F
IPR004731

Transaldolase type 3B/Fructose-6-phosphate aldolase

InterPro entry
Short nameTransaldolase_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

molecular function

  • None

cellular component

  • None

Cross References

Contributing Member Database Entry
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