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Gene Review:

talB - transaldolase B

Escherichia coli str. K-12 substr. MG1655

Sprenger, G.A. et al., Schörken, U. et al., Jia, J. et al.

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Disease relevance of talB

Transaldolase B of Escherichia coli K-12: cloning of its gene, talB, and characterization of the enzyme from recombinant strains [1].

High impact information on talB

After cloning of the gene onto high-copy-number vectors, transaldolase B (D-sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate dihydroxyacetone transferase; EC 2.2.1.2) was overexpressed up to 12.7 U mg of protein-1 compared with less than 0.1 U mg of protein-1 in wild-type homogenates [1].
The roles of invariant residues at the active site of transaldolase B from Escherichia coli have been probed by site-directed mutagenesis [2].

Analytical, diagnostic and therapeutic context of talB

As the enzyme had a molecular mass of 70,000 Da by gel filtration, transaldolase B is likely to form a homodimer [1].
Crystallization and preliminary X-ray crystallographic analysis of recombinant transaldolase B from Eschericha coli [3].

References

Transaldolase B of Escherichia coli K-12: cloning of its gene, talB, and characterization of the enzyme from recombinant strains. Sprenger, G.A., Schörken, U., Sprenger, G., Sahm, H. J. Bacteriol. (1995) [Pubmed]
Identification of catalytically important residues in the active site of Escherichia coli transaldolase. Schörken, U., Thorell, S., Schürmann, M., Jia, J., Sprenger, G.A., Schneider, G. Eur. J. Biochem. (2001) [Pubmed]
Crystallization and preliminary X-ray crystallographic analysis of recombinant transaldolase B from Eschericha coli. Jia, J., Lindqvist, Y., Schneider, G., Schörken, U., Sahm, H., Sprenger, G.A. Acta Crystallogr. D Biol. Crystallogr. (1996) [Pubmed]

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