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MetaCyc Reaction:

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

EC Number:

Enzymes and Genes:

Escherichia coli K-12 substr. MG1655: glucose 6-phosphate-1-dehydrogenaseInferred from experiment: zwf
Homo sapiens: glucose-6-phosphate 1-dehydrogenaseTraceable author statement to experimental support: G6PD
Leuconostoc mesenteroides: glucose-6-phosphate 1-dehydrogenaseInferred from experiment: zwf
Methylobacillus flagellatus: glucose-6-phosphate dehydrogenaseInferred from experiment: zwf
Saccharomyces cerevisiae: glucose-6-phosphate dehydrogenaseInferred from experiment: ZWF1

In Pathway: superpathway of glycolysis and Entner-Doudoroff, NAD/NADP-NADH/NADPH cytosolic interconversion (yeast), pentose phosphate pathway (oxidative branch), heterolactic fermentation, formaldehyde oxidation I

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

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: glucose-6-phosphate dehydrogenase (NADP+)

Enzyme Commission Synonyms: NADP-glucose-6-phosphate dehydrogenase, Zwischenferment, D-glucose 6-phosphate dehydrogenase, glucose 6-phosphate dehydrogenase (NADP), NADP-dependent glucose 6-phosphate dehydrogenase, 6-phosphoglucose dehydrogenase, Entner-Doudoroff enzyme, glucose-6-phosphate 1-dehydrogenase, G6PDH, GPD, glucose-6-phosphate dehydrogenase

Standard Gibbs Free Energy (ΔrG in kcal/mol): -5.9264526Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
The enzyme catalyses a step of the pentose phosphate pathway. The enzyme is specific for NADP+. cf. EC, glucose-6-phosphate dehydrogenase [NAD(P)+] and EC, glucose-6-phosphate dehydrogenase (NAD+).

Citations: [Miclet01 , Noltmann61, Olavarria12, Glaser55, Engel69, Julian61, Hansen02, Ibraheem05, Iyer02, Cho90]

Gene-Reaction Schematic

Gene-Reaction Schematic

Unification Links: KEGG:R02736, Rhea:15841

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:, UniProt:RELATED-TO:O22404, UniProt:RELATED-TO:O22405, UniProt:RELATED-TO:O22406, UniProt:RELATED-TO:O24357, UniProt:RELATED-TO:O24358, UniProt:RELATED-TO:O24359, UniProt:RELATED-TO:O25730, UniProt:RELATED-TO:O51240, UniProt:RELATED-TO:O51581, UniProt:RELATED-TO:O65856, UniProt:RELATED-TO:O66787, UniProt:RELATED-TO:O81978, UniProt:RELATED-TO:P05370, UniProt:RELATED-TO:P0AC53, UniProt:RELATED-TO:P11410, UniProt:RELATED-TO:P11411, UniProt:RELATED-TO:P11412, UniProt:RELATED-TO:P11413, UniProt:RELATED-TO:P12646, UniProt:RELATED-TO:P21907, UniProt:RELATED-TO:P29686, UniProt:RELATED-TO:P37830, UniProt:RELATED-TO:P37986, UniProt:RELATED-TO:P44311, UniProt:RELATED-TO:P48826, UniProt:RELATED-TO:P48828, UniProt:RELATED-TO:P54547, UniProt:RELATED-TO:P54996, UniProt:RELATED-TO:P56110, UniProt:RELATED-TO:P73411, UniProt:RELATED-TO:Q8IKU0, UniProt:RELATED-TO:Q8L743, UniProt:RELATED-TO:Q9FJI5, UniProt:RELATED-TO:Q9FY99, UniProt:RELATED-TO:Q9JTW0, UniProt:RELATED-TO:Q9LK23, UniProt:RELATED-TO:Q9R5T2, UniProt:RELATED-TO:Q00612, UniProt:RELATED-TO:Q27741, UniProt:RELATED-TO:Q42919, UniProt:RELATED-TO:Q43793, UniProt:RELATED-TO:Q43839, UniProt:RELATED-TO:Q49700

Created 21-Jul-2015 by Caspi R, SRI International


Cho90: Cho SW, Joshi JG (1990). "Characterization of glucose-6-phosphate dehydrogenase isozymes from human and pig brain." Neuroscience 38(3);819-28. PMID: 2270145

Engel69: Engel HJ, Domschke W, Alberti M, Domagk GF (1969). "Protein structure and enzymatic activity. II. Purification and properties of a crystalline glucose-6-phosphate dehydrogenase from Candida utilis." Biochim Biophys Acta 191(3);509-16. PMID: 5363983

Glaser55: Glaser L, Brown DH (1955). "Purification and properties of d-glucose-6-phosphate dehydrogenase." J Biol Chem 216(1);67-79. PMID: 13252007

Hansen02: Hansen T, Schlichting B, Schonheit P (2002). "Glucose-6-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: expression of the g6pd gene and characterization of an extremely thermophilic enzyme." FEMS Microbiol Lett 216(2);249-53. PMID: 12435510

Ibraheem05: Ibraheem O, Adewale IO, Afolayan A (2005). "Purification and properties of glucose 6-phosphate dehydrogenase from Aspergillus aculeatus." J Biochem Mol Biol 38(5);584-90. PMID: 16202239

Iyer02: Iyer RB, Wang J, Bachas LG (2002). "Cloning, expression, and characterization of the gsdA gene encoding thermophilic glucose-6-phosphate dehydrogenase from Aquifex aeolicus." Extremophiles 6(4);283-9. PMID: 12215813

Julian61: Julian GR, Wolfe RG, Reithel FJ (1961). "The enzymes of mammary gland. II. The preparation of glucose 6-phosphate dehydrogenase." J Biol Chem 236;754-8. PMID: 13790996

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

Miclet01: Miclet E, Stoven V, Michels PA, Opperdoes FR, Lallemand JY, Duffieux F (2001). "NMR spectroscopic analysis of the first two steps of the pentose-phosphate pathway elucidates the role of 6-phosphogluconolactonase." J Biol Chem 276(37);34840-6. PMID: 11457850

Noltmann61: Noltmann EA, Gubler CJ, Kuby SA (1961). "Glucose 6-phosphate dehydrogenase (Zwischenferment). I. Isolation of the crystalline enzyme from yeast." J Biol Chem 236;1225-30. PMID: 13729473

Olavarria12: Olavarria K, Valdes D, Cabrera R (2012). "The cofactor preference of glucose-6-phosphate dehydrogenase from Escherichia coli--modeling the physiological production of reduced cofactors." FEBS J 279(13);2296-309. PMID: 22519976

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 Pathway Tools version 19.5 (software by SRI International) on Sun May 1, 2016, biocyc14.