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MetaCyc Reaction: 1.2.1.12

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

EC Number: 1.2.1.12

Enzymes and Genes:

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

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

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, 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, and some reactions have been computationally balanced for hydrogen by adding free protons. 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): -15.19458 Inferred 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 SRI International Pathway Tools version 19.0 on Tue Sep 1, 2015, BIOCYC14A.