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MetaCyc 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:

Escherichia coli K-12 substr. MG1655: transketolase IIInferred from experiment: tktB
transketolase IInferred from experiment: tktA
Mycoplasma pneumoniae M129: transketolaseInferred from experiment: tktA
Synechocystis sp. PCC 6803: transketolase: tktA

In Pathway: pentose phosphate pathway (partial), formaldehyde assimilation II (RuMP Cycle), formaldehyde assimilation III (dihydroxyacetone cycle), pentose phosphate pathway (non-oxidative branch), Rubisco shunt, Calvin-Benson-Bassham cycle, Bifidobacterium shunt

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

Standard Gibbs Free Energy (ΔrG in kcal/mol): 1.2300415Inferred by computational analysis [Latendresse13]

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

Unification Links: KEGG:R01641, Rhea:10508

Relationship Links: BRENDA:EC:2.2.1.1, ENZYME:EC:2.2.1.1, IUBMB-ExplorEnz:EC:2.2.1.1, UniProt:RELATED-TO:O20250, UniProt:RELATED-TO:O78327, UniProt:RELATED-TO:P21725, UniProt:RELATED-TO:P21726, UniProt:RELATED-TO:P22976, UniProt:RELATED-TO:P23254, UniProt:RELATED-TO:P27302, UniProt:RELATED-TO:P29277, UniProt:RELATED-TO:P29401, UniProt:RELATED-TO:P33315, UniProt:RELATED-TO:P33570, UniProt:RELATED-TO:P34736, UniProt:RELATED-TO:P43757, UniProt:RELATED-TO:P45694, UniProt:RELATED-TO:P46708, UniProt:RELATED-TO:P47312, UniProt:RELATED-TO:P73282, UniProt:RELATED-TO:P75611, UniProt:RELATED-TO:Q9CF56, UniProt:RELATED-TO:Q9JTR1, UniProt:RELATED-TO:Q9PM31, UniProt:RELATED-TO:Q9RFB7, UniProt:RELATED-TO:Q9URM2, UniProt:RELATED-TO:Q9Z475, UniProt:RELATED-TO:Q42675, UniProt:RELATED-TO:Q42676, UniProt:RELATED-TO:Q42677, UniProt:RELATED-TO:Q49047, UniProt:RELATED-TO:Q52723, UniProt:RELATED-TO:Q58092, UniProt:RELATED-TO:Q58094


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

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

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.


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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