Guanosine-5'-triphosphate (GTP) is a purine nucleoside triphosphate. It is one of the building blocks needed for the synthesis of RNA during the transcription process. Its structure is similar to that of the guanine nucleobase, the only difference being that nucleotides like GTP have a ribose sugar and three phosphates, with the nucleobase attached to the 1' and the triphosphate moiety attached to the 5' carbons of the ribose.
((2R,3S,4R,5R)-5-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyl tetrahydrogen triphosphate
guanosine triphosphate, 9-β-D-ribofuranosylguanine-5'-triphosphate, 9-β-D-ribofuranosyl-2-amino-6-oxo-purine-5'-triphosphate
3D model (JSmol)
|Molar mass||523.18 g·mol−1|
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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It also has the role of a source of energy or an activator of substrates in metabolic reactions, like that of ATP, but more specific. It is used as a source of energy for protein synthesis and gluconeogenesis.
GTP is involved in energy transfer within the cell. For instance, a GTP molecule is generated by one of the enzymes in the citric acid cycle. This is tantamount to the generation of one molecule of ATP, since GTP is readily converted to ATP with nucleoside-diphosphate kinase (NDK).
During the elongation stage of translation, GTP is used as an energy source for the binding of a new amino-bound tRNA to the A site of the ribosome. GTP is also used as an energy source for the translocation of the ribosome towards the 3' end of the mRNA.
Microtubule dynamic instabilityEdit
During microtubule polymerization, each heterodimer formed by an alpha and a beta tubulin molecule carries two GTP molecules, and the GTP is hydrolyzed to GDP when the tubulin dimers are added to the plus end of the growing microtubule. Such GTP hydrolysis is not mandatory for microtubule formation, but it appears that only GDP-bound tubulin molecules are able to depolymerize. Thus, a GTP-bound tubulin serves as a cap at the tip of microtubule to protect from depolymerization; and, once the GTP is hydrolyzed, the microtubule begins to depolymerize and shrink rapidly.
The translocation of proteins into the mitochondrial matrix involves the interactions of both GTP and ATP. The importing of these proteins plays an important role in several pathways regulated within the mitochondria organelle, such as converting oxaloacetate to phosphoenolpyruvate (PEP) in gluconeogenesis.
In the cell, GTP is synthesised through many processes including:
- as a byproduct of the Succinyl-CoA to Succinate conversion catalysed by the Succinyl-CoA synthetase enzyme as part of the Krebs cycle;
- through exchanges of phosphate groups from ATP molecules by the Nucleoside-diphosphate kinase, an enzyme tasked with maintaining an equilibrium between the concentrations of different nucleoside triphosphates.
- Berg, JM; JL Tymoczko; L Stryer (2002). Biochemistry (5th ed.). WH Freeman and Company. p. 476. ISBN 0-7167-4684-0.
- Solomon, EP; LR Berg; DW Martin (2005). Biology (7th ed.). pp. 244–245.
- Gwen V. Childs. "Microtubule structure". cytochemistry.net. Archived from the original on 2010-02-15.
- Sepuri, Naresh Babu V.; Norbert Schülke; Debkumar Pain (16 January 1998). "GTP Hydrolysis Is Essential for Protein Import into the Mitochondrial Matrix". Journal of Biological Chemistry (273): 1420–1424. doi:10.1074/jbc.273.3.1420.
- Boron & Boulpaep (2005). Medical Physiology (Updated ed.). Elsevier Saunders. p. 90. ISBN 1-4160-2328-3.