Triosephosphate dehydrogenase
Triosephosphate isomerase (TPI or TIM) is an enzyme that catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P). Despite the initial request mentioning "triosephosphate dehydrogenase," it appears there might be a mix-up in enzyme names, as the enzyme commonly associated with triose phosphates in glycolysis is triosephosphate isomerase. There is no widely recognized enzyme specifically named "triosephosphate dehydrogenase" in biochemistry literature. Therefore, this article will focus on triosephosphate isomerase, which plays a crucial role in glycolysis.
Function[edit | edit source]
Triosephosphate isomerase plays a critical role in the glycolysis and gluconeogenesis pathways, allowing cells to efficiently extract energy from glucose and convert it into ATP. By catalyzing the conversion between DHAP and G3P, TPI ensures that the amount of G3P needed for the subsequent steps in glycolysis is maintained, optimizing energy yield from glucose molecules.
Structure[edit | edit source]
The enzyme is a dimer, with each monomer consisting of approximately 250 amino acids. The active site, where the isomerization occurs, is located in the center of the monomer. The structure of TPI is highly conserved across different species, indicating its essential role in metabolism.
Genetic and Clinical Significance[edit | edit source]
Mutations in the gene encoding triosephosphate isomerase can lead to Triosephosphate isomerase deficiency (TPI deficiency), a rare autosomal recessive metabolic disorder. This condition is characterized by hemolytic anemia, neuromuscular disorders, and increased susceptibility to infections. The severity of the symptoms can vary widely among affected individuals.
Mechanism[edit | edit source]
The isomerization reaction catalyzed by TPI involves the transfer of a hydrogen atom and the migration of a double bond. This reaction is essential for the efficient continuation of glycolysis, as only G3P, not DHAP, can be further metabolized in the pathway.
Evolutionary Significance[edit | edit source]
Due to its role in a fundamental metabolic pathway, triosephosphate isomerase is considered one of the most efficient enzymes, often cited as an example of a nearly perfect enzyme. Its efficiency and the conservation of its structure across different species highlight its importance in the evolution of life.
See Also[edit | edit source]
Search WikiMD
Ad.Tired of being Overweight? Try W8MD's physician weight loss program.
Semaglutide (Ozempic / Wegovy and Tirzepatide (Mounjaro / Zepbound) available.
Advertise on WikiMD
WikiMD's Wellness Encyclopedia |
Let Food Be Thy Medicine Medicine Thy Food - Hippocrates |
Translate this page: - East Asian
中文,
日本,
한국어,
South Asian
हिन्दी,
தமிழ்,
తెలుగు,
Urdu,
ಕನ್ನಡ,
Southeast Asian
Indonesian,
Vietnamese,
Thai,
မြန်မာဘာသာ,
বাংলা
European
español,
Deutsch,
français,
Greek,
português do Brasil,
polski,
română,
русский,
Nederlands,
norsk,
svenska,
suomi,
Italian
Middle Eastern & African
عربى,
Turkish,
Persian,
Hebrew,
Afrikaans,
isiZulu,
Kiswahili,
Other
Bulgarian,
Hungarian,
Czech,
Swedish,
മലയാളം,
मराठी,
ਪੰਜਾਬੀ,
ગુજરાતી,
Portuguese,
Ukrainian
Medical Disclaimer: WikiMD is not a substitute for professional medical advice. The information on WikiMD is provided as an information resource only, may be incorrect, outdated or misleading, and is not to be used or relied on for any diagnostic or treatment purposes. Please consult your health care provider before making any healthcare decisions or for guidance about a specific medical condition. WikiMD expressly disclaims responsibility, and shall have no liability, for any damages, loss, injury, or liability whatsoever suffered as a result of your reliance on the information contained in this site. By visiting this site you agree to the foregoing terms and conditions, which may from time to time be changed or supplemented by WikiMD. If you do not agree to the foregoing terms and conditions, you should not enter or use this site. See full disclaimer.
Credits:Most images are courtesy of Wikimedia commons, and templates Wikipedia, licensed under CC BY SA or similar.
Contributors: Prab R. Tumpati, MD