Syntetaza

Syntetaza, commonly rendered in English as synthase or synthetase, is a biochemical term for enzymes that catalyze the formation of a bond between two substrates with the input of energy, typically from ATP or another nucleotide triphosphate. The term is often used for ATP-dependent ligases (enzyme class EC 6) that activate a substrate to enable bond formation.

Mechanism and scope: Most syntetases operate by activating one substrate to form an adenosine monophosphate (AMP)–linked intermediate, such as an acyl-adenylate, using ATP, followed by transfer of the activated group to a second substrate. This two-step sequence couples bond formation to ATP hydrolysis.

Key examples: Aminoacyl-tRNA synthetases attach specific amino acids to their corresponding tRNAs, a critical step in protein synthesis. Acyl-CoA synthetases activate fatty acids and other carboxylic acids by forming acyl-adenylates before thioester formation with CoA. Nonribosomal peptide synthetases and certain other assembly-line enzymes also rely on ATP-dependent ligation steps to construct complex natural products.

Nomenclature and distinction: The term syntetaza is used in various languages as the equivalent of the English “synthetase.” It is distinguished from synthase, which denotes enzymes that catalyze bond formation without direct energy input from ATP. In practice, many enzymes with “synthetase” in their name are ATP-dependent ligases.

Role and relevance: Syntetazes are essential across metabolism, protein synthesis, lipid metabolism, and the biosynthesis of secondary metabolites. They are common subjects of study in biochemistry, pharmacology, and metabolic engineering.