IPR004731
Transaldolase type 3B/Fructose-6-phosphate aldolase
InterPro entry
Short name | Transaldolase_3B/F6P_aldolase |
Overlapping homologous superfamilies | |
family relationships |
Description
This entry includes transaldolases type 3B and fructose-6-phosphate aldolase. They share a high degree of structural similarity and sequence identity.
Transaldolase (
2.2.1.2) catalyses the reversible transfer of a three-carbon ketol unit from sedoheptulose 7-phosphate to glyceraldehyde 3-phosphate to form erythrose 4-phosphate and fructose 6-phosphate. This enzyme, together with transketolase, provides a link between the glycolytic and pentose-phosphate pathways. Transaldolase is an enzyme of about 34kDa whose sequence has been well conserved throughout evolution. A lysine has been implicated
[2] in the catalytic mechanism of the enzyme; it acts as a nucleophilic group that attacks the carbonyl group of fructose-6-phosphate.
Fructose-6-phosphate aldolase was originally thought to be transaldolases or transaldolase-related proteins. However, they perform a novel reaction, the cleavage or formation of fructose 6-phosphate
[1].
References
1.Fructose-6-phosphate aldolase is a novel class I aldolase from Escherichia coli and is related to a novel group of bacterial transaldolases. Schurmann M, Sprenger GA. J. Biol. Chem. 276, 11055-61, (2001). View articlePMID: 11120740
2.Lysine144 is essential for the catalytic activity of Saccharomyces cerevisiae transaldolase. Miosga T, Schaaff-Gerstenschlager I, Franken E, Zimmermann FK. Yeast 9, 1241-9, (1993). View articlePMID: 8109173
GO terms
biological process
molecular function
- None
cellular component
- None
Cross References
Contributing Member Database Entry
- NCBIfam:TIGR00875
Representative structure
3r8r: Transaldolase from Bacillus subtilis