Transferase

From WikiMD's Wellness Encyclopedia

Transferase is a class of enzymes that facilitate the transfer of a functional group (e.g., a methyl or phosphate group) from one molecule (called the donor) to another (called the acceptor). Transferases are involved in myriad reactions in the cell.

Classification[edit | edit source]

Transferases can be broadly classified into nine categories based on the type of functional group they transfer:

  1. Transaminases
  2. Acyl transferases
  3. Alkyl or aryl transferases
  4. Diphosphotransferases
  5. Phosphotransferases
  6. Sulfurtransferases
  7. Methyltransferases
  8. Glycosyltransferases
  9. Other transferases

Each of these categories includes numerous specific enzymes, each with its own target donor and acceptor molecules.

Function[edit | edit source]

Transferases play a critical role in various biological processes, including metabolism, where they catalyze the transfer of functional groups to facilitate reactions. For example, in the process of glycolysis, the enzyme phosphoglycerate kinase transfers a phosphate group from 1,3-bisphosphoglycerate to ADP to form ATP and 3-phosphoglycerate.

Clinical significance[edit | edit source]

Abnormal transferase activity can lead to a variety of health conditions. For example, elevated levels of the transaminases ALT and AST in the blood can be an indicator of liver damage. In addition, mutations in the genes encoding transferases can lead to metabolic disorders. For example, a deficiency in the enzyme phenylalanine hydroxylase, which is a type of transferase, results in the metabolic disorder PKU.

See also[edit | edit source]

References[edit | edit source]

Transferase Resources
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Contributors: Prab R. Tumpati, MD