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MetaCyc Reaction: 2.2.1.1

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 2.2.1.1

Enzymes and Genes:

Escherichia coli K-12 substr. MG1655 : transketolase II Inferred from experiment : tktB
transketolase I Inferred from experiment : tktA
Mycoplasma pneumoniae M129 : transketolase Inferred 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) , Bifidobacterium shunt , pentose phosphate pathway (non-oxidative branch) , Rubisco shunt , Calvin-Benson-Bassham cycle

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, 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): 1.2300415 Inferred 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
Page generated by SRI International Pathway Tools version 19.0 on Fri Aug 28, 2015, BIOCYC14B.