3. Enzymes: General Properties. Enzyme Specificity. Nomenclature and Classification. Isozymes. Mechanism of Enzymatic Action.
Covers enzymes as biological catalysts, starting with their general properties such as catalytic power, specificity and sensitivity to conditions, then moving to simple versus conjugated enzymes and the types of cofactors. It goes on to specificity types and the lock-and-key and induced-fit models, the IUBMB six-class EC nomenclature, and isozymes with LDH and creatine kinase patterns. The note closes with the mechanism of catalysis, factors affecting activity and clinical uses of enzymes, and includes several comparison tables.
Inside: 10 sections · 4 labelled pictures · 9 tables · 1 formula · 20 flashcards · 6 min
Topic 3 of 76 in the MU Pleven syllabus for Biochemistry (Medicine, Year 2). The free AceMed note covers it in 10 sections, about 437 words (6 min of reading), with 20 flashcards.
In this note
Enzymes. General properties.
Definition of Enzymes
General Properties of Enzymes
Chemical Nature of Enzymes
Enzyme Specificity
Enzyme Nomenclature and Classification
Isoenzymes (Isozymes)
Mechanism of Enzymatic Action
Factors Affecting Enzyme Activity
Clinical Importance of Enzymes
Definition of Enzymes
Enzymes are biological catalysts — mostly proteins (some RNA molecules also act as enzymes, called ribozymes) — that increase the rate of chemical reactions without being consumed in the process.
Chemical Nature of Enzymes
A. Simple Enzymes
Composed only of protein.
Example: Pepsin, trypsin.
B. Conjugated (Holo) Enzymes
Have protein part (apoenzyme) + non-protein part (cofactor).
Types of Cofactors:
Prosthetic group: Tightly bound (e.g. FAD in succinate dehydrogenase).