Transaldolase

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transaldolase 1
Identifiers
Symbol TALDO1
Entrez 6888
HUGO 11559
OMIM 602063
RefSeq NM_006755
UniProt P37837
Other data
EC number 2.2.1.2
Locus Chr. 11 p15.5-15.4

Transaldolase is an enzyme of the pentose phosphate pathway. Transaldolase has a Lys residue in the active site, which forms a Schiff base with the keto group in sedoheptulose-7-phosphate. The reaction mechanism is similar to the reverse reaction catalyzed by aldolase: the bond joining carbons 3 and 4 is split, leaving dihydroxyacetone joined to the enzyme via a Schiff base. This cleavage reaction generates the unusual aldose sugar erythrose-4-phosphate. Then transaldolase catalyzes the condensation of glyceraldehyde-3-phosphate with the Schiff base of dihydroxyacetone, yielding enzyme bound fructose-6-phosphate. Hydrolysis of the Schiff base liberates free fructose-6-phosphate, one of the products of the pentose phosphate pathway.

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Acknowledgement and Attribution Regarding Sources of Content

Some of the initial content on this page may be incorporated in part from copyleft sources in the public domain including wikis such as Wikipedia and AskDrWiki. Drug information for patients came from the The National Library of Medicine. Infectious disease information may have come from the Centers for Disease Control (CDC). Differential Diagnoses are drawn from clinicians as well as an amalgamation of 3 sources: 1.The Disease Database; 2. Kahan, Scott, Smith, Ellen G. In A Page: Signs and Symptoms. Malden, Massachusetts: Blackwell Publishing, 2004:3; 3. Sailer, Christian, Wasner, Susanne. Differential Diagnosis Pocket. Hermosa Beach, CA: Borm Bruckmeir Publishing LLC, 2002:7 .

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