Transketolase
Enzyme involved in the pentose phosphate pathway
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Identifiers | |
---|---|
EC number | 2.2.1.1 |
CAS number | 9026-58-6 |
Alt. names | |
IntEnz | IntEnz view |
BRENDA | BRENDA entry |
ExPASy | NiceZyme view |
KEGG | KEGG entry |
MetaCyc | metabolic pathway |
Transketolase (TKT) is an enzyme that plays a crucial role in the pentose phosphate pathway, a metabolic pathway parallel to glycolysis. It catalyzes the transfer of a two-carbon unit from a ketose donor to an aldose acceptor. This enzyme is essential for the non-oxidative phase of the pentose phosphate pathway, which is important for the production of nucleotides and nucleic acids.
Function[edit | edit source]
Transketolase catalyzes two key reactions in the pentose phosphate pathway:
- The conversion of xylulose-5-phosphate and ribose-5-phosphate to glyceraldehyde-3-phosphate and sedoheptulose-7-phosphate.
- The conversion of xylulose-5-phosphate and erythrose-4-phosphate to glyceraldehyde-3-phosphate and fructose-6-phosphate.
These reactions are essential for the interconversion of sugars and the generation of NADPH, which is necessary for biosynthetic reactions and antioxidant defense.
Structure[edit | edit source]
Transketolase is a homodimeric enzyme, meaning it consists of two identical subunits. Each subunit contains a binding site for the cofactor thiamine pyrophosphate (TPP), which is essential for its catalytic activity. The enzyme also requires magnesium ions for its function.
Clinical Significance[edit | edit source]
Deficiency in transketolase activity can lead to various metabolic disorders. One such condition is Wernicke-Korsakoff syndrome, a neurological disorder often associated with chronic alcoholism and characterized by a deficiency in thiamine (vitamin B1), which is a cofactor for transketolase. Symptoms include confusion, ataxia, and memory problems.
Related Enzymes[edit | edit source]
Transketolase is part of a family of enzymes that includes transaldolase, which also participates in the pentose phosphate pathway. Both enzymes work together to maintain the balance of sugar phosphates in the cell.
See Also[edit | edit source]
References[edit | edit source]
External Links[edit | edit source]
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Contributors: Prab R. Tumpati, MD