PMID:8805555

Citation	Jia, J, Huang, W, Schörken, U, Sahm, H, Sprenger, GA, Lindqvist, Y and Schneider, G (1996) Crystal structure of transaldolase B from Escherichia coli suggests a circular permutation of the alpha/beta barrel within the class I aldolase family. Structure 4:715-24
Abstract	Transaldolase is one of the enzymes in the non-oxidative branch of the pentose phosphate pathway. It transfers a C3 ketol fragment from a ketose donor to an aldose acceptor. Transaldolase, together with transketolase, creates a reversible link between the pentose phosphate pathway and glycolysis. The enzyme is of considerable interest as a catalyst in stereospecific organic synthesis and the aim of this work was to reveal the molecular architecture of transaldolase and provide insights into the structural basis of the enzymatic mechanism.
Links	PubMed
Keywords	Amino Acid Sequence; Binding Sites; Crystallography, X-Ray; Escherichia coli/enzymology; Escherichia coli/metabolism; Evolution, Molecular; Fructose-Bisphosphate Aldolase/chemistry; Fructose-Bisphosphate Aldolase/classification; Fructose-Bisphosphate Aldolase/genetics; Models, Chemical; Models, Molecular; Molecular Sequence Data; Pentose Phosphate Pathway/genetics; Protein Conformation; Protein Structure, Secondary; Schiff Bases/chemistry; Sequence Alignment; Transaldolase/chemistry
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