Activity
Learning Objectives
- Identify core enzyme classes based on their functional descriptors.
- Distinguish between ATP-dependent and ATP-independent phosphate reactions.
- Recognize essential clinical cofactors required for specific enzyme functions.
1. Phosphate-Handling Enzymes
The movement of phosphate groups is a fundamental mechanism in signal transduction and metabolic regulation.
- Kinase: Catalyzes the transfer of a phosphate group from a high-energy molecule (usually ATP) to a substrate.
- Example: Phosphofructokinase (PFK-1).
- Phosphorylase: Adds inorganic phosphate to a substrate without using ATP.
- Example: Glycogen phosphorylase.
- Phosphatase: Removes a phosphate group from a substrate.
- Example: Fructose-1,6-bisphosphatase 1.
2. Oxidation, Synthesis, and Relocation
Enzymes also manage the redox state and structural arrangement of molecules.
- Dehydrogenase: Catalyzes oxidation-reduction reactions.
- Example: Pyruvate dehydrogenase.
- Carboxylase: Transfers carboxyl groups (−COOH). Often requires Biotin (B7).
- Example: Pyruvate carboxylase.
- Mutase: Relocates a functional group within a molecule.
- Example: Vitamin B12–dependent methylmalonyl-CoA mutase.
Clinical Correlate: Cofactor Deficiencies
Deficiencies in cofactors like Biotin or B12 directly impair the function of Carboxylases and Mutases, leading to metabolic disorders like organic acidemias.
Mnemonic
Kinases kick a phosphate from ATP. Phosphorylases put an inorganic P on. Phosphatases pull a phosphate off.
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