Sandbox GGC8

From Proteopedia

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== Function ==
== Function ==
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This Particular Protein Plays a big role in Glycolysis and activities in the nucleus. Glyceraldehyde-3-phosphate dehydrogenase is a very important enzyme that catalyzes the first step of the glycolysis pathway. This is done by converting D-glyceraldehyde-3-phosphate to 3-phospho-D glyceroyl phosphate. The catalytic reaction begins with the reactants of D-glyceraldehyde-3-phosphate, NAD+, and phosphate. This reaction then proceeds with the products of (2R)-3- phospho-D glyceroyl phosphate, H ion, and NADH. This reaction then proceeds in the glycolysis pathway and creates pyruvate from D-glyceraldehyde-3-phosphate.
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Glyceraldehyde-3-Phosphate dehydrogenase has a big role in the nucleus. It is a part of many processes such as DNA replication, transcription, RNA transport, and apoptosis. Although is participates in all of those nuclear activities, it is mostly known to initiate apoptosis and transcription of the genes that are known to be involved in the antiapoptotic pathways and cell proliferation. GAPDH also plays a role in regulating of telomere length. Many biochemists have determined that this protein interacts with some types of DNA damages. Examples of them are apurinic/ apyrimidinic sites, nucleotide analogs, and covalent DNA adducts with alkylating agents. This then indicates and confirms that it participates in DNA repair by interacting with repair proteins such as APE1.
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This protein also plays a part in carbohydrate degradation. It catalyzes an energy yielding step in carbohydrate metabolism. This happens when the nicotinamide adenine dinucleotide and the inorganic phosphate are present. This protein is a tetramer of chains that are identical.
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Glyceraldehyde-3-Phosphate dehydrogenase is regulated by being inhibited by Fumarate through the formation of S-(2-succinyl) cysteine residues.
== Disease ==
== Disease ==

Revision as of 05:31, 28 April 2021

GAPDH (Glyceraldehyde-3-Phosphate Dehydrogenase)

GAPDH

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References

  1. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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