What is the Difference Between Hydrolase and Transferase?

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Hydrolases and transferases are two types of enzymes that catalyze different types of biochemical reactions. The main difference between them is:

  • Hydrolases: These enzymes catalyze the hydrolysis of substances, which involves the addition of water to break covalent bonds in compounds. Hydrolases use water to cleave compounds into smaller molecules. Examples of hydrolases include lipases, phosphatases, glycosidases, peptidases, and nucleosidases.
  • Transferases: These enzymes catalyze the transfer of functional groups (such as acetyl, amino, methyl, or phosphoryl groups) from one molecule to another. Transferases do not use water during the reaction. Examples of transferases include methyltransferases, formyltransferases, acyltransferases, glycosyltransferases, sulfurtransferases, and transaldolases.

In summary, hydrolases use water to break covalent bonds in compounds, while transferases catalyze the transfer of functional groups from one molecule to another without using water as a reactant.

Comparative Table: Hydrolase vs Transferase

Here is a table comparing the differences between hydrolase and transferase enzymes:

Feature Hydrolase Transferase
Definition Enzymes that catalyze the hydrolysis of substances using water. Enzymes that catalyze the transfer of functional groups (e.g., acetyl, amino, methyl, phosphoryl) from one molecule to another.
Reaction Cleaves covalent bonds in compounds, hydrolyzing them into smaller compounds. Transfers functional groups among compounds.
Examples Lipases, phosphatases, glycosidases, peptidases, and nucleosidases. Methyltransferases, formyltransferases, acyltransferases, glycosyltransferases, sulfurtransferases, and transaldolases.

Hydrolases are enzymes that use water to cleave covalent bonds in compounds, while transferases are enzymes that facilitate the transfer of functional groups from one molecule to another.