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MetaCyc Reaction: 1.2.1.12

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

EC Number: 1.2.1.12

Enzymes and Genes:

Arabidopsis thaliana col: chloroplastic glyceraldehyde 3-phosphate dehydrogenaseInferred from experiment: GapA-1
Bacillus coagulans: glyceraldehyde-3-phosphate dehydrogenaseInferred from experiment: gap
Escherichia coli K-12 substr. MG1655: glyceraldehyde 3-phosphate dehydrogenaseInferred from experiment: gapA
Glycine max: NAD-dependent glyceraldehyde-3-phosphate dehydrogenaseInferred from experiment
Haloarcula vallismortis: glyceraldehyde 3-phosphate dehydrogenaseInferred from experiment
Homo sapiens:
Lactobacillus delbrueckii bulgaricus: glyceraldehyde-3-phosphate dehydrogenaseInferred from experiment: gap
Mycoplasma pneumoniae M129: glyceraldehyde-3-phosphate dehydrogenaseInferred from experiment: gapA
Ogataea angusta: glyceraldehyde-3-phosphate dehydrogenase: GPD
Pinus sylvestris: NAD-dependent glyceraldehyde-3-phosphate dehydrogenaseInferred from experiment: GapCp1
Solanum tuberosum: glyceraldehyde 3-phosphate dehydrogenaseInferred from experiment: GAPC
Streptococcus mutans: NAD+-dependent glyceraldehyde-3-phosphate dehydrogenaseInferred from experiment: gapC
Synechocystis sp. PCC 6803: glyceraldehyde 3-phosphate dehydrogenase 2: gap2
Thermotoga maritima: glyceraldehyde-3-phosphate dehydrogenaseInferred from experiment: gap

In Pathway: glycolysis IV (plant cytosol), formaldehyde assimilation III (dihydroxyacetone cycle), gluconeogenesis III, superpathway of glucose and xylose degradation, glycolysis II (from fructose 6-phosphate), glycolysis III (from glucose), heterolactic fermentation, Bifidobacterium shunt, sucrose biosynthesis I (from photosynthesis), glycolysis I (from glucose 6-phosphate), gluconeogenesis I, glycerol degradation to butanol

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

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.

Direct generic reaction:
D-glyceraldehyde 3-phosphate + NAD(P)+ + phosphate ↔ 1,3-bisphospho-D-glycerate + NAD(P)H + H+ (1.2.1.59)

Enzyme Commission Primary Name: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)

Enzyme Commission Synonyms: triosephosphate dehydrogenase, dehydrogenase, glyceraldehyde phosphate, phosphoglyceraldehyde dehydrogenase, 3-phosphoglyceraldehyde dehydrogenase, NAD+-dependent glyceraldehyde phosphate dehydrogenase, glyceraldehyde phosphate dehydrogenase (NAD+), glyceraldehyde-3-phosphate dehydrogenase (NAD+), NADH-glyceraldehyde phosphate dehydrogenase, glyceraldehyde-3-P-dehydrogenase

Standard Gibbs Free Energy (ΔrG in kcal/mol): -15.19458Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Also acts very slowly on D-glyceraldehyde and some other aldehydes; thiols can replace phosphate.

Citations: [CORI48, HAGEMAN55]

Gene-Reaction Schematic

Gene-Reaction Schematic

Instance reactions of [D-glyceraldehyde 3-phosphate + NAD(P)+ + phosphate ↔ 1,3-bisphospho-D-glycerate + NAD(P)H + H+] (1.2.1.59):
i1: D-glyceraldehyde 3-phosphate + NADP+ + phosphate ← 1,3-bisphospho-D-glycerate + NADPH + H+ (1.2.1.13)

i2: D-glyceraldehyde 3-phosphate + NAD+ + phosphate ↔ 1,3-bisphospho-D-glycerate + NADH + H+ (1.2.1.12)

Unification Links: KEGG:R01061, Rhea:10300

Relationship Links: BRENDA:EC:1.2.1.12, ENZYME:EC:1.2.1.12, IUBMB-ExplorEnz:EC:1.2.1.12, UniProt:RELATED-TO:O04106, UniProt:RELATED-TO:O25902, UniProt:RELATED-TO:O32755, UniProt:RELATED-TO:O34425, UniProt:RELATED-TO:O49222, UniProt:RELATED-TO:O59841, UniProt:RELATED-TO:O67161, UniProt:RELATED-TO:O68075, UniProt:RELATED-TO:O83816, UniProt:RELATED-TO:P00356, UniProt:RELATED-TO:P00357, UniProt:RELATED-TO:P00358, UniProt:RELATED-TO:P00359, UniProt:RELATED-TO:P00360, UniProt:RELATED-TO:P00361, UniProt:RELATED-TO:P00362, UniProt:RELATED-TO:P04406, UniProt:RELATED-TO:P04796, UniProt:RELATED-TO:P04797, UniProt:RELATED-TO:P04970, UniProt:RELATED-TO:P07486, UniProt:RELATED-TO:P07487, UniProt:RELATED-TO:P08439, UniProt:RELATED-TO:P08477, UniProt:RELATED-TO:P08735, UniProt:RELATED-TO:P09124, UniProt:RELATED-TO:P09316, UniProt:RELATED-TO:P09317, UniProt:RELATED-TO:P0A9B2, UniProt:RELATED-TO:P0A9B6, UniProt:RELATED-TO:P10097, UniProt:RELATED-TO:P10618, UniProt:RELATED-TO:P16858, UniProt:RELATED-TO:P17244, UniProt:RELATED-TO:P17329, UniProt:RELATED-TO:P17330, UniProt:RELATED-TO:P17331, UniProt:RELATED-TO:P17721, UniProt:RELATED-TO:P17729, UniProt:RELATED-TO:P17819, UniProt:RELATED-TO:P17878, UniProt:RELATED-TO:P19089, UniProt:RELATED-TO:P20287, UniProt:RELATED-TO:P20445, UniProt:RELATED-TO:P22512, UniProt:RELATED-TO:P22513, UniProt:RELATED-TO:P23722, UniProt:RELATED-TO:P24746, UniProt:RELATED-TO:P24748, UniProt:RELATED-TO:P24749, UniProt:RELATED-TO:P24750, UniProt:RELATED-TO:P24751, UniProt:RELATED-TO:P25858, UniProt:RELATED-TO:P25861, UniProt:RELATED-TO:P26517, UniProt:RELATED-TO:P26518, UniProt:RELATED-TO:P26519, UniProt:RELATED-TO:P26520, UniProt:RELATED-TO:P26521, UniProt:RELATED-TO:P26988, UniProt:RELATED-TO:P28844, UniProt:RELATED-TO:P29272, UniProt:RELATED-TO:P29497, UniProt:RELATED-TO:P32635, UniProt:RELATED-TO:P32636, UniProt:RELATED-TO:P32637, UniProt:RELATED-TO:P32638, UniProt:RELATED-TO:P32809, UniProt:RELATED-TO:P32810, UniProt:RELATED-TO:P34783, UniProt:RELATED-TO:P34917, UniProt:RELATED-TO:P34918, UniProt:RELATED-TO:P34920, UniProt:RELATED-TO:P34922, UniProt:RELATED-TO:P34924, UniProt:RELATED-TO:P35143, UniProt:RELATED-TO:P39460, UniProt:RELATED-TO:P44304, UniProt:RELATED-TO:P46406, UniProt:RELATED-TO:P46713, UniProt:RELATED-TO:P46795, UniProt:RELATED-TO:P47543, UniProt:RELATED-TO:P49644, UniProt:RELATED-TO:P50321, UniProt:RELATED-TO:P50322, UniProt:RELATED-TO:P54118, UniProt:RELATED-TO:P54270, UniProt:RELATED-TO:P55971, UniProt:RELATED-TO:P64178, UniProt:RELATED-TO:P75358, UniProt:RELATED-TO:P78958, UniProt:RELATED-TO:P80534, UniProt:RELATED-TO:Q7LZR1, UniProt:RELATED-TO:Q7M2K2, UniProt:RELATED-TO:Q7M187, UniProt:RELATED-TO:Q7M188, UniProt:RELATED-TO:Q7M516, UniProt:RELATED-TO:Q7M517, UniProt:RELATED-TO:Q9JWT8, UniProt:RELATED-TO:Q9JX51, UniProt:RELATED-TO:Q9UW96, UniProt:RELATED-TO:Q00584, UniProt:RELATED-TO:Q01077, UniProt:RELATED-TO:Q01558, UniProt:RELATED-TO:Q01597, UniProt:RELATED-TO:Q01651, UniProt:RELATED-TO:Q07234, UniProt:RELATED-TO:Q08060, UniProt:RELATED-TO:Q09054, UniProt:RELATED-TO:Q27820, UniProt:RELATED-TO:Q27890, UniProt:RELATED-TO:Q37264, UniProt:RELATED-TO:Q37265, UniProt:RELATED-TO:Q42671, UniProt:RELATED-TO:Q43247, UniProt:RELATED-TO:Q43359, UniProt:RELATED-TO:Q43833, UniProt:RELATED-TO:Q46450, UniProt:RELATED-TO:Q48335, UniProt:RELATED-TO:Q58546, UniProt:RELATED-TO:Q59309, UniProt:RELATED-TO:Q59800, UniProt:RELATED-TO:Q59906, UniProt:RELATED-TO:Q60143, UniProt:RELATED-TO:Q64467


References

CORI48: CORI GT, SLEIN MW, CORI CF (1948). "Crystalline d-glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle." J Biol Chem 173(2);605-18. PMID: 18910716

HAGEMAN55: HAGEMAN RH, ARNON DI (1955). "The isolation of triosephosphate dehydrogenase from pea seeds." Arch Biochem Biophys 55(1);162-8. PMID: 14362612

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


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 Wed May 4, 2016, biocyc14.