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Escherichia coli K-12 substr. MG1655 Reaction: 2.2.1.1


Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number: 2.2.1.1

Enzymes and Genes:
transketolase IIInferred from experiment: tktB
transketolase IInferred from experiment: tktA

In Pathway: pentose phosphate pathway (non-oxidative branch)

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Enzyme Commission Primary Name: transketolase

Enzyme Commission Synonyms: glycolaldehydetransferase

Summary:
This reaction is involved in the pentose phosphate pathway.

Enzyme Commission Summary:
A thiamine-diphosphate protein. Wide specificity for both reactants, e.g. converts hydroxypyruvate and R-CHO into CO2 and R-CHOH-CO-CH2OH. Transketolase from Alkaligenes faecalis shows high activity with D-erythrose as acceptor.

Citations: [DE55, HORECKER56, Racker61, Domagk65]

Gene-Reaction Schematic

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:2.2.1.1, ENZYME:EC:2.2.1.1, IUBMB-ExplorEnz:EC:2.2.1.1


References

DE55: DE LA HABA G, LEDER IG, RACKER E (1955). "Crystalline transketolase from bakers' yeast: isolation and properties." J Biol Chem 214(1);409-26. PMID: 14367398

Domagk65: Domagk GF, Horecker BL (1965). "Fructose and erythrose metabolism in Alcaligenes faecalis." Archives of Biochemistry and Biophysics 109(2);342-349.

HORECKER56: HORECKER BL, HURWITZ J, SMYRNIOTIS PZ (1956). "The role of xylulose 5-phosphate in the transketolase reaction." J Biol Chem 223(2);1009-19. PMID: 13385248

Racker61: Racker E. (1961). "Transketolase." In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds), The Enzymes, 2nd edn, vol. 5, Academic Press, New York pp. 397-412.


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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