A biological catalyst that speeds up chemical reactions in living organisms.
The least amount of energy needed for a chemical reaction to take place.
They are involved in virtually all physiological processes, making them targets for drugs that cure or ameliorate human disease.
Carbonic anhydrase.
The amount of substrate present in a reaction mixture.
They are critical for understanding the mode of action of drugs.
An increase in the rate of reaction with the help of an enzyme as a catalyst.
It increases the number of reactant molecules that achieve sufficient energy to reach activation energy and form products.
A branch of biochemistry that studies the rate of enzyme-catalyzed reactions.
-ase.
Myocardial infarction, congestive heart failure, and liver dysfunction.
The breakage of bonds without hydrolysis.
Increase in activity.
Chemistry.
A factor by which the rate of biological processes increases for a 10 °C increase in temperature.
Oxydoreductase, which catalyzes biological oxidation.
Catalyzes the conversion of pyruvate to acetaldehyde and CO2.
Aspartate aminotransferase; primarily in the liver and myocardium.
Alanine aminotransferase; primarily in the liver.
Gamma-glutamyl transferase; primarily in the liver.
The rate of almost all enzyme-catalyzed reactions depends on pH.
It denatures.
Magnesium (Mg).
Increasing substrate concentration generally increases the rate of reaction until a maximum velocity is reached.
They do not affect the nature and properties of the end product.
DNA.
Transaminase.
Grouping enzymes based on their functions and characteristics.
The process by which enzymes catalyze biochemical reactions.
The rates of enzyme-catalyzed reactions.
Enzymes synthesized and secreted from the cell to work externally.
Enzymes lower the activation energy by changing the route of the reaction.
Enzymes always emerge unchanged.
Only a few substances cross the activation barrier and change into products.
The process of increasing enzyme activity.
Apoenzyme.
Inorganic molecules required for the proper activity of enzymes.
A loosely bound organic co-factor.
Pyruvate dehydrogenase.
The number and order of the individual steps in transforming substrate into products.
It results in very low activation energy.
It increases the rate of reaction by increasing the kinetic energy of reacting molecules.
The reaction rate increases linearly with an increase in substrate concentration.
They are bonded together to form specific enzymes according to DNA's codes.
17 hours.
110 hours.
The substrates.
Energy barriers.
A tightly bound organic co-factor.
The hydrolysis of a bond.
It is referred to as pH.
Pepsin, which hydrolyzes peptide bonds in proteins.
The oxidation of pyruvate to acetyl coenzyme A.
Muscle tissue breakdown.
Biochemistry.
Enzymes can serve as biomarkers for diseases and are targets for drug development.
Km is the substrate concentration at which the reaction rate is half of Vmax.
The maximum velocity of the reaction.
By affecting the catalytic activity of the enzyme.
Higher in uncatalyzed reactions.
By binding of an organic or inorganic cofactor.
Organic co-factors and inorganic co-factors.
Covalent linkages.
Carbonic anhydrase catalyzes the hydration of 10⁶ CO₂ molecules per second, which is 10⁷ times faster than spontaneous hydration.
By lowering the activation energy of the reaction.
Leonor Michaelis and Maud Menten.
Enzyme activity reaches a maximum rate, known as Vmax, where all active sites are saturated.
Yes, they can assist in the diagnosis of cancer.
Pepsin, trypsin, and rennin.
They can accelerate chemical reactions.
Changes in pH, temperature, and substrate concentration.
Lactate dehydrogenase (LD).
A non-protein molecule that carries out chemical reactions not performed by standard 20 amino acids.
Oxidation and reduction reactions.
Pepsin, trypsin, and arginase.
The amount of substrate present in a reaction mixture.
Organic molecules required for the proper activity of enzymes.
2 hours.
The reaction rate increases with substrate concentration but levels off at Vmax.
The total energy of the system remains the same and the equilibrium state is not disturbed.
Vmax.
The formation of an isomer of a compound.
Myocardial infarction (MI) and hepatopathy.
The ability of an enzyme to select for a particular substrate.
Acid phosphatase (ACP).
Activational barrier.
Small organic molecules, metal ions, and other components.
Identify and characterize therapeutic agents that selectively inhibit specific enzyme-catalyzed processes.
A well-known model of enzyme kinetics in biochemistry.
By ribosomes attached to the rough endoplasmic reticulum.
Hydrolase.
Generally between 35 - 45 °C.
In the cytoplasm, nucleus, mitochondria, and chloroplast.
Certain enzyme levels in the blood can indicate the presence of specific diseases.
They are involved in reduction processes.
6 x 10^6 per minute.
Acid phosphatase; primarily in the prostate.
Cholesterol esterase; primarily in the liver.
Holoenzyme or holoprotein.
According to the name of the substrate it catalyses.
5 - 40°C.
Relative concentrations of enzyme (E) and substrate (S).
Enzymes are targets for drugs that aim to inhibit their activity to treat diseases.
Enzymes synthesized and retained in the cell for its own use.
V₀ = (Vmax [S]) / (Km + [S]).
The enzyme is regenerated and can combine with another substrate.
Digestive enzymes produced by the pancreas.
Hepatopathy due to alcohol or drugs.
DNA ligase catalyzes the joining of two fragments of DNA by forming a phosphodiester bond.
Pancreatitis.
A transition state intermediate forms a covalent bond with the enzyme (covalent catalysis).
pH influences the rate of reaction by affecting enzyme structure.
Flavins or heme groups.
Maltase.
How reaction velocity varies with substrate concentration.
Pyridoxal phosphate.
Amylase, Sucrase, and Cellulase.
The initial reaction velocity.
The activation energy.
The number of substrate molecules transformed per minute by one enzyme molecule.
Hepatopathy.
Lactate dehydrogenase; not specific.
It is involved in amino acid metabolism.
An inactive enzyme.
Acidic and basic.
Between pH 5 and 9.
Enzymes provide an alternate pathway for conversion of substrate into products, allowing more substances to cross the activation barrier.
A transient enzyme-substrate complex.
Substrate concentration.
The catalytic mechanism of the enzyme, its role in metabolism, how its activity is controlled, and how drugs or agonists might inhibit it.
By forming a transitional state with low activation energy.
The enzyme is released unaltered.
The rate of reaction at the beginning before significant substrate depletion.
It is formed when the enzyme combines with the substrate before yielding the product.
Small regulatory molecules that bind to allosteric enzymes, influencing their activity.
It can lead to the denaturing of enzymes.
The Michaelis constant, calculated as (k₋₁ + k₂) / k₁.
The substrate concentration.
70%.
Amylase; primarily in the pancreas.
It affects the formation of hydrogen bonds and sulfur bridges, thus influencing their shape.
Temperature.
They assist in the diagnosis of diseases such as cancer and medical events like myocardial infarction.
It causes ionization of the enzyme, resulting in denaturation.
The reversible combination of an enzyme with substrate to form an ES complex that yields product and regenerates the free enzyme.
NAD+ or biotin.
Increasing substrate concentration generally increases the rate of reaction until a maximum velocity is reached.
The reaction rate is increased many folds.
An enzyme that contains a region for small regulatory molecules to bind, affecting its catalytic activity.
Sucrose is split into Glucose and Fructose.
In a region separate from the substrate binding site.
The products.
The duodenum.
They are secreted to work externally in the digestive system.
Pancreatitis.
Inactive.
Substrate (S), enzyme (E), enzyme-substrate complex (ES), and product (P).
The transfer of a chemical group from one compound to another.
They are rate constants.
13 hours.
Transfers an amino group from one molecule to another.
Enzymes can be targeted to create drugs that inhibit or enhance their activity.
In the cytoplasm, mitochondria, Golgi complex, endoplasmic reticulum, and lysosome.
The process by which a substance decreases enzyme activity.
Glycogenolysis.
Creatine kinase; primarily in myocardium and muscles.
Myocardial infarction (CK-MB) and muscle diseases.
0.25 hours.
Steady-State assumptions.
Aldolase, which catalyzes the splitting of fructose-1,6-bisphosphate.
Each enzyme can catalyze one kind of substrate.
At high substrate concentrations, the enzyme becomes saturated, and the reaction rate reaches a maximum.
Q₁₀ = 2.
Phosphoglucomutase catalyzes the conversion of glucose-1-phosphate to glucose-6-phosphate.
Biliary tract diseases and bone diseases.
It is involved in the processing and packaging of enzymes.
The joining of two molecules.
Gamma-glutamyl transferase (GMT).
30%.
The energy levels of molecules.
Alkaline phosphatase; in the biliary tract and bones.
Indicates potential absence of disease or recovery.
Prostatic cancer.
Lipase; primarily in the pancreas.
Alkaline phosphatase.
