Biochemistry - Key Terms

PTM - Post Translational Modification umol = 1/1000 mmol
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Last updated: November 12, 2024
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First submittedNovember 12, 2024
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Chemical modification to the enzyme to increase/decrease activity (e.g phosphorylation, ubiquitinylation)
Covalent control
Reaction involving the changing of position of atoms and functional groups in a molecule
Rearrangement
Enzymatic reaction where 2 molecules are joined with the loss of water
Condensation
What occurs from a single gene but resulting from PTMs/splice variants etc
Isoforms
What occurs from different genes generating different proteins?
Isoenzymes
A reaction pathway which continues in a straight path
Linear
What is the most common covalent modification, which occurs often at Ser/Thr/Tyr residues?
Phosphorylation
Maximal rate at substrate saturation (expressed as rate of substrate conversion)
Vmax
If two enzymes (1: Low Km, 2: High Km) at a metabolic branch point are competing for the same substrate, which one will preferably bind to the substrate?
1
Reaction involving replacement of one group with another
Substitution
Enzyme activity per mg of protein (measures purity)
Specific activity
Which method do eukaryotic cells use utilizing organelles to create specialised areas within the cell?
Compartmentalization
Inhibitors which bind at the active site using a covalent bond and denature the enzyme permanently.
Irreversible
Enzymatic reaction where 2 molecules are joined together but water is not eliminated, can also happen across a double bond
Addition
Dual oxidation and reduction reactions normally involving Co-Enzymes
Redox
Reaction involving transfer of a functional group to a substrate
Transfer
Inhibitors which do not change the structure of the enzyme and bind to the active or regulatory domains.
Reversible
A reaction pathway which splits
Branched
Amount of enzyme which converts 1mole of S to P per min
Kat
Enzymatic reaction where a molecule can be split (includes hydrolysis)
Cleavage
Which type of regulation involves regulator molecules binding (reversibly) to regulatory sites on an enzyme and influencing the binding of substrates to the active site (in a positive or negative manner).
Allosteric
Which enzyme removes phosphate groups?
Phosphatase
A reaction pathway which continues in a cycle, producing by products
Cyclical
Name for the chemicals on the left side of a reaction
Substrate
Forward and reverse reactions create kinetic ________
with equal generation of both substrate/product
Equilibrium
What would adding more substrate do to a reaction speed?
Increase
What influences the concentration of an enzyme in a cell, which can be altered depending on the availability of substrate.
Genetic expression/Gene level control
Substrate concentration for half Vmax (i.e. 50% maximal rate, expressed as concentration)
Km
Which enzyme group adds phosphate groups?
Kinase
Reusable biological catalysts which speed up chemical reactions
Enzyme
Vmax/Enzyme concentration
Kcat
Name for the chemicals on the right side of a reaction
Product
Amount of enzyme which converts 1umol of S to P per minute
IU
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