Guanosine triphosphate

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Guanosine triphosphate (GTP) is a purine nucleotide that plays a crucial role in various cellular processes. It is composed of the nucleoside guanosine and three phosphate groups. GTP is involved in protein synthesis, signal transduction, and acts as an energy source in metabolic processes.

Structure[edit | edit source]

GTP consists of a guanine base attached to a ribose sugar, which is further linked to three phosphate groups. The structure of GTP is similar to that of adenosine triphosphate (ATP), with the primary difference being the nitrogenous base.

Functions[edit | edit source]

Protein Synthesis[edit | edit source]

GTP is essential in the process of translation, where it provides the energy required for the binding of aminoacyl-tRNA to the ribosome. It is hydrolyzed to guanosine diphosphate (GDP) during this process.

Signal Transduction[edit | edit source]

GTP is a key molecule in signal transduction pathways. It acts as a substrate for G-proteins, which are involved in transmitting signals from cell surface receptors to intracellular targets. The binding and hydrolysis of GTP to GDP by G-proteins regulate their activity.

Metabolic Processes[edit | edit source]

GTP is also involved in various metabolic processes, including the synthesis of RNA during transcription and the activation of certain enzymes.

GTPases[edit | edit source]

GTPases are a family of enzymes that hydrolyze GTP to GDP. These enzymes play a critical role in regulating cellular activities such as cell division, cell signaling, and protein transport.

Synthesis and Degradation[edit | edit source]

GTP is synthesized from guanosine diphosphate (GDP) by the enzyme nucleoside diphosphate kinase. It can be degraded back to GDP by the action of GTPases.

Clinical Significance[edit | edit source]

Abnormalities in GTP metabolism and GTPase function are associated with various diseases, including certain types of cancer and genetic disorders.

See Also[edit | edit source]

References[edit | edit source]

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Contributors: Prab R. Tumpati, MD