MindMap Gallery Biochemistry-mind map of the working principle of enzymes
This is a mind map about biochemistry - the working principle of enzymes, including the common points between enzymes and general catalysts, the salient features of enzymes, the working principles of enzymes, etc.
Edited at 2023-12-02 19:32:55El cáncer de pulmón es un tumor maligno que se origina en la mucosa bronquial o las glándulas de los pulmones. Es uno de los tumores malignos con mayor morbilidad y mortalidad y mayor amenaza para la salud y la vida humana.
La diabetes es una enfermedad crónica con hiperglucemia como signo principal. Es causada principalmente por una disminución en la secreción de insulina causada por una disfunción de las células de los islotes pancreáticos, o porque el cuerpo es insensible a la acción de la insulina (es decir, resistencia a la insulina), o ambas cosas. la glucosa en la sangre es ineficaz para ser utilizada y almacenada.
El sistema digestivo es uno de los nueve sistemas principales del cuerpo humano y es el principal responsable de la ingesta, digestión, absorción y excreción de los alimentos. Consta de dos partes principales: el tracto digestivo y las glándulas digestivas.
El cáncer de pulmón es un tumor maligno que se origina en la mucosa bronquial o las glándulas de los pulmones. Es uno de los tumores malignos con mayor morbilidad y mortalidad y mayor amenaza para la salud y la vida humana.
La diabetes es una enfermedad crónica con hiperglucemia como signo principal. Es causada principalmente por una disminución en la secreción de insulina causada por una disfunción de las células de los islotes pancreáticos, o porque el cuerpo es insensible a la acción de la insulina (es decir, resistencia a la insulina), o ambas cosas. la glucosa en la sangre es ineficaz para ser utilizada y almacenada.
El sistema digestivo es uno de los nueve sistemas principales del cuerpo humano y es el principal responsable de la ingesta, digestión, absorción y excreción de los alimentos. Consta de dos partes principales: el tracto digestivo y las glándulas digestivas.
How enzymes work
What enzymes have in common with general catalysts
There are no qualitative or quantitative changes before and after the reaction
Can only catalyze chemical reactions that are thermodynamically allowed
It can only accelerate the process of a reversible reaction without changing the equilibrium point of the reaction.
Salient features of enzymes
Enzymes are extremely efficient on substrates
Enzymes are highly specific for their substrates
absolute specificity
It can only act on a substrate of a specific structure, perform a specific reaction, and generate a product of a specific structure.
For example, urease can only catalyze the hydrolysis of urea to produce CO2 and NH3
relative specificity
The specificity of some enzymes for substrates is not based on the entire substrate molecular structure, but on specific chemical bonds or specific groups in the substrate molecules.
For example: protease
Stereospecificity
Some enzymes with absolute specificity can distinguish between optical isomers and stereoisomers and can only catalyze a reaction with one optical isomer or stereoisomer.
Enzyme tunability
Enzymes are unstable
How enzymes work
Enzymes combine with substrates to form intermediates: enzyme-substrate complexes
Effectively reduce reaction activation energy
Mechanism to reduce activation energy
induced fit
Proximity effect and directional alignment
Surface effects desolvate substrate molecules
Enzymatic reaction kinetics
substrate concentration
When other factors remain unchanged, the effect of substrate concentration on reaction rate is a rectangular hyperbolic relationship.
When the substrate concentration is low: the reaction rate is proportional to the substrate concentration; the reaction is a first-order reaction.
As the substrate concentration increases: the reaction rate no longer accelerates proportionally; the reaction is a mixed-level reaction.
When the substrate concentration reaches a certain level: the reaction rate no longer increases and reaches the maximum rate; the reaction is a zero-order reaction
Michael-Mann equation
V=Vmax[S]/Km[S]
Km
The Km value is equal to the substrate concentration at which the enzymatic reaction rate is half the maximum reaction rate.
Km can represent the affinity of the enzyme to the substrate under certain conditions.
Km ↑ Affinity ↓
Km ↓ Affinity ↑
The Km value is a characteristic constant of the enzyme
Size is not fixed
It is related to the structure of the enzyme, the structure of the substrate, the pH, temperature and ionic strength of the reaction environment.
independent of enzyme concentration
enzyme concentration
When the enzyme is saturated with the substrate, the reaction rate is proportional to the enzyme concentration
pH
Optimum pH
Not a characteristic constant of an enzyme
Affected by factors such as substrate concentration, buffer type and concentration, and enzyme purity
temperature
double impact
Optimum temperature
Not a characteristic constant of an enzyme
Depends on the reaction time
inhibitor
definition
Any substance that can reduce the catalytic activity of an enzyme without causing denaturation of the enzyme protein is called an enzyme inhibitor.
Type of action
irreversible inhibition
Combine with the necessary groups in the active center of the enzyme through covalent bonds to inactivate the enzyme
It cannot be removed by methods such as dialysis and ultrafiltration.
Organophosphorus compounds, low-concentration heavy metal ions and arsenic compounds
reversible inhibition
Reversibly binds to enzymes or enzyme-substrate complexes through non-covalent bonds to reduce or eliminate enzyme activity.
type
competitive inhibition
The inhibitor has a similar structure to the substrate and can compete with the substrate for the active center of the enzyme, thus preventing the enzyme from forming intermediates with the substrate.
Features
I and S have similar structures and compete for the active center of the enzyme.
The degree of inhibition depends on the relative affinity of the inhibitor to the enzyme and the substrate concentration
Dynamic characteristics: Vmax remains unchanged, apparent Km increases
Example
Malonate competes with succinate for succinate dehydrogenase
The antibacterial mechanism of sulfa drugs—competition with para-aminobenzoic acid for dihydrofolate synthase
noncompetitive inhibition
Some inhibitors bind to essential groups outside the active center of the enzyme and do not affect the binding of the enzyme to the substrate. There is no competitive relationship between the substrate and the inhibitor. However, the enzyme-substrate-inhibitor complex (ESI) cannot further release the product.
Features
I combines with essential groups outside the active center of E, and there is no competitive relationship between S and I
The degree of inhibition depends on the concentration of the inhibitor
Dynamic characteristics: Vmax decreases, apparent Km remains unchanged
anticompetitive inhibition
Inhibitors only bind to the intermediate product (ES) formed by the enzyme and substrate, reducing the amount of the intermediate product ES.
Features
Inhibitors bind only to enzyme-substrate complexes
The degree of inhibition depends on the concentration of the inhibitor and the concentration of the substrate
Dynamic characteristics: Vmax decreases, apparent Km decreases
activator
Substances that change enzymes from inactive to active or increase enzyme activity
type
Required Activator
optional activator
regulation of enzymes
Adjustment object
key enzyme
Adjustment method
Regulation of enzyme activity (rapid regulation)
allosteric adjustment
Can reversibly bind to a part outside the active center of certain enzyme molecules to change the enzyme conformation
allosteric enzyme
Often oligomers composed of multiple subunits, with synergistic effects
Allosteric parts
allosteric effect
allosteric activator
allosteric inhibitor
covalent modification regulation
Some groups on the peptide chain of enzyme proteins can be covalently combined with certain chemical groups under the catalysis of other enzymes, and at the same time, the combined chemical groups can be removed under the catalysis of another enzyme, thus affecting the enzyme activity
Phosphorylation vs. dephosphorylation (most common)
Acetylation and deacetylation
Methylation and demethylation
Adenylation and deadenylation
-SH and -S-S change each other
zymogen activation
Zymogen: Some enzymes are in an inactive state before they are synthesized or secreted in cells, or before they can exert their catalytic function.
Activation of zymogen: Under certain conditions, the process of converting zymogen into active enzyme
Mechanism of zymogen activation
The zymogen breaks one or several specific peptide bonds under specific conditions, hydrolyzes one or several short peptides, changes the molecular conformation, and forms or exposes the active center of the enzyme.
Regulation of enzyme content (slow regulation)
induction
repression