U01.01.089 Enzyme terminology

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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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