

A sequence of three consecutive nucleotide bases on mRNA that specifies a particular amino acid or serves as a translational stop signal.

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Stop codon

One of three specific mRNA base triplets (UAG, UAA, or UGA) that do not code for any amino acid and signal the termination of translation.

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Translation

The cellular process wherein the genetic code transcribed onto mRNA is decoded at ribosomes to assemble amino acids into a polypeptide chain.

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Peptidyl site (P-site)

The binding site on a ribosome that holds the tRNA attached to the growing peptide chain during translation.

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<p>Aminoacyl site (A-site)</p>

Aminoacyl site (A-site)

The binding site on a ribosome where an incoming tRNA carrying the next required amino acid enters and aligns with its codon.

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Mutation

A permanent change in the DNA base sequence that occurs at an approximate natural rate of one in every 101010^{10} replicated bases.