((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
|Molar mass||523.18 g·mol−1|
Except where noted otherwise, data is given for materials in their standard state (at 25 °C (77 °F), 100 kPa)
|what is: / ?)(|
Guanosine-5'-triphosphate (GTP) is a purine nucleoside triphosphate. It can act as a substrate for the synthesis of RNA during the transcription process or DNA during DNA replication. 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.
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 instability
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 mitochondria 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.
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- Gwen V. Childs. "Microtubule structure". cytochemistry.net.
- Sepuri, Naresh Babu V.; Norbert Schülke and 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 edition ed.). Elsevier Saunders. p. 90. ISBN 1-4160-2328-3.
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