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MindMap Gallery Medicine - Enzymes and Enzymatic Reactions

Medicine - Enzymes and Enzymatic Reactions

This is a mind map about medicine - enzymes and enzymatic reactions, including the molecular composition of enzymes, How enzymes work, Enzymes promote the substrate to form a transition state to increase the reaction rate, Applications of enzymes in medicine, etc.

Edited at 2023-11-27 16:51:33

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Medicine - Enzymes and Enzymatic Reactions

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Outline

Enzymes and enzymatic reactions

The molecular composition of enzymes

simple enzyme

Conjugation enzyme (holoenzyme)

Enzyme protein

cofactor

coenzyme

prosthetic base

How enzymes work

Enzymes are highly efficient in catalyzing substrates

Enzymes are highly specific for their substrates

absolute specificity

relative specificity

Enzymes are tunable

Enzymes are unstable

Enzymes promote the formation of transition states in substrates to increase the reaction rate

Enzymes reduce activation energy more effectively than ordinary catalysts

Enzyme and substrate form intermediate

induced fit

Make enzyme and substrate more closely connected

Proximity effect and directional alignment

Allow the substrate to correctly position the active center of the enzyme

surface effect

Desolvate the substrate to prevent the formation of a hydrated film, The enzyme and substrate molecules are brought into close contact and combined.

Applications of enzymes in medicine

congenital enzyme defects

Albinism, favismosis

Diagnosis (abnormally increased enzyme content)

Alanine aminotransferase: acute hepatitis

Urinary amylase: acute pancreatitis

regulation of enzymes

Enzyme activity regulation (quick regulation)

(variation) allosteric adjustment

Metabolites in the body are non-covalently bound to a site outside the active center of the enzyme without consuming energy or enzymes.

chemical modification regulation

Under the action of other enzymes, the groups on the enzyme protein peptide chain consume energy and covalently combine with chemical groups, and remove the combined chemical groups.

Features: There is a cascade amplification effect

Example: Phosphorylation and dephosphorylation

zymogen activation

Essence: the process of formation and exposure of enzyme active centers

Enzyme content regulation (slow regulation)

Induction and hindrance of enzyme protein synthesis

Enzymatic protein degradation

Other influencing factors

substrate concentration

When the substrate concentration is sufficient, the effect of enzyme concentration on reaction rate is linear (first-order reaction)

temperature

The impact on enzymatic reactions is dual

Affects the rate of enzymatic reactions by changing the dissociation state of enzyme and substrate

activator

Change enzyme from inactive to active or increase enzyme activity

Example: Chloride ion is a non-essential activator of salivary amylase

Inhibitors affect the rate of enzymatic reactions

irreversibility

specificity

Example: Organophosphorus pesticides combine with the hydroxyl group of serine in the active center of cholinesterase to inactivate it, and are detoxified by pralidoxime and atropine.

non-specificity

Example: Low concentrations of heavy metal ions and Lewis gas combine with the sulfhydryl group outside the active center of sulfhydrylase to deactivate it.

Reversibility

competitive

Inhibition of succinate dehydrogenase by malonate

Inhibition of dihydropteroic acid by sulfonamides

non-competitive

anti-competitive

enzymatic kinetics

Kinetic parameters and its meaning

The Km value is equal to the substrate concentration at which the enzymatic reaction rate is half the maximum reaction rate.

Km is a characteristic constant of the enzyme - it is independent of the enzyme concentration.

Km can represent the affinity of the enzyme for the substrate under certain conditions (negative correlation)

Vmax represents the substrate concentration when the enzyme is completely saturated with the substrate concentration.