Information on EC 1.2.1.12 - glyceraldehyde-3-phosphate dehydrogenase (phosphorylating):

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EC NUMBERCOMMENTARY
1.2.1.12-

RECOMMENDED NAMEGeneOntology No.
glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)GO:0008943

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
bi-uni-uni-uni-ping-pong mechanism in which NAD+ and phosphate interact sequentially with the enzyme, followed in turn by the release of 3-phospho-D-glyceroyl phosphate, the addition of D-glyceraldehyde-3-phosphate, and the release of NADH. At pH 7.2, NAD+ binds to the enzyme in a rapid-equilibrium fashion, whereas at pH 8.8 there is rapid-equilibrium addition of both NAD+ and phosphate to the enzymeGlycine max-287920
D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
B-specific oxidoreductaseEscherichia coliP0A9B2287927
D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
ordered ter bi mechanism characterized by the sequential addition of NAD+, glyceraldehyde 3-phosphate and phosphate to the enzyme and the sequential release of 3-phospho-D-glyceroyl phosphate and NADH from the enzymeHomo sapiens-287945
D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
oxidation----
oxidationArabidopsis thaliana--663144, 673587, 676334
oxidationHomo sapiens--671066, 671070, 673629
oxidationOryctolagus cuniculus--672402
oxidationSpinacia oleracea--673587, 676334
oxidationKluyveromyces marxianus--674688
PhosphorylationSolanum tuberosumQ8LK04-675137
PhosphorylationRattus norvegicus--676108
PhosphorylationPlasmodium falciparumQ8IKK7-677046
redox reaction----
reduction----
reductionArabidopsis thaliana--663144, 673587, 676334
reductionPlasmodium falciparum--671063
reductionHomo sapiens--671066, 671070, 673629
reductionOryctolagus cuniculus--672402
reductionSpinacia oleracea--673587, 676334
reductionKluyveromyces marxianus--674688

PATHWAYKEGG LinkMetaCyc Link
Bifidobacterium shunt-P124-PWY
formaldehyde assimilation III (dihydroxyacetone cycle)-P185-PWY
gluconeogenesis I-GLUCONEO-PWY
glycerol degradation to butanol-PWY-7003
glycolysis I-GLYCOLYSIS
glycolysis II (from fructose-6P)-PWY-5484
glycolysis III (glucokinase)-ANAGLYCOLYSIS-PWY
glycolysis IV (plant cytosol)-PWY-1042
heterolactic fermentation-P122-PWY
sucrose biosynthesis-SUCSYN-PWY
xylose degradation IV-PWY-6901

SYSTEMATIC NAMEIUBMB Comments
D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating)Also acts very slowly on D-glyceraldehyde and some other aldehydes; thiols can replace phosphate.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
3-phosphoglyceraldehyde dehydrogenase----
A4-GAPDHArabidopsis thaliana--673587, 676334
A4-GAPDHSpinacia oleracea--676334
A4-glyceraldehyde-3-phosphate dehydrogenaseArabidopsis thaliana--673587
AB-GAPDHArabidopsis thaliana--676334
AnBn-GAPDHSpinacia oleracea--673587
AsGAPDHAscaris suumQ95YJ4-656745
BARS-38----
CP 17/CP 18----
cytosolic NAD-dependent glyceraldehyde 3-P dehydrogenaseArabidopsis thalianaP25858, Q56WJ4-689409
cytosolic NAD-dependent glyceraldehyde 3-P dehydrogenaseOryctolagus cuniculus, Saccharomyces cerevisiae, Spinacia oleracea--689409
cytosolic phosphorylating glyceraldehyde-3-phosphate dehydrogenaseSolanum tuberosumQ8LK04-675137
D-glyceraldehyde-3-phosphate dehydrogenasePanulirus versicolorP56649-654051
D-glyceraldehyde-3-phosphate dehydrogenaseHomo sapiens--671070, 684120, 684972, 687602
D-glyceraldehyde-3-phosphate dehydrogenasePlasmodium falciparumQ8IKK7-677046
D-glyceraldehyde-3-phosphate dehydrogenaseBacillus megateriumP23722-682151
D-glyceraldehyde-3-phosphate dehydrogenaseMus musculus--685264, 688791
D-glyceraldehyde-3-phosphate dehydrogenaseOryctolagus cuniculus--686305, 687602
D-glyceraldehyde-3-phosphate dehydrogenaseRattus norvegicus--686305
D-glyceraldehyde-3-phosphate dehydrogenaseThermotoga maritima--686481
D-glyceraldehyde-3-phosphate dehydrogenaseLeishmania mexicanaQ27890-687934
D-glyceraldehyde-3-phosphate: NAD+ oxidoreductase (phosphorylating)Rattus norvegicus--688949
dehydrogenase, glyceraldehyde phosphate----
dihydrogenase, glyceraldehyde phosphate----
G3PD----
G3PDHomo sapiens--673629, 685025
G3PDHPlasmodium brasilianumB0F3R1-687069
G3PDHPlasmodium coatneyiB0F3R2-687069
G3PDHPlasmodium cynomolgiB0F3R8-687069
G3PDHPlasmodium falciparumB0F3R3-687069
G3PDHPlasmodium fragileB0F3R4-687069
G3PDHPlasmodium knowlesi strain HB0F3R5-687069
G3PDHPlasmodium malariaeB0F3R6-687069
G3PDHPlasmodium reichenowiB0F3R7-687069
G3PDHPlasmodium vivaxB0F3R9-687069
GADPHHomo sapiens--697687
GAP1Staphylococcus aureus--710757
GapAArabidopsis thaliana-A4 isoform of GAPDH663144
GapAArabidopsis thaliana--676334
GapBArabidopsis thaliana-resulting from the fusion of GapA with the C-terminal half of the regulatory peptide CP12676334
GAPCSolanum tuberosumQ8LK04-675137
GapC-1Arabidopsis thaliana--700811
GapC1Arabidopsis thalianaP25858, Q56WJ4isozyme689409
GapC2Arabidopsis thalianaP25858, Q56WJ4isozyme689409
GAPDBos taurus, Canis lupus familiaris, Homo sapiens, Mus musculus, Oryctolagus cuniculus-somatic isoenzyme of glyceraldehyde-3-phosphate dehydrogenase685292
GAPDH----
GAPDHPanulirus versicolorP56649-654051
GAPDHOryctolagus cuniculus--654080, 654437, 670846, 672402, 673706, 685334, 685613, 686305, 686481, 686849, 687602, 689409, 713466
GAPDHTrypanosoma cruzi--654711, 684403, 684427
GAPDHHomo sapiens--654849, 654850, 654926, 671066, 671070, 672330, 673706, 676259, 684120, 684972, 685294, 686080, 686867, 687584, 687602, 688250, 688661, 712640
GAPDHPleurodeles waltlQ8AXB5-655270
GAPDHXenopus laevis--655270
GAPDHRattus norvegicus--656072, 674503, 685334, 686305, 688949
GAPDHBos taurus--656594
GAPDHAscaris suumQ95YJ4-656745
GAPDHArabidopsis thaliana--663144, 673587, 689409
GAPDHCavia porcellus--670846
GAPDHPlasmodium falciparum--671063
GAPDHGeobacillus stearothermophilus--672306
GAPDHSpinacia oleracea--673587, 676334, 689409
GAPDHParacoccidioides brasiliensisQ8X1X3-673986
GAPDHLactococcus lactis ssp. cremoris--674222
GAPDHStreptococcus pyogenesP0C0G6-674559
GAPDHKluyveromyces marxianus--674688
GAPDHMammalia--675023
GAPDHSolanum tuberosumQ8LK04-675137
GAPDHBacillus megaterium--679982, 682151
GAPDHSardina pilchardus--684121
GAPDHCamelus dromedarius--684127
GAPDHMus musculus--685264, 685334, 688791
GAPDHEntamoeba histolytica--686053, 686607, 687842
GAPDHThermotoga maritima--686481
GAPDHEscherichia coli--687114
GAPDHLactobacillus plantarum--687344
GAPDHLactobacillus crispatus--687380
GAPDHLeishmania mexicanaQ27890-687934
GAPDHNeisseria meningitidis--688953
GAPDHSaccharomyces cerevisiae--689409
GAPDHLentinus polychrousD3K1B6-710790
GAPDHCryptosporidium parvum--711617
GAPDH1----
GAPDH1Staphylococcus aureus--712766
GAPDH2----
GAPDSRattus norvegicus--676108
GAPDSBos taurus, Canis lupus familiaris, Homo sapiens, Mus musculus, Oryctolagus cuniculus-sperm-specific isoenzyme of glyceraldehyde-3-phosphate dehydrogenase685292
GAPDSHomo sapiensO14556sperm-specific GADPH685294
GAPNNeisseria meningitidis--688953
glyceraldehyde 3-phosphate dehydrogenaseHomo sapiens--686080
glyceraldehyde 3-phosphate dehydrogenaseCryptosporidium parvum--711617
glyceraldehyde phosphate dehydrogenase (NAD)----
glyceraldehyde-3 phosphate dehydrogenaseEntamoeba histolyticaQ27646-686053
glyceraldehyde-3-P-dehydrogenase----
glyceraldehyde-3-phosphate dehydrogenaseTrypanosoma cruzi--654711
glyceraldehyde-3-phosphate dehydrogenaseHomo sapiens--654850, 671066, 672330, 673629, 673706, 676259
glyceraldehyde-3-phosphate dehydrogenaseArabidopsis thaliana--663144, 673587, 676334
glyceraldehyde-3-phosphate dehydrogenaseOryctolagus cuniculus--670846, 672402, 673706
glyceraldehyde-3-phosphate dehydrogenaseCavia porcellus--670846
glyceraldehyde-3-phosphate dehydrogenasePlasmodium falciparum--671063, 677046
glyceraldehyde-3-phosphate dehydrogenaseGeobacillus stearothermophilus--672306
glyceraldehyde-3-phosphate dehydrogenaseSpinacia oleracea--673587, 676334
glyceraldehyde-3-phosphate dehydrogenaseParacoccidioides brasiliensisQ8X1X3-673986
glyceraldehyde-3-phosphate dehydrogenaseLactococcus lactis ssp. cremoris--674222
glyceraldehyde-3-phosphate dehydrogenaseRattus norvegicus--674503, 676108
glyceraldehyde-3-phosphate dehydrogenaseStreptococcus pyogenesP0C0G6-674559
glyceraldehyde-3-phosphate dehydrogenaseKluyveromyces marxianus--674688
glyceraldehyde-3-phosphate dehydrogenaseMammalia--675023
glyceraldehyde-3-phosphate dehydrogenaseSolanum tuberosumQ8LK04-675137
glyceraldehyde-3-phosphate dehydrogenase (NAD)----
glyceraldehyde-3-phosphate dehydrogenase 1Staphylococcus aureus--710757
GPD----
Gra3PDH----
GraP-DH----
HsGAPDHHomo sapiens--671070
kmGAPDH1pKluyveromyces marxianus-formerly referred to as p37674688
Larval antigen OVB95----
Major larval surface antigen----
NAD+-G-3-P dehydrogenase----
NAD-dependent glyceraldehyde phosphate dehydrogenase----
NAD-dependent glyceraldehyde-3-phosphate dehydrogenase----
NAD-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenaseNeisseria meningitidis--688953
NAD-dependent phosphorylating glyceraldehyde-3-phosphate dehydrogenaseNeisseria meningitidis--688953
NAD-G3PDH----
NADH-glyceraldehyde phosphate dehydrogenase----
P-37----
PfGAPDHPlasmodium falciparum--671063, 677046
phosphoglyceraldehyde dehydrogenase----
phosphorylating NAD+-dependent GAPDHTetrahymena pyriformis--688066
Plasmin receptor----
Plasminogen-binding protein----
pmGAPDHCavia porcellus--670846
rmGAPDHOryctolagus cuniculus--670846
TDH1Saccharomyces cerevisiae--655286
TLAb----
triose phosphate dehydrogenase----

CAS REGISTRY NUMBERCOMMENTARY
9001-50-7-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Acipenser sp.-287964, 287967--Manually annotated by BRENDA team
Acipenser transmontanus-287942--Manually annotated by BRENDA team
Antheraea mylitta-695391--Manually annotated by BRENDA team
Apis mellifera-287971, 287976--Manually annotated by BRENDA team
Arabidopsis thaliana-656414, 663144, 673587, 676334, 700672, 700811--Manually annotated by BRENDA team
Arabidopsis thalianaecotype Columbia; isoform GapC1689409P25858UniProtManually annotated by BRENDA team
Arabidopsis thalianaisoform GapC2689409Q56WJ4UniProtManually annotated by BRENDA team
Arabidopsis thalianaisoform GAPCp1700836Q9SAJ6UniProtManually annotated by BRENDA team
Arabidopsis thalianaisoform GAPCp2700836Q84WR0UniProtManually annotated by BRENDA team
Ascaris suum-656745Q95YJ4UniprotManually annotated by BRENDA team
Bacillus cereus-287967, 287974--Manually annotated by BRENDA team
Bacillus coagulansKU287944, 287963--Manually annotated by BRENDA team
Bacillus coagulans KUKU287944--Manually annotated by BRENDA team
Bacillus megaterium-682151P23722SwissProtManually annotated by BRENDA team
Bacillus megateriumstrain DSM319679982P23722SwissProtManually annotated by BRENDA team
Bacillus megaterium DSM319strain DSM319679982P23722SwissProtManually annotated by BRENDA team
Bacillus subtilis-287980--Manually annotated by BRENDA team
Bombus appositus-287971, 287976--Manually annotated by BRENDA team
Bombus nevadensis-287971, 287976--Manually annotated by BRENDA team
Bombus occidentalis-287971, 287976--Manually annotated by BRENDA team
Bos taurus-287905, 287911, 287967, 287979, 656594, 685292--Manually annotated by BRENDA team
Bradyrhizobium japonicumCB1809287902--Manually annotated by BRENDA team
Bradyrhizobium japonicum CB1809CB1809287902--Manually annotated by BRENDA team
Caenorhabditis elegans-287918, 287928--Manually annotated by BRENDA team
Camelus dromedarius-684127--Manually annotated by BRENDA team
Canis lupus familiaris-287967, 685292--Manually annotated by BRENDA team
Cavia porcellus-670846--Manually annotated by BRENDA team
Cryptosporidium parvum-697008, 711617Q7YYQ9UniProtManually annotated by BRENDA team
Cyanophora paradoxa-11542--Manually annotated by BRENDA team
Dissostichus mawsoni-287978--Manually annotated by BRENDA team
Drosophila melanogaster-287924--Manually annotated by BRENDA team
Dunaliella salina-697508B1PL92UniProtManually annotated by BRENDA team
Emericella nidulans-287915--Manually annotated by BRENDA team
Emericella nidulansoverproducing transformant and wild-type strain287903--Manually annotated by BRENDA team
Entamoeba histolytica-687842--Manually annotated by BRENDA team
Entamoeba histolyticafragment686053Q27646UniProtManually annotated by BRENDA team
Entamoeba histolyticafragment; strain HM1686607Q27646UniProtManually annotated by BRENDA team
Entamoeba histolytica HM1fragment; strain HM1686607Q27646UniProtManually annotated by BRENDA team
Escherichia coli-287967, 287977, 287983, 698374, 699988--Manually annotated by BRENDA team
Escherichia coli-698925P0A9B2UniProtManually annotated by BRENDA team
Escherichia colienterohemorrhagic strain 86-24h11and enteropathogenic strain E2348/69687114--Manually annotated by BRENDA team
Escherichia coliwild-type and mutant enzymes N313T, Y317A, Y317G and N313T/Y317G287927P0A9B2UniProtManually annotated by BRENDA team
Euglena gracilis-287973--Manually annotated by BRENDA team
Felis catus-287967--Manually annotated by BRENDA team
Gallus gallus-287967--Manually annotated by BRENDA team
Geobacillus stearothermophilus-287900, 287909, 287917, 287926, 287946, 287962, 287967, 287970, 654653, 672306--Manually annotated by BRENDA team
Geobacillus stearothermophilus-287985, 656119P00362UniprotManually annotated by BRENDA team
Geobacillus stearothermophiluswild-type and mutant W84F287947--Manually annotated by BRENDA team
Geobacillus stearothermophiluswild-type enzyme and mutant C149selenocysteine287984--Manually annotated by BRENDA team
Glycine max-287902, 287920--Manually annotated by BRENDA team
Haloarcula vallismortis-287907--Manually annotated by BRENDA team
Hippoglossus sp.halibut287967--Manually annotated by BRENDA team
Homo sapiens-287900, 287910, 287913, 287925, 287932, 287945, 287950, 287967, 654849, 654850, 654926, 657393, 671070, 672330, 673629, 673706, 676259, 684120, 684972, 685025, 685292, 686080, 686867, 688250, 688661, 695298, 695602, 695939, 696174, 696824, 698989, 699035, 699592, 700133, 700503, 712640--Manually annotated by BRENDA team
Homo sapiens-671066, 685294, 687584, 687602, 697687, 698825P04406SwissProtManually annotated by BRENDA team
Homo sapiens-685294O14556UniProtManually annotated by BRENDA team
Huso huso-287942--Manually annotated by BRENDA team
Hypocrea koningiiunder conditions of koningic acid production the koningic-acid-resistant isoenzyme GAPDH I is produced. In peptone-rich medium where non koningic acid is produced the koningic-acid-sensitive isoenzyme GAPDH II is produced in addition to GAPDH II287908--Manually annotated by BRENDA team
Kluyveromyces marxianus-674688--Manually annotated by BRENDA team
Lactobacillus crispatusstrain ST1687380--Manually annotated by BRENDA team
Lactobacillus plantarum-701175--Manually annotated by BRENDA team
Lactobacillus plantarumstrain LA 318687344--Manually annotated by BRENDA team
Lactobacillus plantarum LA 318-701175--Manually annotated by BRENDA team
Lactococcus lactis-712937--Manually annotated by BRENDA team
Lactococcus lactis ssp. cremorisMG1363 and relA acid-resistant mutant674222--Manually annotated by BRENDA team
Leishmania mexicana-287986--Manually annotated by BRENDA team
Leishmania mexicana-687934Q27890UniprotManually annotated by BRENDA team
Lentinus polychrouscommonly known as hed kradang710790D3K1B6UniProtManually annotated by BRENDA team
Lentinus polychrous KPM3commonly known as hed kradang710790D3K1B6UniProtManually annotated by BRENDA team
Lobster-287967--Manually annotated by BRENDA team
Mammalia-675023--Manually annotated by BRENDA team
Marsilea quadrifolia-287956O65843UniprotManually annotated by BRENDA team
Meleagris gallopavo-287967--Manually annotated by BRENDA team
Mesocricetus auratus-699035--Manually annotated by BRENDA team
Mus musculus-287957, 287958, 287982, 685264, 685292, 685334, 688791, 699686--Manually annotated by BRENDA team
Neisseria meningitidisstrain Z2491688953--Manually annotated by BRENDA team
Neisseria meningitidis Z2491strain Z2491688953--Manually annotated by BRENDA team
Oplegnathus fasciatusisoform GAPDH1698019B5AAJ5UniProtManually annotated by BRENDA team
Oplegnathus fasciatusisoform GAPDH2698019B5AAJ6UniProtManually annotated by BRENDA team
Oryctolagus cuniculus-287900, 287904, 287926, 287933, 287934, 287946, 287953, 287957, 287959, 287965, 287967, 287969, 287972, 287978, 287981, 288344, 3247, 654080, 654437, 670846, 672402, 673706, 685292, 685334, 685613, 686305, 686481, 686849, 687602, 689409, 695902, 696421, 698989, 713466--Manually annotated by BRENDA team
Palinurus vulgaris-287951--Manually annotated by BRENDA team
Panulirus versicolor-287987--Manually annotated by BRENDA team
Panulirus versicolor-654051P56649UniprotManually annotated by BRENDA team
Paracoccidioides brasiliensis-673986Q8X1X3UniprotManually annotated by BRENDA team
Phenylobacterium immobile Estrain E, ATCC 30005688066--Manually annotated by BRENDA team
Pinus sylvestris-287922, 287956--Manually annotated by BRENDA team
Pisum sativum-287936, 287967--Manually annotated by BRENDA team
Plasmodium brasilianumfragment; strain Peru II687069B0F3R1UniProtManually annotated by BRENDA team
Plasmodium brasilianum Peru IIfragment; strain Peru II687069B0F3R1UniProtManually annotated by BRENDA team
Plasmodium coatneyifragment687069B0F3R2UniProtManually annotated by BRENDA team
Plasmodium cynomolgifragment; strain Berok687069B0F3R8UniProtManually annotated by BRENDA team
Plasmodium cynomolgi Berokfragment; strain Berok687069B0F3R8UniProtManually annotated by BRENDA team
Plasmodium falciparum-671063--Manually annotated by BRENDA team
Plasmodium falciparum-677046Q8IKK7SwissProtManually annotated by BRENDA team
Plasmodium falciparumfragment; strain FVO687069B0F3R3UniProtManually annotated by BRENDA team
Plasmodium falciparum FVOfragment; strain FVO687069B0F3R3UniProtManually annotated by BRENDA team
Plasmodium fragilefragment; strain Nilgiri687069B0F3R4UniProtManually annotated by BRENDA team
Plasmodium fragile Nilgirifragment; strain Nilgiri687069B0F3R4UniProtManually annotated by BRENDA team
Plasmodium knowlesi strain Hfragment687069B0F3R5UniProtManually annotated by BRENDA team
Plasmodium malariaefragment; strain Uganda I687069B0F3R6UniProtManually annotated by BRENDA team
Plasmodium malariae Uganda Ifragment; strain Uganda I687069B0F3R6UniProtManually annotated by BRENDA team
Plasmodium reichenowifragment; strain CDC1687069B0F3R7UniProtManually annotated by BRENDA team
Plasmodium reichenowi CDC1fragment; strain CDC1687069B0F3R7UniProtManually annotated by BRENDA team
Plasmodium vivaxfragment; strain Salvador I687069B0F3R9UniProtManually annotated by BRENDA team
Plasmodium vivax Salvadorfragment; strain Salvador I687069B0F3R9UniProtManually annotated by BRENDA team
Pleurodeles waltl-655270Q8AXB5SwissProtManually annotated by BRENDA team
Pseudomonas aeruginosa-287919--Manually annotated by BRENDA team
Pseudomonas sp.strain pi9, antarctic psychrophilic bacterium698639A7LHM7UniProtManually annotated by BRENDA team
Pseudomonas sp. pi9strain pi9, antarctic psychrophilic bacterium698639A7LHM7UniProtManually annotated by BRENDA team
Psithyrus suckleyi-287971, 287976--Manually annotated by BRENDA team
Rattus norvegicus-287913, 287925, 287929, 287960, 287967, 656072, 657393, 685334, 686305, 688949--Manually annotated by BRENDA team
Rattus norvegicus-696464P04797UniprotManually annotated by BRENDA team
Rattus norvegicus-698925Q9ESV6UniProtManually annotated by BRENDA team
Rattus norvegicusa two-hybrid interaction assay is performed, using as bait the mouse Kir6.2 C terminus, for the screening a rat heart cDNA library is used674503--Manually annotated by BRENDA team
Rattus norvegicusdiabetic rat695595--Manually annotated by BRENDA team
Rattus norvegicusSprague-Dawley rat676108--Manually annotated by BRENDA team
Saccharomyces cerevisiae-287899, 287931, 287937, 287943, 287952, 287954, 287967, 287975, 288344, 655286, 689409--Manually annotated by BRENDA team
Saccharomyces cerevisiaehigh-affnity cAMP-binding protein I and II287948--Manually annotated by BRENDA team
Sardina pilchardusEuropean pilchard684121--Manually annotated by BRENDA team
Schistosoma mansoni-698033--Manually annotated by BRENDA team
Sinapis alba-287923--Manually annotated by BRENDA team
Solanum tuberosum-675137Q8LK04SwissProtManually annotated by BRENDA team
Spinacia oleracea-287935, 287961, 288344, 673587, 676334, 689409--Manually annotated by BRENDA team
Staphylococcus aureus-710757, 712766Q6GIL8UniProtManually annotated by BRENDA team
Staphylococcus aureusstrain MRSA252, isoform GapA1695363Q6GIL8UniProtManually annotated by BRENDA team
Staphylococcus aureus MRSA252strain MRSA252, isoform GapA1695363Q6GIL8UniProtManually annotated by BRENDA team
Starmerella bombicola-699355B3FPE3UniProtManually annotated by BRENDA team
Streptococcus equinus-697507--Manually annotated by BRENDA team
Streptococcus oralis-698256--Manually annotated by BRENDA team
Streptococcus pneumoniae-655720Q97NL1SwissProtManually annotated by BRENDA team
Streptococcus pyogenes-674559P0C0G6UniprotManually annotated by BRENDA team
Streptomyces arenaeTÜ469, contains pentalenolactone-insensitive glyceraldehyde-3-phosphate dehydrogenase under conditions of production of pentalenolactone. In complex medium no pentalenolactone production is observed and a pentalenolactone-sensitive D-glyceraldehyde 3-phosphate dehydrogenase, rather than the insensitive enzyme can be detected287930--Manually annotated by BRENDA team
Sus scrofa-287914, 287934, 287966, 287967, 3246--Manually annotated by BRENDA team
Tetrahymena pyriformisstrain E, ATCC 30005688066--Manually annotated by BRENDA team
Thermotoga maritima-287906, 686481--Manually annotated by BRENDA team
Thermus aquaticus-287946, 287967--Manually annotated by BRENDA team
Thermus thermophilus-287926, 287938--Manually annotated by BRENDA team
Thermus thermophilusstrain HB 8287968--Manually annotated by BRENDA team
Thermus thermophilus HB 8strain HB 8287968--Manually annotated by BRENDA team
Trypanosoma brucei-287900, 287901--Manually annotated by BRENDA team
Trypanosoma cruzi-287912, 654711, 684403, 684427, 696735--Manually annotated by BRENDA team
Trypanosoma cruzi-696747P22513UniprotManually annotated by BRENDA team
Vigna radiata var. radiata-287949--Manually annotated by BRENDA team
Xanthomonas campestrisGAPDH is constitutively expressed700056Q4UY27UniProtManually annotated by BRENDA team
Xenopus laevis-655270--Manually annotated by BRENDA team
Zymomonas mobilis-287916, 3241--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
metabolismStreptococcus equinus-GAPDH is not involved in the control of the glycolytic flux. A strain overproducing GAPDH shows a high NADH-to-NAD+ ratio, but no significant differences in growth rate when grown on glucose or lactose697507
metabolismEscherichia coli-replacement of Escherichia coli GapA glyceraldehyde 3-phosphate dehydrogenase by Clostridium acetobutylicum GapC glyceraldehyde 3-phosphate dehydrogenase, EC 1.2.1.9 results in significant reduction of flux through the pentose phosphate pathway. Recombinant strains display increased NADPH availability, and consistently higher productivity than parent strains699988
physiological functionDunaliella salinaB1PL92reduction of transcription by 41% and 67% using RNAi leads to transformants with sluggish motility and less active than wild-type697508
physiological functionStreptococcus oralis-interaction of GAPDH with Porphyromonas gingivalis major fimbrae plays an important role in Porphyromonas gingivalis colonization. Amino acid residues 166 to 183 of Streptococcus oralis GAPDH exhibit the strongest binding activity toward rFimA, and the synthetic peptide corresponding to amino acid residues 166 to 183 of GAPDH, peptide DNFGVVEGLMTTIHAYTG inhibits Streptococcus oralis-Porphyromonas gingivalis biofilm formation in a dose-dependent manner. The peptide inhibits interbacterial biofilm formation by several oral streptococci and Porphyromonas gingivalis strains with different types of FimA698256
physiological functionHomo sapiens-GAPDH physically associates with DNA repair enzyme APE1. This interaction allows GAPDH to convert the oxidized species of APE1 to the reduced form, thereby reactivating its endonuclease activity to cleave abasic sites698825
physiological functionXanthomonas campestrisQ4UY27a GAPDH-deficient mutant can still grow in medium with glucose or other sugars as the sole carbon source, and no phosphofructokinase activity is detectable.The mutant can not utilize pyruvate as sole carbon source, whereas the wild-type can. Inactivation of GAPDH results in impairment of bacterial growth and virulence in the host plant, and reduction of intracellular ATP and extracellularpolysaccharide700056
physiological functionHomo sapiens-downregulation of GAPDH using siRNA reduces both macrophage colony stimulating factor CSF-1 mRNA and protein levels, through destabilizing CSF-1 mRNA. CSF-1 mRNA half-lives are decreased by 50% in the presence of GAPDH siRNA. GAPDH associates with a large AU-rich containing regionof CSF-1700133
physiological functionHomo sapiens-GAPDH is a translational suppressor of angiotensin II type 1 receptor expression and mediates the effect of H2O2 on angiotensin II type 1 receptor mRNA700503
physiological functionArabidopsis thaliana-GAPDH controls generation of H2O2 by the proapoptotic family member Bax and heat shock, which in turn suppresses cell death in yeast and plant cells700672
physiological functionArabidopsis thaliana-gapc-1 null mutant line shows a delay in growth, morpholigical alterations in siliques, and low seed number. Embryo development is altered, showing abortions and empty embryonic sacs in basal and apical siliques, respectively. Mutant shows a decrease in ATP levels and reduced respiratory rate as well as a decrease in the expression and activity of aconitase and succinate dehydrogenase and reduced levels of pyruvate and several Krebs cycle intermediates, and increased reactive oxygen species levels700811
physiological functionArabidopsis thalianaQ84WR0, Q9SAJ6double mutants lacking both plastidial isoforms gapcp1 and gapcp2 display a drastic phenotype of arrested root development, dwarfism, and sterility. In spite of their low gene expression level, GAPCp down-regulation leads to altered gene expression and to drastic changes in the sugar and amino acid balance of the plant. GAPCps are important for the synthesis of serine in roots. Serine supplementation to the growth medium rescues root developmental arrest and restores normal levels of carbohydrates and sugar biosynthetic activities in gapcp double mutants; double mutants lacking both plastidial isoforms gapcp1 and gapcp2 display a drastic phenotype of arrested root development, dwarfism, and sterility. In spite of their low gene expression level, GAPCp down-regulation leads to altered gene expression and to drastic changes in the sugar and amino acid balance of the plant. GAPCps are important for the synthesis of serine in roots. Serine supplementation to the growth medium rescues root developmental arrest and restores normal levels of carbohydrates and sugar biosynthetic activities in gapcp double mutants700836
physiological functionLactobacillus plantarum-the adhesion mechanism of the lactobacilli is in part due to GAPDH binding to human ABO-type blood group antigens expressed on human colonic mucin. After periodate oxidation of colonic mucin, adhesion of Lactobacillus plantarum LA 318 bacterial cells significantly decreases compared to normal human colonic mucin. High binding is observed to A and B group antigens, while binding to H group antigen is lower. No interaction is observed between GAPDH and various monosaccharides. GAPDH binding to the B-trisaccharide biotinyl polymer probe [Gala1-3 (Fuca1-2) Gal-] is significantly higher as compared to B-disaccharide, Lewis D-trisaccharide, 3-fucosyl-N-acetylglucosamine and a-N-acetylneuraminic acid biotinyl polymer-probes701175
physiological functionLentinus polychrousD3K1B6the GAPDH gene product is a heat shock protein which might be involved in the developmental phase of the Lentinus polychrous710790

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate
LITERATURE/
Substrate
COMMENTARY/
Product
LITERATURE/
Product
Reversibility
r=reversible
ir=irreversible
?=not specified
3-phospho-D-glyceroyl phosphate + NADHD-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
Homo sapiens--287932--?
3-phospho-D-glyceroyl phosphate + NADHD-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
Homo sapiens--287900, 287913, 287932--r
3-phospho-D-glyceroyl phosphate + NADHD-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
Sus scrofa--287934--r
3-phospho-D-glyceroyl phosphate + NADHD-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
Saccharomyces cerevisiae--287899-287899?
3-phospho-D-glyceroyl phosphate + NADHD-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
Saccharomyces cerevisiae--287931-287931r
3-phospho-D-glyceroyl phosphate + NADHD-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
Saccharomyces cerevisiae--287937--r
3-phospho-D-glyceroyl phosphate + NADHD-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
Bos taurus--287979--r
3-phospho-D-glyceroyl phosphate + NADHD-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
Oryctolagus cuniculus--287900, 287933, 287934, 287946--r
3-phospho-D-glyceroyl phosphate + NADHD-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
Euglena gracilis--287973--r
3-phospho-D-glyceroyl phosphate + NADHD-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
Geobacillus stearothermophilus--287900, 287909, 287946--r
3-phospho-D-glyceroyl phosphate + NADHD-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
Pisum sativum--287936--r
3-phospho-D-glyceroyl phosphate + NADHD-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
Trypanosoma brucei--287900--r
3-phospho-D-glyceroyl phosphate + NADHD-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
Thermotoga maritima--287906--r
3-phospho-D-glyceroyl phosphate + NADHD-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
Streptomyces arenae--287930--r
3-phospho-D-glyceroyl phosphate + NADHD-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
Emericella nidulans-enzyme plays a central role in glyconeogenesis287915--?
3-phospho-D-glyceroyl phosphate + NADH + H+D-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
Spinacia oleracea--673587, 676334--?
3-phospho-D-glyceroyl phosphate + NADH + H+D-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
Arabidopsis thaliana--663144, 673587, 676334--?
acetaldehyde + phosphate + NAD+acetyl phosphate + NADH
show the reaction diagram
Neisseria meningitidis--688953---
acetaldehyde + phosphate + NAD+acetyl phosphate + NADH
show the reaction diagram
Homo sapiens-enzyme form E6.6 shows 27% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E6.8 shows 9% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E8.5 shows 6% of the actity with D-glyceraldehyde 3-phosphate, enzyme form E9.0 shows 0.4% of the activity with D-glyceraldehyde 3-phosphate287913--?
acetaldehyde 3-phosphate + NAD+? + NADH
show the reaction diagram
Neisseria meningitidis--688953--?
arsenate + GSH + NAD+ + glyceraldehyde 3-phosphatearsenite + ?
show the reaction diagram
Homo sapiens, Rattus norvegicus--657393--?
butyraldehyde + phosphate + NAD+butyryl phosphate + NADH
show the reaction diagram
Homo sapiens-enzyme form E6.6 shows 10% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E6.8 shows 15% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E8.5 shows 12% of the actity with D-glyceraldehyde 3-phosphate, enzyme form E9.0 shows 0.9% of the activity with D-glyceraldehyde 3-phosphate287913--?
D-glyceraldehyde 3-phosphate + 3-acetylpyridine hypoxanthine nucleotide + phosphate3-phospho-D-glyceroyl phosphate + ?
show the reaction diagram
Dissostichus mawsoni-1.3% of the activity with NAD+287978--?
D-glyceraldehyde 3-phosphate + 3-acetylpyridine hypoxanthine nucleotide + phosphate3-phospho-D-glyceroyl phosphate + ?
show the reaction diagram
Oryctolagus cuniculus-3.2% of activity with NAD+287978--?
D-glyceraldehyde 3-phosphate + 3-acetylpyridine NAD+ + phosphate3-phospho-D-glyceroyl phosphate + ?
show the reaction diagram
Saccharomyces cerevisiae--287937--?
D-glyceraldehyde 3-phosphate + 3-acetylpyridine NAD+ + phosphate3-phospho-D-glyceroyl phosphate + ?
show the reaction diagram
Dissostichus mawsoni-2.8% of the activity with NAD+287978--?
D-glyceraldehyde 3-phosphate + 3-acetylpyridine NAD+ + phosphate3-phospho-D-glyceroyl phosphate + ?
show the reaction diagram
Oryctolagus cuniculus-4.5% of activity with NAD+287978--?
D-glyceraldehyde 3-phosphate + arsenate + NAD+3-phospho-D-glyceroyl arsenate + NADH
show the reaction diagram
Homo sapiens--287932, 287950--?
D-glyceraldehyde 3-phosphate + arsenate + NAD+3-phospho-D-glyceroyl arsenate + NADH
show the reaction diagram
Sus scrofa--287934--?
D-glyceraldehyde 3-phosphate + arsenate + NAD+3-phospho-D-glyceroyl arsenate + NADH
show the reaction diagram
Saccharomyces cerevisiae--287937--ir
D-glyceraldehyde 3-phosphate + arsenate + NAD+3-phospho-D-glyceroyl arsenate + NADH
show the reaction diagram
Bos taurus--287979--?
D-glyceraldehyde 3-phosphate + arsenate + NAD+3-phospho-D-glyceroyl arsenate + NADH
show the reaction diagram
Oryctolagus cuniculus--287934---
D-glyceraldehyde 3-phosphate + arsenate + NAD+3-phospho-D-glyceroyl arsenate + NADH
show the reaction diagram
Oryctolagus cuniculus--287969--ir
D-glyceraldehyde 3-phosphate + arsenate + NAD+3-phospho-D-glyceroyl arsenate + NADH
show the reaction diagram
Geobacillus stearothermophilus--287970--ir
D-glyceraldehyde 3-phosphate + arsenate + NAD+3-phospho-D-glyceroyl arsenate + NADH
show the reaction diagram
Streptomyces arenae--287930--?
D-glyceraldehyde 3-phosphate + arsenate + NAD+3-phospho-D-glyceroyl arsenate + NADH
show the reaction diagram
Thermus thermophilus-the product arseno-3-phosphoglycerate is decomposed readily to 3-phosphoglycerate287938--ir
D-glyceraldehyde 3-phosphate + C8-(4-(2,2,6,6-tetramethyl-piperidinyl-1-oxyl))-NAD+ + phosphate3-phospho-D-glyceroyl phosphate + C8-(4-(2,2,6,6-tetramethyl-piperidinyl-1-oxyl))-NADH
show the reaction diagram
Huso huso--287942--?
D-glyceraldehyde 3-phosphate + N6-(2-carboxyethyl)-NAD+ + phosphate3-phospho-D-glyceroyl phosphate + N6-(2-carboxyethyl)-NADH
show the reaction diagram
Thermus thermophilus, Oryctolagus cuniculus, Geobacillus stearothermophilus--287926--?
D-glyceraldehyde 3-phosphate + N6-(4-(2,2,6,6-tetramethyl-piperidinyl-1-oxyl))-NAD+ + phosphate3-phospho-D-glyceroyl phosphate + N6-(4-(2,2,6,6-tetramethyl-piperidinyl-1-oxy))-NADH
show the reaction diagram
Huso huso--287942--?
D-glyceraldehyde 3-phosphate + NAD+D-3-phosphoglycerate + NADH
show the reaction diagram
Neisseria meningitidis--688953--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Gallus gallus, Meleagris gallopavo--287967-287967-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Cyanophora paradoxa--11542-11542-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Vigna radiata var. radiata--287949-287949?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Drosophila melanogaster--287924-287924-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Thermus aquaticus--287946-287946-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Thermus aquaticus--287967-287967?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Bacillus subtilis--287980-287980-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Mus musculus--287957-287957-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Mus musculus--287958-287958-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Mus musculus--287982-287982-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Thermus thermophilus--287926-287926-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Thermus thermophilus--287938-287938-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Thermus thermophilus--287968-287968-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Escherichia coliP0A9B2-287927-287927-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Escherichia coli--287967-287967-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Escherichia coli--287977-287977-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Escherichia coli--287983-287983-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Homo sapiens--287910-287910?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Homo sapiens--287925-287925?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Homo sapiens--287945-287945?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Homo sapiens--287950-287950?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Homo sapiens--287967-287967?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Homo sapiens--696174, 712640--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Homo sapiens--287900-287900r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Homo sapiens--287913-287913r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Homo sapiens--287932-287932r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Rattus norvegicus--287913-287913-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Rattus norvegicus--287925-287925?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Rattus norvegicus--287929-287929?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Rattus norvegicus--287960-287960?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Rattus norvegicus--287967-287967?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Sus scrofa--3246-3246-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Sus scrofa--287914-287914-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Sus scrofa--287966-287966-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Sus scrofa--287967-287967-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Sus scrofa--287934-287934r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Saccharomyces cerevisiae--287899-287899-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Saccharomyces cerevisiae--287943-287943-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Saccharomyces cerevisiae--287948-287948-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Saccharomyces cerevisiae--287952-287952-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Saccharomyces cerevisiae--287954-287954-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Saccharomyces cerevisiae--287967-287967-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Saccharomyces cerevisiae--287975-287975-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Saccharomyces cerevisiae--288344-288344-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Saccharomyces cerevisiae--287931-287931r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Saccharomyces cerevisiae--287937-287937r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Bos taurus--287905-287905?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Bos taurus--287911-287911?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Bos taurus--287967-287967?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Bos taurus--287979-287979r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Oryctolagus cuniculus--3247-3247?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Oryctolagus cuniculus--287926-287926?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Oryctolagus cuniculus--287953-287953?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Oryctolagus cuniculus--287957-287957?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Oryctolagus cuniculus--287959-287959?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Oryctolagus cuniculus--287965-287965?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Oryctolagus cuniculus--287967-287967?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Oryctolagus cuniculus--287969-287969?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Oryctolagus cuniculus--287972-287972?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Oryctolagus cuniculus--287978-287978?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Oryctolagus cuniculus--287981-287981?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Oryctolagus cuniculus--288344-288344?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Oryctolagus cuniculus--713466--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Oryctolagus cuniculus--287900-287900r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Oryctolagus cuniculus--287933-287933r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Oryctolagus cuniculus--287934-287934r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Oryctolagus cuniculus--287946-287946r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Euglena gracilis--287973-287973r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Geobacillus stearothermophilus--287917-287917?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Geobacillus stearothermophilus--287926-287926?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Geobacillus stearothermophilus--287947-287947?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Geobacillus stearothermophilus--287962-287962?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Geobacillus stearothermophilus--287967-287967?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Geobacillus stearothermophilus--287970-287970?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Geobacillus stearothermophilus--287984-287984?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Geobacillus stearothermophilusP00362-287985-287985?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Geobacillus stearothermophilus--654653--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Geobacillus stearothermophilus--287900-287900r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Geobacillus stearothermophilus--287909-287909r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Geobacillus stearothermophilus--287946-287946r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Emericella nidulans--287903-287903-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Emericella nidulans--287915-287915-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Bradyrhizobium japonicum--287902-287902-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Spinacia oleracea--287935-287935-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Spinacia oleracea--287961-287961-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Spinacia oleracea--288344-288344-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Pisum sativum--287967-287967-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Pisum sativum--287936-287936r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Glycine max--287902-287902?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Glycine max--287920-287920?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Pseudomonas aeruginosa--287919-287919-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Trypanosoma brucei--287901-287901-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Trypanosoma brucei--287900-287900r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Haloarcula vallismortis--287907-287907?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Canis lupus familiaris, Bacillus cereus--287967-287967-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Bacillus cereus--287974-287974-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Xenopus laevis--655270--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Caenorhabditis elegans--287918-287918-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Caenorhabditis elegans--287928-287928-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Trypanosoma cruzi--287912-287912-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Trypanosoma cruzi--696735--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Trypanosoma cruziP22513-696747--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Felis catus--287967-287967-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Bacillus coagulans--287944-287944-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Bacillus coagulans--287963-287963-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Apis mellifera--287971-287971-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Apis mellifera--287976-287976-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Pinus sylvestris--287922-287922-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Pinus sylvestris--287956-287956-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Leishmania mexicana--287986-287986-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Zymomonas mobilis--3241-3241-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Zymomonas mobilis--287916-287916-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Lobster--287967-287967-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Thermotoga maritima--287906-287906r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Sinapis alba--287923-287923-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Hypocrea koningii--287908-287908?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Panulirus versicolor--287987-287987-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Streptomyces arenae--287930-287930r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Huso huso, Acipenser transmontanus--287942-287942-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Palinurus vulgaris--287951-287951-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Marsilea quadrifoliaO65843-287956-287956-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Acipenser sp.--287964-287964-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Acipenser sp., Hippoglossus sp.--287967-287967-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Bombus nevadensis--287971-287971-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Bombus nevadensis--287976-287976-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Bombus occidentalis--287971-287971-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Bombus occidentalis--287976-287976-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Bombus appositus--287971-287971-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Bombus appositus--287976-287976-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Psithyrus suckleyi--287971-287971-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Psithyrus suckleyi--287976-287976-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Dissostichus mawsoni--287978-287978-
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Pleurodeles waltlQ8AXB5-655270--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Cryptosporidium parvumQ7YYQ9-697008--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Cryptosporidium parvum--711617--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Pseudomonas sp.A7LHM7-698639--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Staphylococcus aureusQ6GIL8-710757--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Staphylococcus aureus--712766--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Lentinus polychrousD3K1B6-710790--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Oryctolagus cuniculus-hydride transfer is a major rate-limiting step287904-287904?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Bacillus subtilis-glycolytic enzyme287980--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Homo sapiens-glycolytic enzyme287925---
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Homo sapiens-glycolytic enzyme287945--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Emericella nidulans-enzyme plays a central role in glycolysis287915--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Escherichia coli-key enzyme of glycolysis287983--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Haloarcula vallismortis-key enzyme of glycolysis287907--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Huso huso, Acipenser transmontanus-key enzyme of glycolysis287942--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Hypocrea koningii-GAPDH I is responsible for glycolysis when koningic acid is produced287908--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Pinus sylvestris-enzyme is involved in cytosolic glycolysis287922--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Homo sapiens-absolute specificity for NAD+695298--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Lactobacillus plantarum--687344--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Mus musculus--685292, 685334, 688791--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Escherichia coli--687114--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Homo sapiens--671070, 673629, 684120, 684972, 685025, 685292, 686080, 688250, 688661--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Rattus norvegicus--676108, 685334, 686305, 688949--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Saccharomyces cerevisiae--689409--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Bos taurus--685292--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Oryctolagus cuniculus--672402, 685292, 685334, 685613, 686305, 686481, 687602, 689409--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Tetrahymena pyriformis--688066--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Spinacia oleracea--689409--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Entamoeba histolytica--687842--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Lactococcus lactis--712937--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Canis lupus familiaris--685292--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Neisseria meningitidis--688953--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Trypanosoma cruzi--684427--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Trypanosoma cruzi--684403--r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Kluyveromyces marxianus--674688--r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Plasmodium falciparum--671063--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Leishmania mexicanaQ27890-687934--r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Camelus dromedarius--684127--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Thermotoga maritima--686481--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Lactobacillus crispatus--687380--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Plasmodium falciparumQ8IKK7-677046--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Homo sapiensO14556-685294--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Homo sapiens--687602--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Homo sapiensP04406-671066--r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Homo sapiens--687584--r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Sardina pilchardus--684121--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Entamoeba histolyticaQ27646-686607--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Entamoeba histolyticaQ27646-686053--r
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Plasmodium falciparumB0F3R3-687069--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Plasmodium reichenowiB0F3R7-687069--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Plasmodium knowlesi strain HB0F3R5-687069--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Plasmodium coatneyiB0F3R2-687069--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Plasmodium cynomolgiB0F3R8-687069--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Plasmodium vivaxB0F3R9-687069--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Plasmodium fragileB0F3R4-687069--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Plasmodium brasilianumB0F3R1-687069--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Plasmodium malariaeB0F3R6-687069--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Arabidopsis thalianaP25858, Q56WJ4-689409--?
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Geobacillus stearothermophilus-activity assay672306--?
D-glyceraldehyde 3-phosphate + poly(ethylene glycol)-bound NAD+ + phosphate3-phospho-D-glyceroyl phosphate + poly(ethylene glycol)-bound NADH
show the reaction diagram
Thermus thermophilus, Oryctolagus cuniculus, Geobacillus stearothermophilus--287926--?
D-glyceraldehyde 3-phosphate + thio-NAD+ + phosphate3-phospho-D-glyceroyl phosphate + thio-NADH
show the reaction diagram
Dissostichus mawsoni-7.2% of the activity with NAD+287978--?
D-glyceraldehyde 3-phosphate + thio-NAD+ + phosphate3-phospho-D-glyceroyl phosphate + thio-NADH
show the reaction diagram
Pisum sativum-thionicotinamide adenine dinucleotide is not as effective as NAD+287936--?
D-glyceraldehyde 3-phosphate + thio-NAD+ + phosphate3-phospho-D-glyceroyl phosphate + thio-NADH
show the reaction diagram
Oryctolagus cuniculus-9.3% of activity with NAD+287978--?
DL-glyceraldehyde + phosphate + NAD+D-glyceroyl phosphate + NADH
show the reaction diagram
Homo sapiens-enzyme form E6.6 shows no activity, enzyme form E6.8 shows 2.5% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E8.5 shows 30% of the actity with D-glyceraldehyde 3-phosphate, enzyme form E9.0 shows 3.0% of the activity with D-glyceraldehyde 3-phosphate287913--?
erythrose 4-phosphate + phosphate + NAD+? + NADH
show the reaction diagram
Homo sapiens-enzyme form E6.6 shows no activity, enzyme form E6.8 shows 1.2% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E8.5 shows 25% of the actity with D-glyceraldehyde 3-phosphate, enzyme form E9.0 shows 1.5% of the activity with D-glyceraldehyde 3-phosphate287913--?
glucose + phosphate + NAD+? + NADH
show the reaction diagram
Homo sapiens-enzyme form E6.6 shows no activity, enzyme form E6.8 shows 0.6% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E8.5 shows 6.0% of the actity with D-glyceraldehyde 3-phosphate, enzyme form E9.0 shows 0.8% of the activity with D-glyceraldehyde 3-phosphate287913--?
p-nitrophenyl acetate + H2Op-nitrophenol + acetate
show the reaction diagram
Escherichia coli--287977--?
propionaldehyde + phosphate + NAD+propionyl phosphate + NADH
show the reaction diagram
Homo sapiens-enzyme form E6.6 shows 33% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E6.8 shows 12% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E8.5 shows 10% of the actity with D-glyceraldehyde 3-phosphate, enzyme form E9.0 shows 0.8% of the activity with D-glyceraldehyde 3-phosphate287913--?
valeraldehyde + phosphate + NAD+pentanoyl phosphate + NADH
show the reaction diagram
Homo sapiens-enzyme form E6.6 shows no activity, enzyme form E6.8 shows 19% of the activity with D-glyceraldehyde 3-phosphate, enzyme form E8.5 shows 18% of the actity with D-glyceraldehyde 3-phosphate, enzyme form E9.0 shows 0.9% of the activity with D-glyceraldehyde 3-phosphate287913--?
glyceraldehyde + NAD+? + NADH
show the reaction diagram
Neisseria meningitidis--688953--?
additional information?-Geobacillus stearothermophilus-mutant enzyme C149selenocysteine shows selenoperoxidase activity with tert-butyl hydroperoxide and 3-carboxy 4-nitrobenzenethiol. Wild-type enzyme has no peroxidase activity287984---
additional information?-Geobacillus stearothermophilus-mutant enzyme L187A/P188S is catalytically active not only with NAD+, as the wild-type enzyme, but also with NADP+287909---
additional information?-Bacillus subtilis-wild-type enzyme has no activity with NADP+, the mutant enzyme D32A/L187N shows catalytic efficiency with NADP+ higher than that with NAD+287980---
additional information?-Neisseria meningitidis-no activity with NADP+688953---
additional information?-Emericella nidulans-the overproducing transformant grows faster and more efficient than the wild-type strain287903---
additional information?-Saccharomyces cerevisiae-the isoproteins TLAb-a and TLAb-2 change depending on the cell growth phase, the carbon source and sodium chloride shock287899---
additional information?-Saccharomyces cerevisiae-high-affinity binding of cAMP to D-glyceraldehyde 3-phosphate dehydrogenase may significantly reduce intracellular cAMP287948---
additional information?-Caenorhabditis elegans-activity of isoenzyme 2 increases during postembryonic development287928---
additional information?-Homo sapiens-enzyme is regulated by ATP and by D-glyceraldehyde 3-phosphate287945---
additional information?-Pseudomonas aeruginosa-importance of the enzyme in glucose catabolism. Activity is reduced severalfold after growth on gluconeogenic substrates such as citrate compared to growth on glucose287919---
additional information?-Homo sapiens-classical glycolytic protein involved exclusively in cytosolic energy production654849---
additional information?-Homo sapiens-hypoxia upregulates the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase in endothelial cells through a 5'-hypoxic regulatory element. Cell-specific patterns of HIF-1alpha and HIF-2alpha expression lead to cell-specific gene upregulation during hypoxia654850---
additional information?-Saccharomyces cerevisiae-NADH-reductive stress in Saccharomyces cerevisiae induces the expression of the minor isoform of glyceraldehyde-3-phosphate dehydrogenase, TDH1655286---
additional information?-Oryctolagus cuniculus-oxidation of GAPDH could be the signal for binding with nucleic acids and for change of quarternary structure. Theses events could facilitate GAPDH functioning in DNA reparation and tRNA transportation during oxidative stress654437---
additional information?-Rattus norvegicus-plays a role in microtubule dynamics in the early secretory pathway656072---
additional information?-Streptococcus pneumoniaeQ97NL1the concerted action of both alpha-enolase and GAPDH on the bacterial cell surface might result in an enhancement of the pathogen‘s ability to degrade the extracellular matrix and to invade host tissues655720---
additional information?-Bos taurus-the enzyme is a GABA(A) receptor kinase linking glycolysis to neuronal inhibition656594---
additional information?-Oryctolagus cuniculus-oxidation of SH-groups of the active site of GAPDH enhances its binding with total transfer RNA or with total DNA. Both NAD+ and NADH inhibit GAPDH-RNA or GAPDH-DNA interaction654437---
additional information?-Streptococcus pneumoniaeQ97NL1the enzyme has a specific plasmin- and plasminogen-binding activity, high affinity for plasmin and significantly lower affinity for plasminogen655720---
additional information?-Lactobacillus crispatus-binds plasminogen687380---
additional information?-Mus musculus-GAPDH is a Ca2+-dependent substrate of phosphorylase kinase although the rate of phosphorylation is very slow685264---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)
COMMENTARY PRODUCTLITERATURE
(Product)
3-phospho-D-glyceroyl phosphate + NADHD-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
Emericella nidulans-enzyme plays a central role in glyconeogenesis287915--
3-phospho-D-glyceroyl phosphate + NADH + H+D-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
Spinacia oleracea--673587, 676334--
3-phospho-D-glyceroyl phosphate + NADH + H+D-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
Arabidopsis thaliana--663144, 673587, 676334--
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Staphylococcus aureusQ6GIL8-710757--
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Bacillus subtilis-glycolytic enzyme287980--
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Homo sapiens-glycolytic enzyme287925, 287945--
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Emericella nidulans-enzyme plays a central role in glycolysis287915--
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Escherichia coli-key enzyme of glycolysis287983--
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Haloarcula vallismortis-key enzyme of glycolysis287907--
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Huso huso, Acipenser transmontanus-key enzyme of glycolysis287942--
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Hypocrea koningii-GAPDH I is responsible for glycolysis when koningic acid is produced287908--
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
Pinus sylvestris-enzyme is involved in cytosolic glycolysis287922--
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Homo sapiens--671070, 673629--
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Rattus norvegicus--676108--
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Oryctolagus cuniculus--672402--
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Kluyveromyces marxianus--674688--
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Plasmodium falciparum--671063--
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Plasmodium falciparumQ8IKK7-677046--
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Homo sapiensP04406-671066--
D-glyceraldehyde 3-phosphate + phosphate + NAD+3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
Geobacillus stearothermophilus-activity assay672306--
additional information?-Emericella nidulans-the overproducing transformant grows faster and more efficient than the wild-type strain287903--
additional information?-Saccharomyces cerevisiae-the isoproteins TLAb-a and TLAb-2 change depending on the cell growth phase, the carbon source and sodium chloride shock287899--
additional information?-Saccharomyces cerevisiae-high-affinity binding of cAMP to D-glyceraldehyde 3-phosphate dehydrogenase may significantly reduce intracellular cAMP287948--
additional information?-Caenorhabditis elegans-activity of isoenzyme 2 increases during postembryonic development287928--
additional information?-Homo sapiens-enzyme is regulated by ATP and by D-glyceraldehyde 3-phosphate287945--
additional information?-Pseudomonas aeruginosa-importance of the enzyme in glucose catabolism. Activity is reduced severalfold after growth on gluconeogenic substrates such as citrate compared to growth on glucose287919--
additional information?-Homo sapiens-classical glycolytic protein involved exclusively in cytosolic energy production654849--
additional information?-Homo sapiens-hypoxia upregulates the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase in endothelial cells through a 5'-hypoxic regulatory element. Cell-specific patterns of HIF-1alpha and HIF-2alpha expression lead to cell-specific gene upregulation during hypoxia654850--
additional information?-Saccharomyces cerevisiae-NADH-reductive stress in Saccharomyces cerevisiae induces the expression of the minor isoform of glyceraldehyde-3-phosphate dehydrogenase, TDH1655286--
additional information?-Oryctolagus cuniculus-oxidation of GAPDH could be the signal for binding with nucleic acids and for change of quarternary structure. Theses events could facilitate GAPDH functioning in DNA reparation and tRNA transportation during oxidative stress654437--
additional information?-Rattus norvegicus-plays a role in microtubule dynamics in the early secretory pathway656072--
additional information?-Streptococcus pneumoniaeQ97NL1the concerted action of both alpha-enolase and GAPDH on the bacterial cell surface might result in an enhancement of the pathogen‘s ability to degrade the extracellular matrix and to invade host tissues655720--
additional information?-Bos taurus-the enzyme is a GABA(A) receptor kinase linking glycolysis to neuronal inhibition656594--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
3-acetylpyridine hypoxanthine nucleotideDissostichus mawsoni-1.3% of the activity with NAD+287978 2D-image
3-acetylpyridine hypoxanthine nucleotideOryctolagus cuniculus-3.2% of activity with NAD+287978 2D-image
3-acetylpyridine-NAD+Saccharomyces cerevisiae--287937 2D-image
3-acetylpyridine-NAD+Dissostichus mawsoni-2.8% of the activity with NAD+287978 2D-image
3-acetylpyridine-NAD+Oryctolagus cuniculus-4.5% of activity with NAD+ as cofactor287978 2D-image
C6-(4-(2,2,6,6-tetramethyl-piperidinyl-1-oxyl))-NAD+Huso huso-can replace NAD+ as cofactor287942-
N6-(2-carboxyethyl)-NAD+Geobacillus stearothermophilus, Oryctolagus cuniculus, Thermus thermophilus-can replace NAD+ as cofactor287926 2D-image
NAD+Cyanophora paradoxa--11542 2D-image
NAD+Saccharomyces cerevisiae--287899, 287943, 287948, 287952, 287954, 287967, 287975, 288344, 689409 2D-image
NAD+Trypanosoma brucei--287900, 287901 2D-image
NAD+Oryctolagus cuniculus--287900, 287904, 287933, 287934, 287946, 287953, 287957, 287965, 287967, 287969, 287972, 287978, 287981, 288344, 3247, 654437, 685292, 685334, 685613, 686305, 686481, 687602, 689409, 713466 2D-image
NAD+Geobacillus stearothermophilus--287900, 287909, 287917, 287962, 287967, 287984, 654653 2D-image
NAD+Homo sapiens--287900, 287910, 287913, 287925, 287932, 287945, 287967, 684120, 684972, 685025, 685292, 686080, 687584, 687602, 688250, 688661, 712640 2D-image
NAD+Bradyrhizobium japonicum, Glycine max--287902 2D-image
NAD+Emericella nidulans--287903, 287915 2D-image
NAD+Bos taurus--287905, 287911, 287967, 287979, 685292 2D-image
NAD+Thermotoga maritima--287906, 686481 2D-image
NAD+Haloarcula vallismortis--287907 2D-image
NAD+Hypocrea koningii--287908 2D-image
NAD+Trypanosoma cruzi--287912, 684427, 696735 2D-image
NAD+Rattus norvegicus--287913, 287925, 287929, 287960, 287967, 685334, 686305, 688949 2D-image
NAD+Sus scrofa-NAD+-induced protein isomerization is the rate-limiting process for the formation of a catalytically competent holoenzyme287914 2D-image
NAD+Zymomonas mobilis--287916, 3241 2D-image
NAD+Caenorhabditis elegans--287918, 287928 2D-image
NAD+Pseudomonas aeruginosa--287919 2D-image
NAD+Glycine max-at pH 8.8 there is rapid-equilibrium addition of both NAD+ and phosphate to the enzyme287920 2D-image
NAD+Pinus sylvestris--287922, 287956 2D-image
NAD+Sinapis alba--287923 2D-image
NAD+Drosophila melanogaster--287924 2D-image
NAD+Geobacillus stearothermophilus, Oryctolagus cuniculus, Thermus thermophilus-poly(ethylene glycol)-bound NAD+ can replace NAD+ as cofactor287926 2D-image
NAD+Escherichia coli--287927, 287967, 287983, 687114 2D-image
NAD+Streptomyces arenae--287930 2D-image
NAD+Saccharomyces cerevisiae-activity with D-glyceraldehyde 3-phosphate in presence of 0.0006-0.006 mM NAD+: activity of the monomeric form is negligible or absent, high activity of the tetramer. 0.02-0.06 mM NAD+: markedly higher catalytic activity of the monomer. 2 mM NAD+: specific activities of monomeric and tetrameric forms are similar and equal to 0.06 mM/min. Activity with 3-phospho-D-glyceroyl phosphate: activity of the monomer is considerably higher than that of the tetramer287931 2D-image
NAD+Sus scrofa--287934, 287967, 3246 2D-image
NAD+Spinacia oleracea--287935, 288344, 689409 2D-image
NAD+Pisum sativum-contains 0.5-0.7 mol of NAD+ per mol of subunit287936 2D-image
NAD+Saccharomyces cerevisiae-weak binding of NAD+ to the enzyme287937 2D-image
NAD+Thermus thermophilus--287938, 287968 2D-image
NAD+Acipenser transmontanus, Huso huso--287942 2D-image
NAD+Bacillus coagulans--287944 2D-image
NAD+Thermus aquaticus--287946, 287967 2D-image
NAD+Geobacillus stearothermophilus-enzyme contains 4 equivalents of firmly bound NAD+287946, 287970 2D-image
NAD+Geobacillus stearothermophilus-effects of NAD+ binding on the luminescence of Trp84 and Trp310. NAD+-induced conformational change is sequential and subtle rearrangement in the structure of unligated subunits might be responsible for the negative cooperative behavior of NAD+ binding287947 2D-image
NAD+Vigna radiata var. radiata--287949 2D-image
NAD+Homo sapiens-contains 3.0-3.5 M of NAD+ bound per mol of tetramer287950 2D-image
NAD+Palinurus vulgaris-the binding of NAD+ to apoenzyme in solution at 25°C is anticooperative287951 2D-image
NAD+Marsilea quadrifoliaO65843-287956 2D-image
NAD+Mus musculus--287957, 287958, 287982, 685292, 685334 2D-image
NAD+Oryctolagus cuniculus-between three and four molecules of NAD+ bound per tetramer287959 2D-image
NAD+Spinacia oleracea-contains about 1.8 mol NAD+ per mol of enzyme287961 2D-image
NAD+Bacillus coagulans-enzyme contains 4 equivalents of firmly bound NAD+287963 2D-image
NAD+Acipenser sp.-negative cooperativity in nicotinamide adenine dinucleotide binding287964 2D-image
NAD+Sus scrofa-2-3 mol of tightly bound NAD+287966 2D-image
NAD+Bacillus cereus--287967, 287974 2D-image
NAD+Canis lupus familiaris--287967, 685292 2D-image
NAD+Acipenser sp., Felis catus, Gallus gallus, Hippoglossus sp., Lobster, Meleagris gallopavo, Pisum sativum--287967 2D-image
NAD+Bombus appositus, Bombus nevadensis, Bombus occidentalis, Psithyrus suckleyi--287971, 287976 2D-image
NAD+Apis mellifera-contains 4 mol of NAD+ per mol of enzyme287971 2D-image
NAD+Euglena gracilis--287973 2D-image
NAD+Apis mellifera--287976 2D-image
NAD+Escherichia coli-contains less than 0.3 mol of NAD+ per mol of native protein287977 2D-image
NAD+Dissostichus mawsoni-contains 4 mol of NAD+ per mol of enzyme287978 2D-image
NAD+Bacillus subtilis--287980 2D-image
NAD+Geobacillus stearothermophilus-dimers generated from the tetrameric enzyme are inactive but exhibit cooperativity in NAD+ binding287985 2D-image
NAD+Leishmania mexicana--287986 2D-image
NAD+Panulirus versicolor--287987 2D-image
NAD+Oryctolagus cuniculus-the cofactor is bound to two subunits of the tetrameric enzyme, which is consistent with the negative cooperativity of NAD+ binding to this enzyme654080 2D-image
NAD+Pleurodeles waltlQ8AXB5-655270 2D-image
NAD+Xenopus laevis--655270 2D-image
NAD+Sardina pilchardus-dependent684121 2D-image
NAD+Camelus dromedarius-dependent684127 2D-image
NAD+Trypanosoma cruzi-dependent684403 2D-image
NAD+Homo sapiensO14556; 685294 2D-image
NAD+Entamoeba histolytica--686053, 686607, 687842 2D-image
NAD+Plasmodium brasilianumB0F3R1-687069 2D-image
NAD+Plasmodium coatneyiB0F3R2-687069 2D-image
NAD+Plasmodium cynomolgiB0F3R8-687069 2D-image
NAD+Plasmodium falciparumB0F3R3-687069 2D-image
NAD+Plasmodium fragileB0F3R4-687069 2D-image
NAD+Plasmodium knowlesi strain HB0F3R5-687069 2D-image
NAD+Plasmodium malariaeB0F3R6-687069 2D-image
NAD+Plasmodium reichenowiB0F3R7-687069 2D-image
NAD+Plasmodium vivaxB0F3R9-687069 2D-image
NAD+Lactobacillus plantarum--687344 2D-image
NAD+Lactobacillus crispatus--687380 2D-image
NAD+Leishmania mexicanaQ27890dependent687934 2D-image
NAD+Tetrahymena pyriformis-dependent688066 2D-image
NAD+Mus musculus-GAPDH binds four NAD+ molecules per subunit688791 2D-image
NAD+Neisseria meningitidis-; absolute specificity for NAD+688953 2D-image
NAD+Arabidopsis thalianaP25858, Q56WJ4-689409 2D-image
NAD+Homo sapiens-absolute specifity for NAD+695298 2D-image
NAD+Staphylococcus aureusQ6GIL8-710757, 712766 2D-image
NAD+Lentinus polychrousD3K1B6-710790 2D-image
NAD+Cryptosporidium parvum--711617 2D-image
NAD+Lactococcus lactis--712937 2D-image
NADHSaccharomyces cerevisiae-cofactor287899, 287931, 287937 2D-image
NADHGeobacillus stearothermophilus-cofactor287900, 287909, 287946 2D-image
NADHHomo sapiens-cofactor287900, 287913, 287932 2D-image
NADHOryctolagus cuniculus-cofactor287900, 287933, 287934, 287946 2D-image
NADHTrypanosoma brucei-cofactor287900 2D-image
NADHThermotoga maritima-cofactor287906 2D-image
NADHStreptomyces arenae-cofactor287930 2D-image
NADHSus scrofa-cofactor287934 2D-image
NADHPisum sativum-cofactor287936 2D-image
NADHEuglena gracilis-cofactor287973 2D-image
NADHBos taurus-cofactor287979 2D-image
NADHOryctolagus cuniculus--654437, 670846, 672402 2D-image
NADHArabidopsis thaliana--663144, 673587, 676334 2D-image
NADHCavia porcellus--670846 2D-image
NADHPlasmodium falciparum-one molecule NAD+ is bound to each of the four subunits of the tetrameric enzyme671063 2D-image
NADHHomo sapiens-each subunit is bound to one NAD+671066 2D-image
NADHHomo sapiens--671070, 673629, 695298 2D-image
NADHGeobacillus stearothermophilus--672306 2D-image
NADHSpinacia oleracea--673587, 676334 2D-image
NADHLactococcus lactis ssp. cremoris--674222 2D-image
NADHKluyveromyces marxianus--674688 2D-image
NADHRattus norvegicus--676108 2D-image
NADHPlasmodium falciparumQ8IKK7-677046 2D-image
NADP+Bacillus subtilis-wild-type enzyme has no activity with NADP+. The mutant enzyme D32A/L187N shows catalytic efficiency with NADP+ higher than that with NAD+. Activity of mutant enzyme D32A with NAD+ is equal to that of the wild-type enzyme. Activity of mutant L187N with NAD+ is higher than that of the wild-type enzyme. Mutant enzymes D32A and L187N also show activity with NADP+, 3-7% of the activity with NAD+287980 2D-image
NADPHSpinacia oleracea--673587 2D-image
Thio-NAD+Pisum sativum-thionicotinamide adenine dinucleotide is not as effective as NAD+287936 2D-image
Thio-NAD+Dissostichus mawsoni-7.2% of the activity with NAD+287978 2D-image
Thio-NAD+Oryctolagus cuniculus-9.3% of activity with NAD+287978 2D-image
Thio-NAD+Panulirus versicolorP56649the coenzyme analogue binds in a non-productive manner, resulting in a disordered thionicotinamide ring and rearranged active-site residues, effective as substrate to replace NAD+654051 2D-image
C8-(4-(2,2,6,6-tetramethyl-piperidinyl-1-oxyl))-NAD+Huso huso-can replace NAD+ as cofactor287942-
additional informationNeisseria meningitidis-undetectable activity with NADP+688953-

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
(NH4)2SO4Thermus thermophilus-0.045 M, 10fold activation287938, 287968
CsClThermus thermophilus-activates287938
CsClThermus thermophilus-activates; maximal activation: 20fold287968
K+Haloarcula vallismortis-KCl, activity is enhanced by increasing concentrations of the salt287907
K+Thermus thermophilus-KCl, activates287938
K+Vigna radiata var. radiata-activates to a small extent below 0.1 M287949
K+Thermus thermophilus-maximal activation: 22fold287968
LiClHaloarcula vallismortis-activity is partly enhanced287907
LiClThermus thermophilus-activates287938
LiClThermus thermophilus-maximal activation: 10fold287968
Na2SO4Thermus thermophilus-up to 5fold activation287938, 287968
NaClHaloarcula vallismortis-activity is enhanced by increasing concentrations of the salt287907
NaClThermus thermophilus-up to 5fold activation287938
NH4ClHaloarcula vallismortis-activity is enhanced by increasing concentrations of the salt287907
NH4ClThermus thermophilus-0.1 M, 25fold activation287938, 287968
RbClHaloarcula vallismortis-activity is enhanced by increasing concentrations of the salt. Optimum activity in 3 M RbCl287907
ZnHomo sapiens-enzyme form E8.5 contains 0.64 gatoms of zinc per mol of enzyme, enzyme form E9.0 contain 2.76 gatom of zinc per mol of enzyme287913

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
(8E,11E)-C15:2-anacardic acidTrypanosoma cruziP22513-696747 2D-image
(8E,11E,14E)-C15:3-anacardic acidTrypanosoma cruziP22513-696747 2D-image
(E)-2-hydroxy-6-(pentadec-8-en-1-yl)benzoic acidTrypanosoma cruziP22513-696747 2D-image
(E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamideOryctolagus cuniculus-treatment with (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide between 0.001 and 1 mM induces the oligomerization of GAPDH, dithiothreitol reduces (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide-induced aggregation in a concentration-dependent manner687602 2D-image
(NH4)2SO4Haloarcula vallismortis--287907 2D-image
1-hydroxy-2-oxo-3,3-bis(2-aminoethyl)-1-triazeneHomo sapiens, Oryctolagus cuniculus--687602 2D-image
2'-deoxy-2'-[(quinolin-7-ylcarbonyl)amino]adenosineLeishmania mexicanaQ27890-687934 2D-image
2,3-diphosphoglycerateGlycine max--287920 2D-image
2,3-diphosphoglycerateHomo sapiens--287945 2D-image
2-(6-amino-2-methyl-9H-purin-9-yl)-5-(hydroxymethyl)tetrahydrofuran-3,4-diolLeishmania mexicanaQ27890-687934 2D-image
2-(dodec-1-en-1-yl)-6-hydroxybenzoic acidTrypanosoma cruzi-inhibition is not reversed or prevented by addition of Triton X-100. Noncompetitive with respect to both substrate and cofactor696735-
2-(hydroxymethyl)-5-[6-[(2-methylphenyl)amino]-9H-purin-9-yl]tetrahydrofuran-3,4-diolLeishmania mexicanaQ27890-687934 2D-image
2-(hydroxymethyl)-5-[6-[(3-methylbutyl)amino]-9H-purin-9-yl]tetrahydrofuran-3,4-diolLeishmania mexicanaQ27890-687934 2D-image
2-(hydroxymethyl)-5-[6-[(3-methylphenyl)amino]-9H-purin-9-yl]tetrahydrofuran-3,4-diolLeishmania mexicanaQ27890-687934 2D-image
2-methyl-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
2-pentadecyl-6-hydroxybenzoic acidTrypanosoma cruzi-inhibition is not reversed or prevented by addition of Triton X-100. Noncompetitive with respect to both substrate and cofactor696735-
2-[6-amino-8-(pyrimidin-2-ylsulfanyl)-9H-purin-9-yl]-5-(hydroxymethyl)tetrahydrofuran-3,4-diolLeishmania mexicanaQ27890-687934 2D-image
2-[9-(2-deoxy-2-[[(2,4-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-yl]-2,3-dihydroisoquinolineLeishmania mexicanaQ27890-687934 2D-image
3',4',5',5,7-pentamethoxyflavoneEntamoeba histolyticaQ27646-686053 2D-image
3',4'-methylenedioxy-5,6,7-trimethoxyflavoneEntamoeba histolyticaQ27646-686053 2D-image
3',5'-AMPApis mellifera--287971 2D-image
3-(1,3-benzodioxol-5-yl)-2-oxo-2H-chromen-6-ylacetateEntamoeba histolyticaQ27646-686053 2D-image
3-(1,3-benzodioxol-5-yl)-2-oxo-2H-chromen-7-ylacetateEntamoeba histolyticaQ27646-686053 2D-image
3-(1,3-benzodioxol-5-yl)-2-oxo-2H-chromen-8-ylacetateEntamoeba histolyticaQ27646-686053 2D-image
3-(1,3-benzodioxol-5-yl)-2H-chromen-2-oneEntamoeba histolyticaQ27646-686053 2D-image
3-(1,3-benzodioxol-5-yl)-6-hydroxy-2H-chromen-2-oneEntamoeba histolyticaQ27646-686053 2D-image
3-(1,3-benzodioxol-5-yl)-6-nitro-2H-chromen-2-oneEntamoeba histolyticaQ27646-686053 2D-image
3-(1,3-benzodioxol-5-yl)-6-[[(1E)-1H-indol-3-ylmethylene]amino]-2H-chromen-2-oneEntamoeba histolyticaQ27646-686053 2D-image
3-(1,3-benzodioxol-5-yl)-6-[[(1E)-1H-pyrrol-2-ylmethylene]amino]-2H-chromen-2-oneEntamoeba histolyticaQ27646-686053 2D-image
3-(1,3-benzodioxol-5-yl)-6-[[(1E)-2-furylmethylene]amino]-2H-chromen-2-oneEntamoeba histolyticaQ27646-686053 2D-image
3-(1,3-benzodioxol-5-yl)-6-[[(1E)-pyridin-2-ylmethylene]amino]-2H-chromen-2-oneEntamoeba histolyticaQ27646-686053 2D-image
3-(1,3-benzodioxol-5-yl)-6-[[(1E)-thien-2-ylmethylene]amino]-2H-chromen-2-oneEntamoeba histolyticaQ27646-686053 2D-image
3-(1,3-benzodioxol-5-yl)-7-hydroxy-2H-chromen-2-oneEntamoeba histolyticaQ27646-686053 2D-image
3-(1,3-benzodioxol-5-yl)-8-hydroxy-2H-chromen-2-oneEntamoeba histolyticaQ27646-686053 2D-image
3-(chloroacetyl)-pyridine adenine dinculeotideGeobacillus stearothermophilus--287909 2D-image
3-morpholino-sydnonimineMus musculus-the NO-generating compound inactivates by induction of a covalent binding of NAD+ to the enzyme. The superoxide anion released by 3-morpholino-sydnonimine potentiates the inactivation287982 2D-image
3-phospho-D-glyceroyl phosphatePisum sativum--287936 2D-image
5'-deoxy-5'-[(diphenylacetyl)amino]adenosineLeishmania mexicanaQ27890-687934 2D-image
5'-deoxy-5'-[[(4'-ethylbiphenyl-4-yl)carbonyl]amino]adenosineLeishmania mexicanaQ27890-687934 2D-image
6-amino-3-(1,3-benzodioxol-5-yl)-2H-chromen-2-oneEntamoeba histolyticaQ27646-686053 2D-image
6-phosphogluconatePseudomonas aeruginosa--287919 2D-image
9-(2-aminoethyl)-8-thiophen-2-yl-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(2,4-dichlorophenyl)carbonyl]amino]pentofuranosyl)-N-(3-hydroxynaphthalen-1-yl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(2,4-dichlorophenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-1-yl-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(2,4-dichlorophenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-2-yl-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(2,4-dihydroxyphenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-1-yl-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(2,4-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(3-hydroxynaphthalen-1-yl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(2,4-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-1-yl-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(2,4-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-2-yl-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(2-hydroxy-3-methoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(3,4-dihydroxyphenyl)carbonyl]amino]pentofuranosyl)-N-(naphthalen-1-ylmethyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(3,4-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(naphthalen-1-ylmethyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(3,5-dihydroxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(3,5-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(2-methylphenyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(3,5-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(3-methylphenyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(3,5-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-phenyl-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(3,5-dimethoxyphenyl)carbonyl]amino]pentofuranosyl)-N-[(3-methoxynaphthalen-1-yl)methyl]-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(3-ethoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(3-hydroxy-4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-1-yl-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(3-hydroxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(3-hydroxyphenyl)carbonyl]amino]pentofuranosyl)-N-(naphthalen-1-ylmethyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(3-hydroxyphenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-1-yl-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(3-methoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(3-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(2-methoxyphenyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(3-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-phenyl-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(3-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-[(7-methylnaphthalen-1-yl)methyl]-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(4-heptylphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(4-hydroxy-3-methoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(4-hydroxy-3-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-naphthalen-1-yl-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(1-phenylethyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(2,5-dimethylphenyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(3,4-dimethylphenyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-deoxy-2-[[(4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-N-(3-hydroxynaphthalen-1-yl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-[[(4-chlorophenyl)carbonyl]amino]-2-deoxypentofuranosyl)-N-(3-hydroxynaphthalen-1-yl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-[[(4-chlorophenyl)carbonyl]amino]-2-deoxypentofuranosyl)-N-(naphthalen-1-ylmethyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-(2-[[(4-chlorophenyl)carbonyl]amino]-2-deoxypentofuranosyl)-N-naphthalen-1-yl-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-[2-(benzylamino)ethyl]-8-thiophen-2-yl-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-[2-([[2,4-bis(acetyloxy)phenyl]carbonyl]amino)-2-deoxypentofuranosyl]-N-naphthalen-1-yl-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-[2-([[3,4-bis(acetyloxy)phenyl]carbonyl]amino)-2-deoxypentofuranosyl]-N-naphthalen-1-yl-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-[2-([[3-(acetyloxy)phenyl]carbonyl]amino)-2-deoxypentofuranosyl]-N-(naphthalen-1-ylmethyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-[2-([[3-(acetyloxy)phenyl]carbonyl]amino)-2-deoxypentofuranosyl]-N-naphthalen-1-yl-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-[2-([[4-(acetyloxy)-3-methoxyphenyl]carbonyl]amino)-2-deoxypentofuranosyl]-N-(naphthalen-1-ylmethyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-[2-deoxy-2-([[4-(dimethylamino)phenyl]carbonyl]amino)pentofuranosyl]-N-naphthalen-1-yl-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
9-[2-deoxy-2-[(phenylcarbonyl)amino]pentofuranosyl]-8-thiophen-2-yl-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
acetylleucine chloromethyl ketoneHomo sapiens-binds to GAPDH to modulate the conformation of the enzyme, the modified enzyme is susceptible to chymotrypsin-like protease activity, cleavage at TRp195-Arg196; irreversible inhibition, enzyme modified by acetylleucine chloromethyl ketone is deduced to be digested at the peptide bond Trp196-Arg196654926 2D-image
ADPApis mellifera--287971 2D-image
ADPEscherichia coli-inhibition of esterase activity with p-nitrophenyl acetate287977 2D-image
ADPHomo sapiens, Rattus norvegicus-moderately inhibits arsenate reductase activity657393 2D-image
ADP-ribosePanulirus versicolorP56649coenzyme analogue with a non-cooperative behaviour of binding, is a potent competitive inhibitor654051 2D-image
Agaricic acidOryctolagus cuniculus-0.14 mM, 50% inhibition in absence of NAD+. 2 mM, 35% loss of activity in presence of 0.017 mM NAD+287900 2D-image
Agaricic acidTrypanosoma brucei-glyoxysomal enzyme: 0.2 mM, 60% loss of activity. Cytosolic enzyme: 2 mM, less than 20% loss of activity287900 2D-image
alpha-chlorohydrinRattus norvegicusQ9ESV6the contraceptive activity of alpha-chlorohydrin and its apparent specificity for the sperm isoform in vivo are likely to be due to differences in metabolism to 3-chlorolactaldehyde in spermatozoa and somatic cells698925 2D-image
AMPPseudomonas aeruginosa--287919 2D-image
AMPGlycine max--287920 2D-image
AMPApis mellifera--287971 2D-image
AMPEscherichia coli-inhibition of esterase activity with p-nitrophenyl acetate287977 2D-image
AMPDissostichus mawsoni-18 mM, only 5% loss of activity287978 2D-image
anti-TLAb serumSaccharomyces cerevisiae--287899-
ATPPseudomonas aeruginosa--287919 2D-image
ATPHomo sapiens-noncompetitive inhibitor287945 2D-image
ATPSus scrofa-at 0°C, loss of activity. Some of the lost activity is regained upon warming to room temperature287966 2D-image
ATPApis mellifera--287971 2D-image
ATPEuglena gracilis-10 mM, 50% inhibition287973 2D-image
ATPEscherichia coli-inhibition of esterase activity with p-nitrophenyl acetate287977 2D-image
ATPDissostichus mawsoni-1 mM, 25% loss of activity287978 2D-image
ATPHomo sapiens, Rattus norvegicus-moderately inhibits arsenate reductase activity657393 2D-image
ATPHomo sapiens-inhibition is less pronounced for enzyme from sarcoma tissue as compared to normal muscle tissue696174 2D-image
beta-mercaptoethanolNeisseria meningitidis-strong inhibition at 10 mM688953 2D-image
cAMPEuglena gracilis--287973 2D-image
Cd2+Camelus dromedarius-strong inhibition684127 2D-image
CdCl2Thermus thermophilus--287938, 287968 2D-image
CdCl2Pleurodeles waltlQ8AXB520 mM, about 30% inhibition. 10 mM, 70% inhibition655270 2D-image
CdCl2Xenopus laevis-20 mM, about 65% inhibition655270 2D-image
CGP-3466Homo sapiens-deprenyl-related compound that inhibits the pro-apoptotic activity of GAPDH671070 2D-image
chalepinEntamoeba histolyticaQ27646-686053 2D-image
chalepinEntamoeba histolytica-natural inhibitor of GAPDH687842 2D-image
Cu2+Haloarcula vallismortis-1 mM CuCl2, complete inhibition287907 2D-image
Cu2+Thermus thermophilus--287938, 287968 2D-image
Cu2+Bacillus cereus--287974 2D-image
Cu2+Camelus dromedarius--684127 2D-image
CuCl2Arabidopsis thaliana-1 mM673587 2D-image
CuSO4Pleurodeles waltlQ8AXB50.001 mM, 90% inhibition within 2 min655270 2D-image
CuSO4Xenopus laevis-0.001 mM, 70% inhibition in 2 min655270 2D-image
D-Glyceraldehyde 3-phosphatePisum sativum-substrate inhibition287936 2D-image
D-Glyceraldehyde 3-phosphateHomo sapiens-substrate inhibition287945 2D-image
D-Glyceraldehyde 3-phosphateDissostichus mawsoni-substrate inhibition287978 2D-image
demethylasterriquinone B1Homo sapiens-binding of demethylasterriquinone B1 toGAPDH could disrupt phosphatase acting upon phosphatidylinositol lipids and thereby potentiate insulin signaling via the phosphatidylinositol-3-kinase pathway688250 2D-image
DiamideArabidopsis thaliana-1 mM673587 2D-image
diepoxybutaneHomo sapiens-incubation of GAPDH with bis-electrophiles results in inhibition of its catalytic activity, but only at high concentrations of diepoxybutane686080 2D-image
dithiothreitolArabidopsis thaliana-DTT663144 2D-image
dithiothreitolNeisseria meningitidis-strong inhibition at 2 mM688953 2D-image
Fe2+Oryctolagus cuniculus-in the absence of quercetin, GAPDH can be oxidized by ferrous ions due to the formation of reactive oxygen species according to the following series of reactions686849 2D-image
ferriprotoporphorin IXPlasmodium falciparumQ8IKK7-677046 2D-image
ferriprotoporphyrin IXPlasmodium falciparum--671063 2D-image
ferriprotoporphyrin IXHomo sapiens-enzyme is partially inactivated through oxidation of critical thiols673629 2D-image
FK506-binding protein 36Homo sapiens-i.e. FKBP36. The interaction between FKBP36 and GAPDH directly inhibits the catalytic activity of GAPDH. FKBP36 expression causes a significant reduction of the GAPDH level and activity in COS-7 cells. GAPDH is depleted by FKBP36 expression, particularly in the cytosolic fraction698989-
FK506-binding protein 36Oryctolagus cuniculus-i.e. FKBP36, forms complexes with glyceraldehyde-3-phosphate dehydrogenase and Hsp90. Both proteins bind independently to different sites of the FKBP36 tetratricopeptide repeat domain. The interaction between FKBP36 and GAPDH directly inhibits the catalytic activity of GAPDH698989-
fumarateOryctolagus cuniculus-approximately 20% of GAPDH activity is lost by incubation with 0.5 mM fumarate for 24 h, and 100% activity is lost in incubations with 500 mM fumarate at 24 h, NADH in the presence or absence of D-glyceraldehyde 3-phosphate significantly accelerates the inactivation of GAPDH by fumarate686305 2D-image
fumarateRattus norvegicus-inactivation of GAPDH by fumarate in vitro correlates with formation of S-(2-succinyl)cysteine, in diabetic compared with control rats fumarate and S-(2-succinyl)cysteine concentration increase approximately 5fold, accompanied by an about 25% decrease in GAPDH specific activity686305 2D-image
glutathioneArabidopsis thaliana-5 mM oxidized glutathione, GSSG, formation of mixed disulfide between glutathione and A4-GAPDH results in the inhibition of enzyme activity673587 2D-image
glutathioneSpinacia oleracea-formation of mixed disulfide between glutathione and GAPDH results in the inhibition of enzyme activity673587 2D-image
glutathioneArabidopsis thalianaP25858, Q56WJ4inactivation with 10 mM glutathione is reversible upon addition of 20 mM dithiothreitol689409 2D-image
glutathioneOryctolagus cuniculus, Saccharomyces cerevisiae, Spinacia oleracea-inactivation with 10 mM glutathione is reversible upon addition of 20 mM dithiothreitol689409 2D-image
gossypolTrypanosoma brucei--287900 2D-image
guajaverinTrypanosoma cruziP22513molecular docking studies. Guajaverin is stabilized by five hydrogen bonds with the amino acids Ser165, Thr226, Arg249, Ser134, and Glu336696747 2D-image
H2O2Arabidopsis thaliana--663144 2D-image
H2O2Oryctolagus cuniculus--672402, 687602 2D-image
H2O2Arabidopsis thaliana-1 mM673587 2D-image
H2O2Spinacia oleracea--673587 2D-image
H2O2Homo sapiens--673629, 687602, 688661 2D-image
H2O2Oryctolagus cuniculus-GAPDH is oxidized by H2O2 which is likely formed due to the spontaneous dismutation of the superoxide anion that is formed during the autooxidation of quercetin that can result in the oxidation of SH-groups of GAPDH686849 2D-image
Hg2+Camelus dromedarius-strong inhibition684127 2D-image
HgCl2Haloarcula vallismortis-1 mM, complete inhibition287907 2D-image
HgCl2Thermus thermophilus--287938, 287968 2D-image
hydrogen peroxideTetrahymena pyriformis-maximum inhibition is observed at concentrations of 0.2 mM688066 2D-image
iodoacetamideHaloarcula vallismortis-5 mM, complete inhibition287907 2D-image
iodoacetamideThermus thermophilus--287938 2D-image
iodoacetamideThermus thermophilus-0.5 mM, 9% inhibition287968 2D-image
iodoacetamideHomo sapiens--686080 2D-image
iodoacetateThermus thermophilus--287938 2D-image
iodoacetateHomo sapiens--287950 2D-image
iodoacetateThermus thermophilus-0.2 mM, 67% inhibition287968 2D-image
iodoacetateApis mellifera--287971 2D-image
iodoacetateEuglena gracilis--287973 2D-image
iodoacetateBacillus cereus--287974 2D-image
iodoacetateEscherichia coli--287977 2D-image
iodoacetateLactococcus lactis--712937 2D-image
K+Vigna radiata var. radiata-0.2-1.0 M287949 2D-image
K+Camelus dromedarius--684127 2D-image
Koningic acidHypocrea koningii-irreversible inhibition, GAPDH I : 50% inhibition by 1 mM, no effect at 0.1 mM. GAPDH II: 50% inhibition by 0.01 mM. Under conditions of koningic acid production the koningic-acid-resistant isoenzyme GAPDH I is produced. In peptone-rich medium where non koningic acid is produced the koningic-acid-sensitive isoenzyme GAPDH II is produced in addition to GAPDH 1287908 2D-image
Koningic acidHomo sapiens, Rattus norvegicus-inhibits arsenate reductase activity and activity with D-glyceraldehyde 3-phosphate, phosphate and NAD+657393 2D-image
mangiferinTrypanosoma cruziP22513-696747 2D-image
Mn2+Camelus dromedarius--684127 2D-image
N-(1,2,3,4-tetrahydronaphthalen-1-yl)adenosineLeishmania mexicanaQ27890-687934 2D-image
N-(2-[[2-(hydroxymethyl)phenyl]sulfanyl]phenyl)adenosineLeishmania mexicanaQ27890-687934 2D-image
N-(3-acetylnaphthalen-1-yl)-9-(2-deoxy-2-[[(2,4-dichlorophenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
N-(3-acetylnaphthalen-1-yl)-9-(2-deoxy-2-[[(4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
N-(4-acetylnaphthalen-1-yl)-9-(2-deoxy-2-[[(4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
N-(4-acetylnaphthalen-1-yl)-9-[2-deoxy-2-([[4-(methylamino)phenyl]carbonyl]amino)pentofuranosyl]-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
N-(diphenylmethyl)adenosineLeishmania mexicanaQ27890-687934 2D-image
N-(naphthalen-2-ylmethyl)-9-pentofuranosyl-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
N-acetylcysteineHomo sapiens-5 mM N-acetylcysteine significantly reduces G3PD activation induced by both H2O2 and ferric protoporphyrin IX685025 2D-image
N-benzyl-9-(2-deoxy-2-[[(4-methoxyphenyl)carbonyl]amino]pentofuranosyl)-9H-purin-6-amineLeishmania mexicanaQ27890-687934 2D-image
N-cycloheptyladenosineLeishmania mexicanaQ27890-687934 2D-image
N-ethylmaleimideOryctolagus cuniculus-1 mM completely inactivates the enzyme in 10 min686305 2D-image
N-[2-(6-amino-8-bromo-9H-purin-9-yl)-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-3-yl]benzamideLeishmania mexicanaQ27890-687934 2D-image
N-[2-(6-amino-9H-purin-9-yl)-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-3-yl]-1H-benzimidazole-5-carboxamideLeishmania mexicanaQ27890-687934 2D-image
N-[2-(6-amino-9H-purin-9-yl)-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-3-yl]-3,4,5-trihydroxybenzamideLeishmania mexicanaQ27890-687934 2D-image
N-[2-(6-amino-9H-purin-9-yl)-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-3-yl]benzamideLeishmania mexicanaQ27890-687934 2D-image
N-[2-(6-amino-9H-purin-9-yl)-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-3-yl]thiophene-2-carboxamideLeishmania mexicanaQ27890-687934 2D-image
N-[2-(6-amino-9H-purin-9-yl)cyclopentyl]-3-bromobenzamideLeishmania mexicanaQ27890-687934 2D-image
N-[2-(6-amino-9H-purin-9-yl)ethyl]-4-methylbenzamideLeishmania mexicanaQ27890-687934 2D-image
Na+Vigna radiata var. radiata-120 mM almost complete inhibition. Cys, GSH and deproteinated crude extract protect against inhibition287949 2D-image
Na2S4O6Thermus thermophilus--287938-
Na2S4O6Thermus thermophilus-0.1 mM, complete inhibition287968-
Na2S4O6Bacillus cereus--287974-
NAD+Geobacillus stearothermophilus-competitive against NADH287909 2D-image
NAD+Homo sapiens-competitive against NADH287932 2D-image
NAD+Pisum sativum-substrate inhibition287936 2D-image
NAD+Sus scrofa--287966 2D-image
NADHPseudomonas aeruginosa--287919 2D-image
NADHGlycine max-competitive with respect to NAD+ and phosphate287920 2D-image
NADHHomo sapiens-competitive against NAD+287932 2D-image
NADHPisum sativum-competitive with NAD+ and with D-glyceraldehyde 3-phosphate287936 2D-image
NADHHomo sapiens--287945 2D-image
NADHGeobacillus stearothermophilus--287970 2D-image
NADHHomo sapiens, Rattus norvegicus-strongly inhibits arsenate reductase activity657393 2D-image
NADHLactococcus lactis-competitive712937 2D-image
NADP+Neisseria meningitidis-75% inhibition in the presence of 2 mM NADP+688953 2D-image
NADPHNeisseria meningitidis--688953 2D-image
NEMApis mellifera--287971 2D-image
NEMEuglena gracilis-1 mM, complete inhibition287973 2D-image
NEMBacillus cereus--287974 2D-image
NiCl2Thermus thermophilus--287968 2D-image
nitrogen oxideTetrahymena pyriformis--688066 2D-image
NOMus musculus-inactivation by induction of a covalent binding of NAD+ to the enzyme287982 2D-image
NOTetrahymena pyriformis-diminishes GAPDH specific activity by 10%-20%688066 2D-image
NO3-Homo sapiens-uncompetitive inhibitor with NAD+, dead end inhibitor287945 2D-image
oxidized glutathioneArabidopsis thalianaP25858, Q56WJ4inactivation, at least partially reversible upon addition of dithiothreitol. Both residues C155 and C159 are found glutathionylated; inactivation, at least partially reversible upon addition of dithiothreitol. Both residues C155 and C159 are found glutathionylated689409 2D-image
oxidized glutathioneOryctolagus cuniculus, Spinacia oleracea-inactivation, at least partially reversible upon addition of dithiothreitol689409 2D-image
p-hydroxymercuribenzoateGeobacillus stearothermophilus--287970 2D-image
PCMBHaloarcula vallismortis-5 mM, complete inhibition287907 2D-image
PCMBEuglena gracilis-1 mM, complete inhibition, partially reversed by dithiothreitol; 1 mM, inhibition is partially reversed by dithiothreitol287973 2D-image
PCMBBos taurus--287979 2D-image
PentalenolactoneOryctolagus cuniculus-irreversible287900, 288344 2D-image
PentalenolactoneGeobacillus stearothermophilus-reversible287900 2D-image
PentalenolactoneTrypanosoma brucei-most potent inhibitor; reversible287900 2D-image
PentalenolactoneHaloarcula vallismortis-insensitive to287907 2D-image
PentalenolactoneStreptomyces arenae-pentalenolactone-sensitive enzyme is strongly inhibited, pentalenolactone-insensitive enzyme is not inhibited287930 2D-image
PentalenolactoneSaccharomyces cerevisiae--288344 2D-image
PentalenolactoneSpinacia oleracea-irreversible288344 2D-image
phosphatePisum sativum-substrate inhibition287936 2D-image
pyridoxal 5'-phosphateMus musculus-inactivation with pseudo-first-order kinetics287957 2D-image
pyridoxal 5'-phosphateOryctolagus cuniculus--287957 2D-image
quercetinTrypanosoma cruziP22513molecular docking studies. Quercetin is stabilized by two hydrogen bonds with the amino acids Ala198 and Pro253696747 2D-image
S-(2-succinyl)cysteineRattus norvegicus-chemical modification by S-(2-succinyl)cysteine causes irreversible inactivation of glyceraldehyde-3-phosphate dehydrogenase in vitro. In diabetic rats, succination of GAPDH is increased in muscle, and the extent of succination correlates strongly with the decrease in specific activity of the enzyme695595 2D-image
S-nitrosoglutathioneArabidopsis thalianaP25858, Q56WJ4inactivation, at least partially reversible upon addition of dithiothreitol. Both residues C155 and C159 are found nitrosylated; inactivation, at least partially reversible upon addition of dithiothreitol. Both residues C155 and C159 are found nitrosylated; inactivation with 0.5 mM S-nitrosoglutathione is reversible upon addition of 20 mM dithiothreitol689409 2D-image
S-nitrosoglutathioneOryctolagus cuniculus-inactivation, at least partially reversible upon addition of dithiothreitol; inactivation with 0.5 mM S-nitrosoglutathione is reversible upon addition of 20 mM dithiothreitol689409 2D-image
S-nitrosoglutathioneSaccharomyces cerevisiae-inactivation with 0.5 mM S-nitrosoglutathione is reversible upon addition of 20 mM dithiothreitol689409 2D-image
S-nitrosoglutathioneSpinacia oleracea-inactivation, at least partially reversible upon addition of dithiothreitol; inactivation with 0.5 mM S-nitrosoglutathione is reversible upon addition of 20 mM dithiothreitol689409 2D-image
sodium nitroprussideOryctolagus cuniculus-inhibition in presence of NAD+ is due primarily to active-site nitrosylation, covalent binding of NAD+ through a NO-dependent thiol intermediate287981 2D-image
sodium nitroprussideMus musculus-the NO-generating compound inactivates by induction of a covalent binding of NAD+ to the enzyme287982 2D-image
sodium nitroprussideTetrahymena pyriformis-maximum inhibition is observed at concentrations of 0.2 mM688066 2D-image
Sodium tetrathionateThermus thermophilus--287938 2D-image
Sodium tetrathionateBacillus cereus--287974 2D-image
suraminTrypanosoma brucei-cyosolic enzyme: competitive with NAD+. Effect on Km-value and maximal veocity of glyoxysomal enzyme287900 2D-image
tilirosideTrypanosoma cruziP22513molecular docking studies. Tiliroside is stabilized by four hydrogen bonds with the amino acids Cys166, Ser134, and Ser110696747 2D-image
Trinitrobenzenesulfonic acidMus musculus-inactivation with pseudo-first-order kinetics. D-glyceraldehyde-3-phosphate, NAD+, NADH and 3-phospho-D-glyceroyl phosphate almost completely protect from inactivation287957 2D-image
Trinitrobenzenesulfonic acidOryctolagus cuniculus--287957 2D-image
Zn2+Camelus dromedarius--684127 2D-image
ZnSO4Pleurodeles waltlQ8AXB520 mM, 70% inhibition655270 2D-image
ZnSO4Xenopus laevis-20 mM, 50% inhibition655270 2D-image
monoclonal antibody 8B7Oryctolagus cuniculus-antibody is specific for glyceraldehyde 3-phosphate dehydrogenase. In lysates of Sf21 cells, the antibody inhibits protein translation, possibly due to inhibition of the binding of glyceraldehyde 3-phosphate dehydrogenase to mRNA and tRNA695902-
additional informationGeobacillus stearothermophilus-the produced type I antibody induces a time-dependent decrease in the activity by 80-90% of the active holoenzyme and 25% of the apoenzyme672306-
additional informationHomo sapiens-inhibited by binding to the cell membrane673629-
additional informationLactococcus lactis ssp. cremoris-the NADH/NAD+ ratio is shown to modulate the in vivo activity; the wild type GADPH is strongly inhibited in vitro by decreased pH values674222-
additional informationHomo sapiens-stauroporine does not inhibit stimulation of G3PD activity685025-
additional informationMus musculus, Oryctolagus cuniculus, Rattus norvegicus-not inhibited by thiorphan and lipopolysaccharide685334-
additional informationHomo sapiens-not inhibited by DMSO, dibromomethane and 1,2-dibromoethane686080-
additional informationOryctolagus cuniculus-succinate has no effect on enzyme activity686305-
additional informationTetrahymena pyriformis-H2O2 does not significantly alter GAPDH-specific activity levels in cell free extracts688066-
additional informationNeisseria meningitidis-NADH, glucose-1-phosphate, AMP, ADP, ATP, and fructose-6-phosphate do not affect kinetic properties of GAPN and no change in cofactor preference from NAD+ to NADP+ in the presence of these metabolic intermediates is detected688953-
additional informationHomo sapiens-anti-GAPDH immunoglobulin G in the cerebrospinal fluid of patients with multiple sclerosis inhibits GAPDH glycolytic activity (38% or 58% inhibition after incubation of GAPDH with 0.002 or 0.004 mg, respectively)712640-
additional informationLactococcus lactis-no inhibition by D-glucose 6-phosphate, D-fructose 6-phosphate, D-fructose 1,6-bisphosphate, dihydroxyacetone phosphate, phosphoenolpyruvate, pyruvate712937-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
2,3-DimercaptopropanolBos taurus-poor activation287979 2D-image
2-mercaptoethanolHaloarcula vallismortis-maximal activation at 5 mM, dependent on sulfhydryl compound287907 2D-image
2-mercaptoethanolBos taurus-10 mM, 2fold activation of the oxidation of D-glyceraldehyde 3-phosphate287979 2D-image
acetoneThermus thermophilus-activates287938 2D-image
CysBos taurus-10 mM, 2.8fold activation of the oxidation of D-glyceraldehyde 3-phosphate287979 2D-image
dithioerythritolBos taurus-10 mM, 2fold activation of the oxidation of D-glyceraldehyde 3-phosphate287979 2D-image
DMSOTrypanosoma cruzi-activity is increased about 2fold in the presence of 5% DMSO (v/v)684403 2D-image
DoxorubicinHomo sapiens-treatment results in increased nuclear localization of expressed wild-type GAPDH, where it protects telomeres against rapid degradation, concomitant with increased resistance to the growth-inhibitory effects of the drug699592 2D-image
EDTABos taurus-poor activation287979 2D-image
ethanolThermus thermophilus-30% v/v, 5fold activation287938, 287968 2D-image
Ferric protoporphyrin IXHomo sapiens-145% increase of activity at 0.04 mM ferric protoporphyrin IX after 30 min exposure to stauroporin685025 2D-image
gemcitabineHomo sapiens-treatment results in increased nuclear localization of expressed wild-type GAPDH, where it protects telomeres against rapid degradation, concomitant with increased resistance to the growth-inhibitory effects of the drug699592 2D-image
GSHHaloarcula vallismortis-dependent on sulfhydryl compound287907 2D-image
GSHBos taurus-poor activation287979 2D-image
H2O2Homo sapiens-186% increase of activity at 1 mM H2O2685025 2D-image
H2O2Homo sapiens-subapoptotic doses lead to strong hyperactivation, related to mild oxidative stress. U937 cells hyperactivate glyceraldehyde 3-phosphate dehydrogenase with the same timing observed for glyceraldehyde 3-phosphate dehydrogenase alterations from apoptogenic doses of H2O2695602 2D-image
NAD+Entamoeba histolyticaQ27646highest activity in the presence of 0.2 mM NAD+ at 30°C686607 2D-image
NADPHPseudomonas aeruginosa-slight activation287919 2D-image
propan-1-olThermus thermophilus-activates287968 2D-image
propan-2-olThermus thermophilus-activates287968 2D-image
tetrabutylammonium chlorideThermus thermophilus-50% activation287968 2D-image
Triton X-100Homo sapiens--685025 2D-image
methanolTrypanosoma cruzi-activity is increased about 6fold in the presence of 5% methanol (v/v)684403 2D-image
additional informationBacillus cereus-enzyme contains 8 SH groups per tetramer of which 4 are highly reactive and essential for activity287974-
additional informationHomo sapiens-human TATA-binding protein-associated factor II 68-TEC fusion protein-dependent transcription is enhanced by GAPDH684972-
additional informationHomo sapiens-GAPDH functions as a coactivator with high selectivity for androgen receptor and enhances androgen receptor transactivation independent of its glycolytic activity687584-
additional informationHomo sapiens-20% increase of GADPH expression 3 h post concentric exercise697687-

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.01-1,3-Diphosphoglyceric acidHomo sapiens-enzyme form E6.6, pH 7287913 2D-image
0.012-1,3-Diphosphoglyceric acidHomo sapiens-enzyme form E8.5, pH 7287913 2D-image
0.018-1,3-Diphosphoglyceric acidHomo sapiens-enzyme form E9.0, pH 7287913 2D-image
0.158-3-acetyl-NAD+Oryctolagus cuniculus--287978 2D-image
0.62-3-acetyl-NAD+Dissostichus mawsoni--287978 2D-image
1.43-3-acetylpyridine hypoxanthine nucleotideOryctolagus cuniculus--287978 2D-image
8.15-3-acetylpyridine hypoxanthine nucleotideDissostichus mawsoni--287978 2D-image
0.002-3-phospho-D-glyceroyl phosphateHomo sapiens-enzyme form E6.8, pH 7287913 2D-image
0.032-3-phospho-D-glyceroyl phosphateHomo sapiens-enzyme form E9.0, pH 9287913 2D-image
0.034-3-phospho-D-glyceroyl phosphateGeobacillus stearothermophilus--287900 2D-image
0.035-3-phospho-D-glyceroyl phosphateHomo sapiens-enzyme form E8.5, pH 9287913 2D-image
0.042-3-phospho-D-glyceroyl phosphateHomo sapiens-enzyme form E6.6, pH 9287913 2D-image
0.1-3-phospho-D-glyceroyl phosphateTrypanosoma brucei-glyoxysomal enzyme287900 2D-image
0.13-3-phospho-D-glyceroyl phosphateOryctolagus cuniculus--287900 2D-image
0.14-3-phospho-D-glyceroyl phosphateHomo sapiens--287900 2D-image
0.14-3-phospho-D-glyceroyl phosphateTrypanosoma brucei-cytosolic enzyme287900 2D-image
0.172-3-phospho-D-glyceroyl phosphateHomo sapiens-enzyme form E6.8, pH 9287913 2D-image
0.47-3-phospho-D-glyceroyl phosphateEuglena gracilis--287973 2D-image
0.31-acetaldehydeNeisseria meningitidis-recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), at 25°C688953 2D-image
1-arsenateBacillus cereus--287974 2D-image
1.54-arsenateBos taurus-pH 8.9287979 2D-image
1.7-arsenateBos taurus-pH 8.0287979 2D-image
0.2-C6-(4-(2,2,6,6-tetramethyl-piperidinyl-1-oxyl))-NAD+Huso huso--287942-
0.061-C8-(4-(2,2,6,6-tetramethyl-piperidinyl-1-oxyl))-NAD+Huso huso--287942-
0.0102-D-glyceraldehydeTrypanosoma cruzi-in the presence of 5% (v/v) methanol, in TEA-HCl buffer (pH 7.5) at 25°C684403 2D-image
0.0108-D-glyceraldehydeTrypanosoma cruzi-in the presence of 5% (v/v) DMSO, in TEA-HCl buffer (pH 7.5) at 25°C684403 2D-image
0.0393-D-glyceraldehydeTrypanosoma cruzi-in the absence of DMSO and methanol, in TEA-HCl buffer (pH 7.5) at 25°C684403 2D-image
2.9-D-glyceraldehydeBos taurus-pH 8.0287979 2D-image
0.0207-D-Glyceraldehyde 3-phosphateHomo sapiens-pH 8.5, 25°C695298 2D-image
0.053-D-Glyceraldehyde 3-phosphateHaloarcula vallismortis--287907 2D-image
0.07-D-Glyceraldehyde 3-phosphateHomo sapiens--287900 2D-image
0.081-D-Glyceraldehyde 3-phosphateEuglena gracilis--287973 2D-image
0.082-D-Glyceraldehyde 3-phosphateOryctolagus cuniculus--287900 2D-image
0.087-D-Glyceraldehyde 3-phosphateHomo sapiens-pH 7.3, enzyme isolated of sarcoma tissue696174 2D-image
0.089-D-Glyceraldehyde 3-phosphateHomo sapiens-pH 8.0, enzyme isolated of sarcoma tissue696174 2D-image
0.09-D-Glyceraldehyde 3-phosphateGeobacillus stearothermophilus, Oryctolagus cuniculus--287900 2D-image
0.09-D-Glyceraldehyde 3-phosphateOryctolagus cuniculus--287934 2D-image
0.1-D-Glyceraldehyde 3-phosphateStreptomyces arenae-pentalenolactone-insensitive enzyme287930 2D-image
0.11-D-Glyceraldehyde 3-phosphateHomo sapiens-pH 8.8, enzyme isolated of sarcoma tissue696174 2D-image
0.147-D-Glyceraldehyde 3-phosphateTetrahymena pyriformis-in 50 mM Tricine buffer, pH 8.5, 10 mM sodium arsenate, at 35°C688066 2D-image
0.149-D-Glyceraldehyde 3-phosphateHomo sapiens-pH 7.3, enzyme isolated of healthy patients696174 2D-image
0.15-D-Glyceraldehyde 3-phosphateTrypanosoma brucei-glyoxysomal enzyme287900 2D-image
0.159-D-Glyceraldehyde 3-phosphateHomo sapiens-pH 8.0, enzyme isolated of healthy patients696174 2D-image
0.16-D-Glyceraldehyde 3-phosphateHomo sapiens-pH 8.8, enzyme isolated of healthy patients696174 2D-image
0.17-D-Glyceraldehyde 3-phosphateTrypanosoma brucei-cytosolic enzyme287900 2D-image
0.21-D-Glyceraldehyde 3-phosphateCamelus dromedarius-in 50 mM tricine-NaOH buffer (pH 8.5) with 10 mM sodium arsenate, at 25°C684127 2D-image
0.23-D-Glyceraldehyde 3-phosphateDissostichus mawsoni--287978 2D-image
0.24-D-Glyceraldehyde 3-phosphateSus scrofa--287966 2D-image
0.24-D-Glyceraldehyde 3-phosphateBos taurus-pH 8.0287979 2D-image
0.25-D-Glyceraldehyde 3-phosphateStreptomyces arenae-pentalenolactone-sensitive enzyme287930 2D-image
0.29-D-Glyceraldehyde 3-phosphateEscherichia coliP0A9B2mutant N313T/Y317G287927 2D-image
0.3-D-Glyceraldehyde 3-phosphateSus scrofa--287934 2D-image
0.3-D-Glyceraldehyde 3-phosphateThermus thermophilus--287938, 287968 2D-image
0.31-D-Glyceraldehyde 3-phosphateGeobacillus stearothermophilus-mutant enzyme W48F287947 2D-image
0.31-D-Glyceraldehyde 3-phosphateStaphylococcus aureus-wild type enzyme, pH 8.7, 25°C712766 2D-image
0.32-D-Glyceraldehyde 3-phosphateStaphylococcus aureus-mutant enzyme H178N, pH 8.7, 25°C712766 2D-image
0.33-D-Glyceraldehyde 3-phosphateHypocrea koningii-GAPDH II287908 2D-image
0.34-D-Glyceraldehyde 3-phosphateStaphylococcus aureus-mutant enzyme C151S/H178N, pH 8.7, 25°C; mutant enzyme C151S, pH 8.7, 25°C712766 2D-image
0.344-D-Glyceraldehyde 3-phosphatePinus sylvestris--287956 2D-image
0.385-D-Glyceraldehyde 3-phosphateBos taurus-pH 8.9287979 2D-image
0.4-D-Glyceraldehyde 3-phosphateSpinacia oleracea--287961 2D-image
0.42-D-Glyceraldehyde 3-phosphateEscherichia coliP0A9B2mutant N313T287927 2D-image
0.51-D-Glyceraldehyde 3-phosphateBacillus cereus--287974 2D-image
0.54-D-Glyceraldehyde 3-phosphateHypocrea koningii-GAPDH I287908 2D-image
0.55-D-Glyceraldehyde 3-phosphateLactococcus lactis-30°C, pH 7.2712937 2D-image
0.6-D-Glyceraldehyde 3-phosphateSaccharomyces cerevisiae--287937 2D-image
0.762-D-Glyceraldehyde 3-phosphateCryptosporidium parvum--697008 2D-image
0.763-D-Glyceraldehyde 3-phosphateCryptosporidium parvum-wild type enzyme, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, pH 8.8, temperature not specified in the publication711617 2D-image
0.77-D-Glyceraldehyde 3-phosphateHomo sapiensO14556in 50 mM glycine, 50 mM potassium phosphate, 5 mM EDTA, pH 9.0685294 2D-image
0.8-D-Glyceraldehyde 3-phosphateGeobacillus stearothermophilus-wild-type enzyme287947 2D-image
0.8-D-Glyceraldehyde 3-phosphateGeobacillus stearothermophilus-mutant enzyme Y46G287985 2D-image
0.88-D-Glyceraldehyde 3-phosphateEscherichia coliP0A9B2mutant Y317A287927 2D-image
0.89-D-Glyceraldehyde 3-phosphateEscherichia coliP0A9B2wild-type enzyme287927 2D-image
0.9-D-Glyceraldehyde 3-phosphateGeobacillus stearothermophilus-mutant enzyme E276G287985 2D-image
1-D-Glyceraldehyde 3-phosphateGeobacillus stearothermophilus-mutant enzyme D186G and mutant enzyme S48G287985 2D-image
1.1-D-Glyceraldehyde 3-phosphateGeobacillus stearothermophilus-wild-type enzyme287985 2D-image
1.45-D-Glyceraldehyde 3-phosphateNeisseria meningitidis-recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), at 25°C688953 2D-image
2.05-D-Glyceraldehyde 3-phosphateEscherichia coliP0A9B2mutant Y317G287927 2D-image
0.0734-D-Glyceraldehyde-3-phosphateSardina pilchardus-in 50 mM tricine-NaOH buffer (pH 8.5) with 10 mM sodium arsenate, at 25°C684121 2D-image
0.425-D-Glyceraldehyde-3-phosphateTrypanosoma cruzi-free enzyme684427 2D-image
0.5-D-Glyceraldehyde-3-phosphateTrypanosoma cruzi-GAPDH immobilized on an octyl silica column684427 2D-image
0.1-DL-glyceraldehydeHomo sapiens-enzyme form E8.5, pH 7287913 2D-image
0.119-erythrose 4-phosphateHomo sapiens-enzyme form E8.5, pH 7287913 2D-image
0.127-erythrose 4-phosphateHomo sapiens-enzyme form E9.0, pH 7287913 2D-image
0.0102-N6-(2-carboxyethyl)-NAD+Thermus thermophilus--287926 2D-image
0.0674-N6-(2-carboxyethyl)-NAD+Oryctolagus cuniculus--287926 2D-image
0.145-N6-(2-carboxyethyl)-NAD+Geobacillus stearothermophilus--287926 2D-image
3.2e-05-NAD+Cryptosporidium parvum--697008 2D-image
3.2e-05-NAD+Cryptosporidium parvum-wild type enzyme, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, pH 8.8, temperature not specified in the publication711617 2D-image
0.00519-NAD+Thermus thermophilus--287926 2D-image
0.006-NAD+Sus scrofa--287934 2D-image
0.0066-NAD+Euglena gracilis--287973 2D-image
0.01-NAD+Homo sapiens-enzyme form E8.5, pH 9287913 2D-image
0.012-NAD+Sus scrofa--287966 2D-image
0.013-NAD+Oryctolagus cuniculus--287934 2D-image
0.014-NAD+Hypocrea koningii-GAPDH I287908 2D-image
0.0178-NAD+Homo sapiens-pH 8.5, 25°C695298 2D-image
0.018-NAD+Oryctolagus cuniculus--287978 2D-image
0.02-NAD+Homo sapiens-enzyme form E9.0, pH 9287913 2D-image
0.022-NAD+Homo sapiensO14556in 50 mM glycine, 50 mM potassium phosphate, 5 mM EDTA, pH 9.0685294 2D-image
0.025-NAD+Camelus dromedarius-in 50 mM tricine-NaOH buffer (pH 8.5) with 10 mM sodium arsenate, at 25°C684127 2D-image
0.027-NAD+Homo sapiens-enzyme form E6.8, pH 9287913 2D-image
0.031-NAD+Bos taurus-pH 8.9287979 2D-image
0.035-NAD+Homo sapiens-pH 7.3, enzyme isolated of sarcoma tissue696174 2D-image
0.036-NAD+Homo sapiens-pH 8.0, enzyme isolated of sarcoma tissue696174 2D-image
0.0386-NAD+Thermus thermophilus-poly(ethylene glycol)-bound287926 2D-image
0.039-NAD+Geobacillus stearothermophilus--287900 2D-image
0.04-NAD+Trypanosoma brucei-cytosolic enzyme287900 2D-image
0.04-NAD+Geobacillus stearothermophilus-mutant enzyme S48G287985 2D-image
0.04-NAD+Homo sapiens-pH 8.8, enzyme isolated of sarcoma tissue696174 2D-image
0.045-NAD+Escherichia coliP0A9B2wild-type enzyme287927 2D-image
0.046-NAD+Hypocrea koningii-GAPDH II287908 2D-image
0.047-NAD+Homo sapiens-pH 8.8, enzyme isolated of healthy patients696174 2D-image
0.05-NAD+Geobacillus stearothermophilus, Homo sapiens--287900 2D-image
0.05-NAD+Escherichia coliP0A9B2mutant Y317A287927 2D-image
0.05-NAD+Geobacillus stearothermophilus-wild-type enzyme287985 2D-image
0.05-NAD+Geobacillus stearothermophilus-pH 8.0, 25°C, tetrameric enzyme form, wild-type654653 2D-image
0.0507-NAD+Oryctolagus cuniculus--287926 2D-image
0.057-NAD+Neisseria meningitidis-recombinant enzyme, in the presence of D-glyceraldehyde 3-phosphate, in 50 mM Tricine buffer (pH 8.5), at 25°C688953 2D-image
0.058-NAD+Escherichia coliP0A9B2mutant N313T/Y317G287927 2D-image
0.06-NAD+Oryctolagus cuniculus--287900 2D-image
0.06-NAD+Geobacillus stearothermophilus-pH 8.0, 25°C, tetrameric enzyme form, mutant Y283V654653 2D-image
0.062-NAD+Pinus sylvestris--287956 2D-image
0.062-NAD+Homo sapiens-pH 8.0, enzyme isolated of healthy patients696174 2D-image
0.064-NAD+Tetrahymena pyriformis-in 50 mM Tricine buffer, pH 8.5, 10 mM sodium arsenate, at 35°C688066 2D-image
0.07-NAD+Geobacillus stearothermophilus-mutant enzyme E276G287985 2D-image
0.071-NAD+Homo sapiens-pH 7.3, enzyme isolated of healthy patients696174 2D-image
0.076-NAD+Dissostichus mawsoni--287978 2D-image
0.0806-NAD+Geobacillus stearothermophilus--287926 2D-image
0.088-NAD+Neisseria meningitidis-recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), in the presence of glyceraldehyde, at 25°C688953 2D-image
0.092-NAD+Sardina pilchardus-in 50 mM tricine-NaOH buffer (pH 8.5) with 10 mM sodium arsenate, at 25°C684121 2D-image
0.097-NAD+Huso huso--287942 2D-image
0.1-NAD+Saccharomyces cerevisiae--287937 2D-image
0.1-NAD+Thermus thermophilus--287938, 287968 2D-image
0.1-NAD+Bacillus subtilis-wild-type enzyme287980 2D-image
0.1-NAD+Geobacillus stearothermophilus-pH 8.0, 25°C, tetrameric enzyme form, mutant W310F654653 2D-image
0.109-NAD+Neisseria meningitidis-recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), in the presence of acetaldehyde, at 25°C688953 2D-image
0.11-NAD+Streptomyces arenae-pentalenolactone-sensitive enzyme287930 2D-image
0.11-NAD+Geobacillus stearothermophilus-mutant enzyme W84F287947 2D-image
0.12-NAD+Streptomyces arenae-pentalenolactone-insensitive enzyme287930 2D-image
0.143-NAD+Homo sapiens-enzyme form E6.6, pH 9287913 2D-image
0.15-NAD+Geobacillus stearothermophilus-wild-type enzyme287947 2D-image
0.19-NAD+Escherichia coliP0A9B2mutant N313T and Y317G287927 2D-image
0.19-NAD+Bos taurus-pH 8.0287979 2D-image
0.2-NAD+Geobacillus stearothermophilus-pH 8.0, 25°C, tetrameric enzyme form, mutant D282G654653 2D-image
0.2-NAD+Lactococcus lactis-30°C, pH 7.2712937 2D-image
0.23-NAD+Geobacillus stearothermophilus-poly(ethylene glycol)-bound NAD+287926 2D-image
0.25-NAD+Spinacia oleracea--287961 2D-image
0.258-NAD+Trypanosoma cruzi-free enzyme684427 2D-image
0.27-NAD+Bacillus cereus--287974 2D-image
0.29-NAD+Geobacillus stearothermophilus-pH 8.0, 25°C, tetrameric enzyme form, mutant T34Q/T39S/L43Q654653 2D-image
0.33-NAD+Geobacillus stearothermophilus-mutant enzyme S186G287985 2D-image
0.45-NAD+Trypanosoma brucei-glyoxysomal enzyme287900 2D-image
0.5-NAD+Bacillus subtilis-mutant enzyme D32A287980 2D-image
0.674-NAD+Trypanosoma cruzi-GAPDH immobilized on an octyl silica column684427 2D-image
0.75-NAD+Bacillus subtilis-mutant enzyme D32A/L187N287980 2D-image
1-NAD+Bacillus subtilis-mutant enzyme L187N287980 2D-image
2.46-NAD+Geobacillus stearothermophilus-poly(ethylene glycol)-bound NAD+287926 2D-image
2.5-NAD+Geobacillus stearothermophilus-pH 8.0, 25°C, tetrameric enzyme form, mutant N313T654653 2D-image
312-NAD+Staphylococcus aureus-mutant enzyme C151S/H178N, pH 8.7, 25°C712766 2D-image
316-NAD+Staphylococcus aureus-wild type enzyme, pH 8.7, 25°C712766 2D-image
320-NAD+Staphylococcus aureus-mutant enzyme H178N, pH 8.7, 25°C712766 2D-image
322-NAD+Staphylococcus aureus-mutant enzyme C151S, pH 8.7, 25°C712766 2D-image
0.0033-NADHOryctolagus cuniculus--287934 2D-image
0.007-NADHTrypanosoma brucei-cytosolic enzyme287900 2D-image
0.01-NADHHomo sapiens--287900 2D-image
0.012-NADHGeobacillus stearothermophilus, Oryctolagus cuniculus--287900 2D-image
0.02-NADHTrypanosoma brucei-glyoxysomal enzyme287900 2D-image
0.021-NADHEuglena gracilis--287973 2D-image
0.023-NADHSus scrofa--287934, 287966 2D-image
1.7-NADP+Bacillus subtilis-mutant enzyme D32A/L187N287980 2D-image
7.1-NADP+Bacillus subtilis-mutant enzyme D32A and L187N287980 2D-image
0.2-phosphateHypocrea koningii-isoenzyme I and II287908 2D-image
0.53-phosphateEscherichia coliP0A9B2wild-type enzyme287927 2D-image
1.5-phosphateSaccharomyces cerevisiae--287937 2D-image
2.54-phosphateStaphylococcus aureus-wild type enzyme, pH 8.7, 25°C712766 2D-image
3.03-phosphateStaphylococcus aureus-mutant enzyme H178N, pH 8.7, 25°C712766 2D-image
3.09-phosphateStaphylococcus aureus-mutant enzyme C151S, pH 8.7, 25°C712766 2D-image
3.4-phosphateBos taurus-pH 8.9287979 2D-image
3.68-phosphateStaphylococcus aureus-mutant enzyme C151S/H178N, pH 8.7, 25°C712766 2D-image
4-phosphateHomo sapiens-pH 8.8, enzyme isolated of healthy patients696174 2D-image
4.8-phosphateEscherichia coliP0A9B2mutant enzyme Y317A287927 2D-image
6.9-phosphateEscherichia coliP0A9B2mutant enzyme N313T/Y317G287927 2D-image
7-phosphateGeobacillus stearothermophilus-mutant enzyme E276G and mutant enzyme S48G287985 2D-image
7.15-phosphateBos taurus-pH 8.0287979 2D-image
8-phosphateGeobacillus stearothermophilus-mutant enzyme Y46G287985 2D-image
8.3-phosphateGeobacillus stearothermophilus-wild-type enzyme287947 2D-image
9.6-phosphateGeobacillus stearothermophilus-mutant enzyme W84F287947 2D-image
9.9-phosphateHomo sapiens-pH 8.8, enzyme isolated of sarcoma tissue696174 2D-image
18-phosphateGeobacillus stearothermophilus-mutant enzyme D186G287985 2D-image
20-phosphateEscherichia coliP0A9B2mutant enzyme N313T287927 2D-image
35.1-phosphateEscherichia coliP0A9B2mutant enzyme Y317G287927 2D-image
37-phosphateGeobacillus stearothermophilus-wild-type enzyme287985 2D-image
0.0435-Thio-NAD+Oryctolagus cuniculus--287978 2D-image
0.235-Thio-NAD+Dissostichus mawsoni--287978 2D-image
0.2-glyceraldehydeNeisseria meningitidis-recombinant enzyme, at 25°C688953 2D-image
additional information-additional informationGeobacillus stearothermophilus--287909-
additional information-additional informationGlycine max--287920-
additional information-additional informationHomo sapiens--287932, 287950-
additional information-additional informationOryctolagus cuniculus-activity depends non-linearly on protein concentration in the range 0.00003-0.003 mM. With increasing concentrations the apparently hyperbolic substrate saturation curves turn into sigmoidal ones287953-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
4.03-acetaldehydeNeisseria meningitidis-recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), at 25°C688953 2D-image
71.4-D-glyceraldehydeTrypanosoma cruzi-in the absence of DMSO and methanol, in TEA-HCl buffer (pH 7.5) at 25°C684403 2D-image
118-D-glyceraldehydeTrypanosoma cruzi-in the presence of 5% (v/v) DMSO, in TEA-HCl buffer (pH 7.5) at 25°C684403 2D-image
442-D-glyceraldehydeTrypanosoma cruzi-in the presence of 5% (v/v) methanol, in TEA-HCl buffer (pH 7.5) at 25°C684403 2D-image
0.002-D-Glyceraldehyde 3-phosphateStaphylococcus aureus-mutant enzyme C151S/H178N, pH 8.7, 25°C712766 2D-image
0.05-D-Glyceraldehyde 3-phosphateStaphylococcus aureus-mutant enzyme H178N, pH 8.7, 25°C712766 2D-image
0.09-D-Glyceraldehyde 3-phosphateStaphylococcus aureus-mutant enzyme C151S, pH 8.7, 25°C712766 2D-image
16.7-D-Glyceraldehyde 3-phosphateSaccharomyces cerevisiae--287937 2D-image
24.51-D-Glyceraldehyde 3-phosphateNeisseria meningitidis-recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), at 25°C688953 2D-image
46-D-Glyceraldehyde 3-phosphateGeobacillus stearothermophilus-mutant enzyme W84F287947 2D-image
50-D-Glyceraldehyde 3-phosphateSpinacia oleracea--287935 2D-image
70-D-Glyceraldehyde 3-phosphateGeobacillus stearothermophilus--287947 2D-image
70-D-Glyceraldehyde 3-phosphateStaphylococcus aureus-wild type enzyme, pH 8.7, 25°C712766 2D-image
0.1-NAD+Geobacillus stearothermophilus-pH 8.0, 25°C, tetrameric enzyme form, mutant D282G; pH 8.0, 25°C, tetrameric enzyme form, mutant T34Q/T39S/L43Q654653 2D-image
1-NAD+Geobacillus stearothermophilus-pH 8.0, 25°C, tetrameric enzyme form, mutant N313T654653 2D-image
2.5-NAD+Bacillus subtilis-mutant enzyme D32A/L187N287980 2D-image
51-NAD+Geobacillus stearothermophilus-pH 8.0, 25°C, tetrameric enzyme form, mutant W310F654653 2D-image
65-NAD+Geobacillus stearothermophilus-pH 8.0, 25°C, tetrameric enzyme form, wild-type654653 2D-image
70-NAD+Bacillus subtilis-wild-type enzyme and mutant enzyme L187N287980 2D-image
70-NAD+Lactococcus lactis-30°C, pH 7.2712937 2D-image
73-NAD+Geobacillus stearothermophilus-pH 8.0, 25°C, tetrameric enzyme form, mutant Y283V654653 2D-image
112-NAD+Bacillus subtilis-mutant enzyme L187N287980 2D-image
2-NADP+Bacillus subtilis-mutant enzyme D32A287980 2D-image
8-NADP+Bacillus subtilis-mutant enzyme L187N287980 2D-image
17.7-NADP+Bacillus subtilis-mutant enzyme D32A/L187N287980 2D-image
4.35-glyceraldehydeNeisseria meningitidis-recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), at 25°C688953 2D-image
additional information-additional informationEscherichia coliP0A9B2-287927-
additional information-additional informationGeobacillus stearothermophilus--287985-

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.004-2-(dodec-1-en-1-yl)-6-hydroxybenzoic acidTrypanosoma cruzi-pH 8.9, 25°C, substrate D-glyceraldehyde 3-phosphate696735-
0.005-2-(dodec-1-en-1-yl)-6-hydroxybenzoic acidTrypanosoma cruzi-pH 8.9, 25°C, substrate NAD+696735-
0.002-2-pentadecyl-6-hydroxybenzoic acidTrypanosoma cruzi-pH 8.9, 25°C, substrate D-glyceraldehyde 3-phosphate696735-
0.004-2-pentadecyl-6-hydroxybenzoic acidTrypanosoma cruzi-pH 8.9, 25°C, substrate NAD+696735-
0.145-iodoacetateLactococcus lactis-30°C, pH 7.2712937 2D-image
0.02-NADHLactococcus lactis-30°C, pH 7.2, competitive inhibitor, no effect on the maximum velocity712937 2D-image

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.161-(8E)-C15:1-anacardic acidTrypanosoma cruziP22513pH 7.5, 25°C696747 2D-image
0.069-(8E,11E)-C15:2-anacardic acidTrypanosoma cruziP22513pH 7.5, 25°C696747 2D-image
0.038-(8E,11E,14E)-C15:3-anacardic acidTrypanosoma cruziP22513pH 7.5, 25°C696747 2D-image
0.055-2-(dodec-1-en-1-yl)-6-hydroxybenzoic acidTrypanosoma cruzi-pH 8.9, 25°C696735-
0.028-2-pentadecyl-6-hydroxybenzoic acidTrypanosoma cruzi-pH 8.9, 25°C696735-
4.6-Cd2+Camelus dromedarius-at 25°C684127 2D-image
22.7-Cu2+Camelus dromedarius-at 25°C684127 2D-image
0.14-guajaverinTrypanosoma cruziP22513pH 7.5, 25°C696747 2D-image
6.2-Hg2+Camelus dromedarius-at 25°C684127 2D-image
0.075-hydrogen peroxideTetrahymena pyriformis-in 50 mM Tricine buffer, pH 8.5, 10 mM sodium arsenate, at 35°C688066 2D-image
34.6-K+Camelus dromedarius-at 25°C684127 2D-image
0.149-mangiferinTrypanosoma cruziP22513pH 7.5, 25°C696747 2D-image
25.8-Mn2+Camelus dromedarius-at 25°C684127 2D-image
0.142-quercetinTrypanosoma cruziP22513pH 7.5, 25°C696747 2D-image
0.05-sodium nitroprussideTetrahymena pyriformis-in 50 mM Tricine buffer, pH 8.5, 10 mM sodium arsenate, at 35°C688066 2D-image
0.046-tilirosideTrypanosoma cruziP22513pH 7.5, 25°C696747 2D-image
14.2-Zn2+Camelus dromedarius-at 25°C684127 2D-image

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.01-Solanum tuberosumQ8LK04transgenic line 7, source leaves675137
0.025-Solanum tuberosumQ8LK04transgenic line 56, source leaves675137
0.035-Solanum tuberosumQ8LK04wild-type, untransformed control, source leaves675137
0.042-Solanum tuberosumQ8LK04transgenic line 97, source leaves675137
0.1-Solanum tuberosumQ8LK04transgenic line 7, growing tubers; transgenic line 97, growing tubers675137
0.1767-Entamoeba histolyticaQ27646crude extract, at 30 °C686607
0.18-Solanum tuberosumQ8LK04transgenic line 7, sink leaves675137
0.2-Solanum tuberosumQ8LK04transgenic line 56, stolons; transgenic line 7, stolons; transgenic line 97, sink leaves; transgenic line 97, stolons675137
0.25-Solanum tuberosumQ8LK04transgenic line 97, roots675137
0.3-Solanum tuberosumQ8LK04transgenic line 56, growing tubers; transgenic line 7, roots675137
0.35-Solanum tuberosumQ8LK04transgenic line 56, sink leaves675137
0.46-Sardina pilchardus-crude extract684121
0.5-Solanum tuberosumQ8LK04transgenic line 56, roots675137
0.52-Neisseria meningitidis-recombinant enzyme from crude extract, in 50 mM Tricine buffer (pH 8.5), at 25°C688953
0.72-Tetrahymena pyriformis-cell-free extract, in 50 mM Tricine buffer, pH 8.5, 10 mM sodium arsenate, at 25°C688066
0.75-Solanum tuberosumQ8LK04transgenic line 7, stem675137
0.891-Lactococcus lactis ssp. cremoris-strain MG1363, pH 6.6674222
0.9-Solanum tuberosumQ8LK04wild-type, untransformed control, growing tubers675137
1.1-Solanum tuberosumQ8LK04wild-type, untransformed control, roots675137
1.1-Homo sapiens-pH 8.5, 25°C695298
1.2-Solanum tuberosumQ8LK04wild-type, untransformed control, sink leaves675137
1.38-Lactococcus lactis ssp. cremoris-strain MG1363, pH 5.0674222
1.5-Solanum tuberosumQ8LK04transgenic line 56, stem; transgenic line 97, stem675137
1.68-Camelus dromedarius-crude extract, at 25°C684127
1.75-Solanum tuberosumQ8LK04wild-type, untransformed control, stem675137
1.8-Solanum tuberosumQ8LK04wild-type, untransformed control, stolons675137
2.16-Neisseria meningitidis-crude extract, at 25°C688953
3.01-Lactococcus lactis ssp. cremoris-strain MG1363, pH 4.7674222
3.6-Pseudomonas sp.A7LHM723°C, pH 7.5, recombinant His-tagged enzyme698639
3.92-Lactococcus lactis ssp. cremoris-relA acid-resistant mutant, pH 6.6674222
4.313-Lactococcus lactis ssp. cremoris-strain MG1363, pH 4.4674222
4.49-Lactococcus lactis ssp. cremoris-relA acid-resistant mutant, pH 4.7674222
5.4-Thermus thermophilus-crystalline enzyme287938
5.4-Thermus thermophilus--287968
8.6-Homo sapiens-enzyme form E6.6287913
13-Homo sapiens-enzyme form E6.8287913
16-Thermus aquaticus-apoenzyme287946
16.5-Thermus aquaticus-holoenzyme287946
25.1-Neisseria meningitidis-recombinant enzyme after 48.3fold purification, in 50 mM Tricine buffer (pH 8.5), at 25°C688953
26.4-Tetrahymena pyriformis-after 36.7fold purifictaion, in 50 mM Tricine buffer, pH 8.5, 10 mM sodium arsenate, at 25°C688066
26.69-Geobacillus stearothermophilus--287946
30-Arabidopsis thalianaP25858, Q56WJ4purified isozyme GapC1689409
33-Streptomyces arenae-pentalenolactone-insensitive enzyme287930
33-Arabidopsis thalianaP25858, Q56WJ4purified GapC2 C159S mutant isozyme689409
35.75-Sardina pilchardus-after 77.71fold purification684121
41.5-Haloarcula vallismortis--287907
44-Thermotoga maritima--287906
45.1-Camelus dromedarius-after 26.8fold purification, at 25°C684127
50.5-Bos taurus--287979
60-Apis mellifera--287971
60-Arabidopsis thalianaP25858, Q56WJ4purified isozyme GapC2689409
62-Homo sapiensO14556-685294
68.1-Homo sapiens-enzyme from liver287932
75-Sus scrofa-enzyme from liver3246
80-Sus scrofa-enzyme from muscle3246
80.4-Spinacia oleracea--287935
90-Spinacia oleracea-purified enzyme689409
91.4-Bos taurus--287905
94-Oryctolagus cuniculus--670846
97.9-Oryctolagus cuniculus--287969
98-Homo sapiens--287945
100-Oryctolagus cuniculus, Saccharomyces cerevisiae-purified enzyme689409
109-Bacillus coagulans--287963
112-Streptomyces arenae-pentalenolactone-sensitive enzyme287930
125-Hypocrea koningii--287908
145-Glycine max--287902
150-Sus scrofa--287966
150-Geobacillus stearothermophilus-purified enzyme672306
158-Homo sapiens-enzyme form E8.5287913
190-Cavia porcellus--670846
195-Bos taurus-brain287911
211-Bos taurus-muscle287911
219-Bos taurus-heart287911
620-Homo sapiens-enzyme form E9.0287913
additional information-Geobacillus stearothermophilus, Trypanosoma brucei--287900
additional information-Caenorhabditis elegans--287928
additional information-Pisum sativum--287936
additional information-Saccharomyces cerevisiae--287937, 287948
additional information-Mus musculus--287958
additional information-Spinacia oleracea--287961
additional information-Geobacillus stearothermophilus--287970
additional information-Euglena gracilis--287973
additional information-Bacillus cereus--287974

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
7-Homo sapiens-enzyme form E6.8, two pH optima: pH 7.0 and pH 8.5, with activity between pH 7.5 and pH 8.0 being rather low287913
7-Bos taurus-reduction of 3-phospho-D-glyceroyl phosphate, triethanolamine buffer287979
7.27.3Homo sapiens-reaction with 3-phospho-D-glyceroylphosphate287932
7.2-Lactococcus lactis ssp. cremoris-activity assay674222
7.38.8Homo sapiens-enzyme isolated from sarcoma tissue, broad696174
7.48.1Bos taurus-reduction of 1,3-diphosphogycerate, Tris buffer287979
7.4-Cavia porcellus, Oryctolagus cuniculus-activity assay670846
7.5-Solanum tuberosumQ8LK04activity assay675137
7.88.1Bos taurus-oxidation of D-glyceraldehyde 3-phosphate, Tris buffer and triethanolamine buffer287979
7.8-Camelus dromedarius--684127
7.98.9Euglena gracilis--287973
7.9-Arabidopsis thaliana-activity assay673587
88.3Homo sapiens-reaction with D-glyceraldehyde 3-phosphate287932
88.3Homo sapiensO14556-685294
88.5Trypanosoma brucei--287901
89Thermotoga maritima-oxidation of D-glyceraldehyde 3-phosphate, at 40°C287906
89Homo sapiensO14556-685294
8-Escherichia coli-50 mM Tris-chloride buffer and triethanolamine-chloride buffer287977
8-Sardina pilchardus--684121
8.3-Thermus thermophilus--287938, 287968
8.48.8Sus scrofa--287934, 287966
8.59Trypanosoma brucei-cytosolic enzyme and enzyme from glyoxysomes287900
8.59Pisum sativum--287936
8.5-Homo sapiens-enzyme form E6.8, two pH optima: pH 7.0 and pH 8.5, with activity between pH 7.5 and pH 8.0 being rather low287913
8.5-Saccharomyces cerevisiae-phosphorolysis and arsenolysis287937
8.5-Bos taurus-oxidation of D-glyceraldehyde 3-phosphate, glycine buffer287979
8.5-Streptococcus pyogenesP0C0G6the enzymatic activity of cell-associated Plr-SDH-GAPDH complex is measured674559
8.5-Homo sapiens--695298
8.6-Haloarcula vallismortis--287907
8.6-Bacillus coagulans--287963
8.6-Bacillus cereus--287974
8.6-Homo sapiens-enzyme isolated from normal tissue, sharp optimum696174
8.7-Staphylococcus aureus--712766
8.8-Escherichia coli-50 mM sodium diphosphate buffer287977
8.99.1Spinacia oleracea--287935
8.9-Hypocrea koningii-GAPDH I and GAPDH II287908
8.9-Oryctolagus cuniculus-activity assay672402
910Neisseria meningitidis--688953
9.1-Apis mellifera--287971
9.3-Pseudomonas aeruginosa--287919
9.8-Homo sapiens-enzyme form E8.5, D-glyceraldehyde 3-phosphate287913
10-Geobacillus stearothermophilus--287970
10-Geobacillus stearothermophilus-activity assay672306

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
5.59Trypanosoma brucei-pH 5.5: about 50% of maximal activity, pH 9.0: about 55% of maximal activity, cytosolic enzyme287901
610Thermotoga maritima-pH 6.0: about 50% of maximal activity, pH 10.0: about 60% of maximal activity, oxidation of D-glyceraldehyde 3-phosphate, at 40°C287906
78.5Camelus dromedarius--684127
78.8Thermus thermophilus-pH 7.0: about 55% of maximal activity, pH 8.8: about 95% of maximal activity287968
79Trypanosoma brucei-about 40% of maximal activity at pH 7.0 and at pH 9.0, glyoxysomal enzyme287901
79.5Bacillus cereus-pH 7.0: about 70% of maximal activity, pH 9.5: about 55% of maximal activity287974
7.49.6Sus scrofa-about 50% of maximal activity at pH 7.4 and at ph 9.6287934, 287966
7.58.5Escherichia coli-about 85% of maximal activity at pH 7.5 and pH 8.5, 50 mM Tris-chloride buffer. About 75% of maximal activity at pH 7.5 and pH 8.5, 50 mM triethanolamine-chloride buffer287977
7.58.5Sardina pilchardus--684121
8.39.3Escherichia coli-85% of maximal activity at pH 8.3 and pH 9.3, 50 mM sodium diphosphate buffer287977
8.8-Homo sapiens-above, sharp decline in activity for enzyme of patients with chronic myeloid leukemia, no similar sharp decline for enzyme of healthy subjects696174

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
25-Oryctolagus cuniculus-activity assay672402
25-Arabidopsis thaliana-activity assay673587
25-Staphylococcus aureus--712766
2832Camelus dromedarius--684127
30-Euglena gracilis--287973
30-Lactococcus lactis ssp. cremoris-activity assay674222
30-Sardina pilchardus--684121
35-Tetrahymena pyriformis--688066
37-Streptococcus pyogenesP0C0G6the enzymatic activity of cell-associated Plr-SDH-GAPDH complex is measured674559
43-Homo sapiens--695298
64-Neisseria meningitidis--688953

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
2832Sardina pilchardus--684121
45-Oryctolagus cuniculus-100% thermoinactivation of GAPDH in the absence and in the presence of GroEL after 80 and 60 min, respectively, at 45°C672402

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
5.6-Lentinus polychrousD3K1B6calculated from amino acid sequence710790
6.2-Oplegnathus fasciatusB5AAJ5, B5AAJ6calculated698019
6.3-Neisseria meningitidis-isoelectric focusing688953
6.4-Entamoeba histolyticaQ27646isoelectric focusing686607
6.5-Ascaris suumQ95YJ4-656745
6.8-Paracoccidioides brasiliensisQ8X1X3one of two identified isoforms673986
6.9-Pleurodeles waltlQ8AXB5isoelectric focusing655270
77.5Mammalia-GAPDHc, localized in the cytosol675023
7-Paracoccidioides brasiliensisQ8X1X3one of two identified isoforms673986
7.1-Xenopus laevis-isoelectric focusing655270
7.2-Camelus dromedarius-isoelectric focusing684127
7.6-Plasmodium falciparumQ8IKK7calculated677046
7.9-Sardina pilchardus-isoelectric focusing684121
8.4-Oryctolagus cuniculus--670846
8.68.7Mammalia-GAPDHn, localized in the nucleus675023
8.7-Oplegnathus fasciatusB5AAJ5, B5AAJ6calculated698019
8.8-Tetrahymena pyriformis-isoelectric focusing688066
9.1-Dunaliella salinaB1PL92calculated697508

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
A-549 cellHomo sapiens--699592Manually annotated by BRENDA team
bacteroidBradyrhizobium japonicum--287902Manually annotated by BRENDA team
BHK-21 cellMesocricetus auratus-infected with Japanese encephalitis virus699035Manually annotated by BRENDA team
bloodMus musculus--688791Manually annotated by BRENDA team
brainBos taurus--287911Manually annotated by BRENDA team
brainHomo sapiens--287913, 287932Manually annotated by BRENDA team
brainMus musculus--688791Manually annotated by BRENDA team
brainOplegnathus fasciatusB5AAJ5, B5AAJ6strong est expression; weak expression698019Manually annotated by BRENDA team
brain cortexMus musculus, Rattus norvegicus--685334Manually annotated by BRENDA team
C28/I2 cellHomo sapiens-human juvenile costal chondrocyte cell684972Manually annotated by BRENDA team
cerebellumMus musculus, Rattus norvegicus--685334Manually annotated by BRENDA team
cerebral cortexBos taurus--656594Manually annotated by BRENDA team
commercial preparationOryctolagus cuniculus--698989Manually annotated by BRENDA team
coronary artery smooth muscleHomo sapiens--700503Manually annotated by BRENDA team
COS-7 cellHomo sapiens--684972Manually annotated by BRENDA team
Ehrlich ascites carcinoma cellMus musculus--287957Manually annotated by BRENDA team
endothelial cellHomo sapiens-lung, microvascular654850Manually annotated by BRENDA team
epithelial cellHomo sapiens--673706Manually annotated by BRENDA team
erythrocyteHomo sapiens--287900, 287910, 287932, 287945, 287950, 657393, 673629, 685025, 688250, 695298, 712640Manually annotated by BRENDA team
eyeBos taurus-rod outer segment287905Manually annotated by BRENDA team
eyeOplegnathus fasciatusB5AAJ5, B5AAJ6strong expression; weak expression; weak expression698019Manually annotated by BRENDA team
fibroblastHomo sapiens-in both fetal and senior cells, considerable GAPDH is present in intracellular domains characterized by significantly reduced catalysis. Human cells contain significant intracellular levels of enzymatically inactive GAPDH which is age-independent654849Manually annotated by BRENDA team
finOplegnathus fasciatusB5AAJ5, B5AAJ6moderate expression; poor expression698019Manually annotated by BRENDA team
flowerArabidopsis thalianaP25858, Q56WJ4-689409Manually annotated by BRENDA team
fruitbodyLentinus polychrousD3K1B6-710790Manually annotated by BRENDA team
gillOplegnathus fasciatusB5AAJ5, B5AAJ6moderate expression; weak expression698019Manually annotated by BRENDA team
HCT-116 cellHomo sapiens--676259Manually annotated by BRENDA team
heartBos taurus--287911Manually annotated by BRENDA team
heartHomo sapiens--287932Manually annotated by BRENDA team
heartRattus norvegicus--674503Manually annotated by BRENDA team
heartMus musculus--688791Manually annotated by BRENDA team
heartOplegnathus fasciatusB5AAJ5, B5AAJ6moderate expression; moderate expression698019Manually annotated by BRENDA team
HEK-293 cellHomo sapiens-infected with Japanese encephalitis virus699035Manually annotated by BRENDA team
HEK-293 cellHomo sapiens--700503Manually annotated by BRENDA team
HEK-293T cellHomo sapiens--684972Manually annotated by BRENDA team
HeLa cellHomo sapiens--684972, 696824Manually annotated by BRENDA team
hepatocyteRattus norvegicus--688949Manually annotated by BRENDA team
hypodermisAscaris suumQ95YJ4-656745Manually annotated by BRENDA team
intestinal epitheliumAscaris suumQ95YJ4-656745Manually annotated by BRENDA team
intestineOplegnathus fasciatusB5AAJ5, B5AAJ6moderate expression; moderate expression698019Manually annotated by BRENDA team
KB cellHomo sapiens-KB cell line ATCC CCL17673706Manually annotated by BRENDA team
kidneyHomo sapiens--287932Manually annotated by BRENDA team
kidneyMus musculus--287958, 688791Manually annotated by BRENDA team
kidneyOplegnathus fasciatusB5AAJ5, B5AAJ6moderate expression; strong expression698019Manually annotated by BRENDA team
leafSpinacia oleracea--287935, 287961, 689409Manually annotated by BRENDA team
leafArabidopsis thaliana-expression slowly decreases in the dark and is stable in sucrose-treated leaves656414Manually annotated by BRENDA team
leafSolanum tuberosumQ8LK04-675137Manually annotated by BRENDA team
leafArabidopsis thalianaP25858, Q56WJ4-689409Manually annotated by BRENDA team
leukemic monocyte cell lineHomo sapiens--686867Manually annotated by BRENDA team
liverHomo sapiens--287913, 287932, 671066, 685292, 685294, 699592Manually annotated by BRENDA team
liverRattus norvegicus--287913, 656072, 657393Manually annotated by BRENDA team
liverSus scrofa--287934, 287966, 3246Manually annotated by BRENDA team
liverMus musculus--287958, 688791Manually annotated by BRENDA team
liverBos taurus--287979Manually annotated by BRENDA team
liverOplegnathus fasciatusB5AAJ5, B5AAJ6poor expression; predominant expression698019Manually annotated by BRENDA team
lungHomo sapiens--287932Manually annotated by BRENDA team
lungHomo sapiens-microvascular endothelial cell654850Manually annotated by BRENDA team
muscleOryctolagus cuniculus--287900, 287904, 287926, 287933, 287953, 287957, 287959, 287965, 287967, 287969, 287972, 287978, 287981, 288344, 654080, 654437, 670846, 672402, 673706, 685292, 686305, 686481, 686849, 687602, 689409, 696421, 698989Manually annotated by BRENDA team
muscleHomo sapiens--287900, 287967Manually annotated by BRENDA team
muscleBos taurus--287911, 287967Manually annotated by BRENDA team
muscleSus scrofa--287914, 287967, 3246Manually annotated by BRENDA team
muscleCaenorhabditis elegans-isoenzyme 2 is body-wall muscle specific activity located within the actin-containing I and A zones of the nematode‘s sarcomers287928Manually annotated by BRENDA team
muscleRattus norvegicus--287929, 287967, 686305Manually annotated by BRENDA team
muscleHomo sapiens-skeletal muscle287932Manually annotated by BRENDA team
muscleHuso huso--287942Manually annotated by BRENDA team
musclePalinurus vulgaris-tail muscle287951Manually annotated by BRENDA team
muscleMus musculus--287957, 287958Manually annotated by BRENDA team
muscleRattus norvegicus-skeletal muscle287960Manually annotated by BRENDA team
muscleAcipenser sp.--287964, 287967Manually annotated by BRENDA team
muscleCanis lupus familiaris, Felis catus, Gallus gallus, Hippoglossus sp., Lobster, Meleagris gallopavo--287967Manually annotated by BRENDA team
muscleApis mellifera-flight muscle, located at or near the Z-band cross-striations287971Manually annotated by BRENDA team
muscleDissostichus mawsoni-skeletal muscle287978Manually annotated by BRENDA team
muscleOryctolagus cuniculus-of back and hind legs3247Manually annotated by BRENDA team
muscleAscaris suumQ95YJ4-656745Manually annotated by BRENDA team
muscleCavia porcellus--670846Manually annotated by BRENDA team
muscleOplegnathus fasciatusB5AAJ5, B5AAJ6poor expression; predominant expression698019Manually annotated by BRENDA team
myceliumEmericella nidulans--287903Manually annotated by BRENDA team
myceliumLentinus polychrousD3K1B6-710790Manually annotated by BRENDA team
myocyteRattus norvegicus-ventricular myocytes isolated from adult Sprague-Dawley rats674503Manually annotated by BRENDA team
neuroblastoma cellHomo sapiens--687602Manually annotated by BRENDA team
neuronMus musculus-striatal287982Manually annotated by BRENDA team
noduleGlycine max-nitrogen fixing287902Manually annotated by BRENDA team
noduleGlycine max--287920Manually annotated by BRENDA team
NOSE1 cellHomo sapiens-normal human ovarian surface epithelial cell line700133Manually annotated by BRENDA team
ovarian carcinoma cellHomo sapiens--700133Manually annotated by BRENDA team
ovaryAscaris suumQ95YJ4-656745Manually annotated by BRENDA team
placentaHomo sapiens--671070Manually annotated by BRENDA team
seedPisum sativum--287936, 287967Manually annotated by BRENDA team
SH-SY5Y cellHomo sapiens--687602Manually annotated by BRENDA team
siliqueArabidopsis thalianaP25858, Q56WJ4-689409Manually annotated by BRENDA team
skeletal muscleHomo sapiens-for structural comparison671066Manually annotated by BRENDA team
skeletal muscleSardina pilchardus--684121Manually annotated by BRENDA team
skeletal muscleCamelus dromedarius--684127Manually annotated by BRENDA team
skeletal muscleMus musculus--685264Manually annotated by BRENDA team
skeletal muscleOryctolagus cuniculus--685334, 685613, 695902, 713466Manually annotated by BRENDA team
skeletal muscleHomo sapiens--697687Manually annotated by BRENDA team
spermBos taurus, Canis lupus familiaris, Homo sapiens, Mus musculus, Oryctolagus cuniculus--685292Manually annotated by BRENDA team
spermHomo sapiensO14556GAPDS exists in sperms bound to the fibrous sheath of the flagellum685294Manually annotated by BRENDA team
spermRattus norvegicusQ9ESV6-698925Manually annotated by BRENDA team
spleenMus musculus--688791Manually annotated by BRENDA team
spleenOplegnathus fasciatusB5AAJ5, B5AAJ6poor expression; strong expression698019Manually annotated by BRENDA team
stemArabidopsis thalianaP25858, Q56WJ4-689409Manually annotated by BRENDA team
tailMus musculus--688791Manually annotated by BRENDA team
tail musclePanulirus versicolorP56649-654051Manually annotated by BRENDA team
testisRattus norvegicus--676108Manually annotated by BRENDA team
trophozoiteEntamoeba histolyticaQ27646-686607Manually annotated by BRENDA team
tuberSolanum tuberosumQ8LK04-675137Manually annotated by BRENDA team
U-937 cellHomo sapiens--654926, 686867, 695602Manually annotated by BRENDA team
uterusAscaris suumQ95YJ4-656745Manually annotated by BRENDA team
vastus lateralisHomo sapiens--697687Manually annotated by BRENDA team
vegetativeBacillus cereus--287974Manually annotated by BRENDA team
lungMus musculus--688791Manually annotated by BRENDA team
additional informationCaenorhabditis elegans-isoenzyme 1 is present in all cells287928Manually annotated by BRENDA team
additional informationAscaris suumQ95YJ4ubiquitously expressed in all stages of the organism656745Manually annotated by BRENDA team
additional informationRattus norvegicus-COS7L cells are used for transfection674503Manually annotated by BRENDA team
additional informationOplegnathus fasciatusB5AAJ5, B5AAJ6mRNA is detected ubiquitously in all tissues examined; mRNA is detected ubiquitously in all tissues examined698019Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
cell surfaceStreptococcus pneumoniaeQ97NL1-9986655720Manually annotated by BRENDA team
cell surfaceParacoccidioides brasiliensisQ8X1X3-9986673986Manually annotated by BRENDA team
cell surfaceStreptococcus pyogenesP0C0G6in complex with the streptococcal plasmin receptor, Plr, and streptococcal surface dehydrogenase, SDH9986674559Manually annotated by BRENDA team
cell surfaceLactobacillus crispatus-GAPDH attaches to the cell wall at pH 5 but is released to the medium at pH 89986687380Manually annotated by BRENDA team
cell wallKluyveromyces marxianus-associated with the cell wall5618674688Manually annotated by BRENDA team
chloroplastPinus sylvestris-organism contains a cytosolic and a nuclear-encoded, plastid specific enzyme9507287922Manually annotated by BRENDA team
chloroplastMarsilea quadrifoliaO65843-9507287956Manually annotated by BRENDA team
chloroplastPinus sylvestris--9507287956Manually annotated by BRENDA team
chloroplastArabidopsis thaliana, Spinacia oleracea--9507673587, 676334Manually annotated by BRENDA team
chloroplastArabidopsis thalianaQ84WR0, Q9SAJ6; 9507700836Manually annotated by BRENDA team
cytoplasmHomo sapiens--5737654849, 672330, 684972Manually annotated by BRENDA team
cytoplasmStreptococcus pneumoniaeQ97NL1-5737655720Manually annotated by BRENDA team
cytoplasmParacoccidioides brasiliensisQ8X1X3-5737673986Manually annotated by BRENDA team
cytoplasmPlasmodium falciparumQ8IKK7-5737677046Manually annotated by BRENDA team
cytoplasmHomo sapiensO14556; 5737685294Manually annotated by BRENDA team
cytoplasmRattus norvegicus-cytoplasmic expression is elevated in apoptosis and proliferation5737688949Manually annotated by BRENDA team
cytoplasmRattus norvegicusP04797O-GlcNAcylation at residue T227 interrupts the hydrophobic interfaces formed between the enzyme monomers in its terameric state and allows for nucleic translocation of the cytoplasmic enzyme5737696464Manually annotated by BRENDA team
cytoplasmEscherichia coli--5737698374Manually annotated by BRENDA team
cytosolCyanophora paradoxa--582911542Manually annotated by BRENDA team
cytosolTrypanosoma brucei--5829287900, 287901Manually annotated by BRENDA team
cytosolBos taurus--5829287911, 685292Manually annotated by BRENDA team
cytosolPinus sylvestris-organism contains a cytosolic and a nuclear-encoded, plastid specific enzyme5829287922Manually annotated by BRENDA team
cytosolSinapis alba--5829287923Manually annotated by BRENDA team
cytosolMus musculus--5829287982, 685292Manually annotated by BRENDA team
cytosolRattus norvegicus--5829656072, 657393Manually annotated by BRENDA team
cytosolArabidopsis thaliana-isoform GadC-15829656414Manually annotated by BRENDA team
cytosolOryctolagus cuniculus--5829670846, 673706, 685292, 689409Manually annotated by BRENDA team
cytosolCavia porcellus--5829670846Manually annotated by BRENDA team
cytosolHomo sapiens--5829673629, 673706, 676259, 684120, 685025, 685292, 699592Manually annotated by BRENDA team
cytosolMammalia--5829675023Manually annotated by BRENDA team
cytosolSolanum tuberosumQ8LK04-5829675137Manually annotated by BRENDA team
cytosolSardina pilchardus--5829684121Manually annotated by BRENDA team
cytosolCamelus dromedarius--5829684127Manually annotated by BRENDA team
cytosolCanis lupus familiaris--5829685292Manually annotated by BRENDA team
cytosolEntamoeba histolyticaQ27646-5829686607Manually annotated by BRENDA team
cytosolPlasmodium brasilianumB0F3R1-5829687069Manually annotated by BRENDA team
cytosolPlasmodium coatneyiB0F3R2-5829687069Manually annotated by BRENDA team
cytosolPlasmodium cynomolgiB0F3R8-5829687069Manually annotated by BRENDA team
cytosolPlasmodium falciparumB0F3R3-5829687069Manually annotated by BRENDA team
cytosolPlasmodium fragileB0F3R4-5829687069Manually annotated by BRENDA team
cytosolPlasmodium knowlesi strain HB0F3R5-5829687069Manually annotated by BRENDA team
cytosolPlasmodium malariaeB0F3R6-5829687069Manually annotated by BRENDA team
cytosolPlasmodium reichenowiB0F3R7-5829687069Manually annotated by BRENDA team
cytosolPlasmodium vivaxB0F3R9-5829687069Manually annotated by BRENDA team
cytosolHomo sapiens-protein complex containing GAPDH and androgen receptor in the cytosol5829687584Manually annotated by BRENDA team
cytosolArabidopsis thalianaP25858, Q56WJ4; 5829689409Manually annotated by BRENDA team
cytosolSaccharomyces cerevisiae, Spinacia oleracea--5829689409Manually annotated by BRENDA team
cytosolHomo sapiens, Mesocricetus auratus-GAPDH colocalizes with viral RNA-dependentRNA polymerase in cells infected with Japanese encephalitis virus. GAPDH remains relatively constant in the cytosol, while increasing at 12 to 24 hours postinfection and decreasing at 36 hours postinfection in the nuclear fraction of infected cells. There is no direct protein-protein interaction; instead, GAPDH binds to the 3' termini of plus- and minus-strand RNAs of Japanese encephalitis virus. GAPDH binds to the minus-strand more efficiently than to the plus-strand of Japanese encephalitis virus RNAs5829699035Manually annotated by BRENDA team
cytosolArabidopsis thaliana--5829700811Manually annotated by BRENDA team
extracellularStreptococcus pyogenesP0C0G6the Plr-SDH-GAPDH complex is expressed on the bacterial surface and released from cells-674559Manually annotated by BRENDA team
extracellularEscherichia coli-secreted GAPDH is located on the bacterial surface and released to the culture medium of enterohemorrhagic and enteropathogenic strains, secreted GAPDH remains associated with colonic Caco-2 epithelial cells after adhesion and binds human plasminogen and fribinogen, non-pathogenic Escherichia coli strains do not secrete GAPDH-687114Manually annotated by BRENDA team
extracellularLactobacillus crispatus-GAPDH attaches to the cell wall at pH 5 but is released to the medium at pH 8-687380Manually annotated by BRENDA team
extracellularEscherichia coli---698374Manually annotated by BRENDA team
flagellumRattus norvegicus-fibrous sheath of the sperm flagellum19861676108Manually annotated by BRENDA team
glycosomeLeishmania mexicana--20015287986Manually annotated by BRENDA team
glyoxysomeTrypanosoma brucei--9514287900, 287901Manually annotated by BRENDA team
membraneHomo sapiens-isolated from human erytrocyt ghosts16020287945, 287950Manually annotated by BRENDA team
membraneHomo sapiens--16020654849, 672330, 673629, 673706, 676259Manually annotated by BRENDA team
membraneRattus norvegicus-membrane proteins extracted from rat heart16020674503Manually annotated by BRENDA team
membraneMammalia--16020675023Manually annotated by BRENDA team
membraneSchistosoma mansoni-intact ex vivo larvae and 5 day old in vitro grown larvae express glyceraldehyde 3-phosphate dehydrogenase on their surface membrane16020698033Manually annotated by BRENDA team
mitochondrionHomo sapiens-enzyme form E6.8, E8.5 and E9.05739287913Manually annotated by BRENDA team
nucleusHomo sapiens-minor amounts5634654849Manually annotated by BRENDA team
nucleusHomo sapiens--5634672330, 676259, 684972, 685292, 686080, 699592Manually annotated by BRENDA team
nucleusMammalia--5634675023Manually annotated by BRENDA team
nucleusBos taurus, Canis lupus familiaris, Mus musculus, Oryctolagus cuniculus--5634685292Manually annotated by BRENDA team
nucleusHomo sapiens-protein complex containing GAPDH and androgen receptor in the nucleus5634687584Manually annotated by BRENDA team
nucleusRattus norvegicus-nuclear expression of GAPDH increases in apoptosis5634688949Manually annotated by BRENDA team
nucleusArabidopsis thalianaP25858, Q56WJ4; of protoplast, both isoforms GapC1 and GapC2; of protoplast, both isoforms GapC1 and GapC25634689409Manually annotated by BRENDA team
nucleusRattus norvegicusP04797O-GlcNAcylation at residue T227 interrupts the hydrophobic interfaces formed between the enzyme monomers in its terameric state and allows for nucleic translocation of the cytoplasmic enzyme5634696464Manually annotated by BRENDA team
nucleusHomo sapiens, Mesocricetus auratus-GAPDH colocalizes with viral RNA-dependentRNA polymerase in cells infected with Japanese encephalitis virus. GAPDH remains relatively constant in the cytosol, while increasing at 12 to 24 hours postinfection and decreasing at 36 hours postinfection in the nuclear fraction of infected cells. There is no direct protein-protein interaction; instead, GAPDH binds to the 3' termini of plus- and minus-strand RNAs of Japanese encephalitis virus. GAPDH binds to the minus-strand more efficiently than to the plus-strand of Japanese encephalitis virus RNAs5634699035Manually annotated by BRENDA team
plasma membraneBos taurus-the enzyme reversibly interacts with a protease-sensitive plasma membrane-specific protein of rad outer segments5886287905Manually annotated by BRENDA team
plasma membraneHomo sapiens--5886287910Manually annotated by BRENDA team
plasma membraneBos taurus-neuronal5886656594Manually annotated by BRENDA team
plastidArabidopsis thaliana-isoform GadCp-19536656414Manually annotated by BRENDA team
plastidArabidopsis thalianaQ84WR0, Q9SAJ6; 9536700836Manually annotated by BRENDA team
protoplastArabidopsis thalianaP25858, Q56WJ4--689409Manually annotated by BRENDA team
mitochondrionRattus norvegicus--5739287913Manually annotated by BRENDA team
additional informationHomo sapiens-the subcellular localization of enzyme form E6.6 is uncertain-287913Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
3l0d, downloadSCOP (3l0d)CATH (3l0d)Bartonella henselae
3hja, downloadSCOP (3hja)CATH (3hja)Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
1vsu, downloadSCOP (1vsu)CATH (1vsu)Cryptosporidium parvum
1vsv, downloadSCOP (1vsv)CATH (1vsv)Cryptosporidium parvum
3cif, downloadSCOP (3cif)CATH (3cif)Cryptosporidium parvum
1dc3, downloadSCOP (1dc3)CATH (1dc3)Escherichia coli (strain K12)
1dc4, downloadSCOP (1dc4)CATH (1dc4)Escherichia coli (strain K12)
1dc5, downloadSCOP (1dc5)CATH (1dc5)Escherichia coli (strain K12)
1dc6, downloadSCOP (1dc6)CATH (1dc6)Escherichia coli (strain K12)
1gad, downloadSCOP (1gad)CATH (1gad)Escherichia coli (strain K12)
1gae, downloadSCOP (1gae)CATH (1gae)Escherichia coli (strain K12)
1s7c, downloadSCOP (1s7c)CATH (1s7c)Escherichia coli (strain K12)
2vyn, downloadSCOP (2vyn)CATH (2vyn)Escherichia coli (strain K12)
2vyv, downloadSCOP (2vyv)CATH (2vyv)Escherichia coli (strain K12)
1dbv, downloadSCOP (1dbv)CATH (1dbv)Geobacillus stearothermophilus
1gd1, downloadSCOP (1gd1)CATH (1gd1)Geobacillus stearothermophilus
1npt, downloadSCOP (1npt)CATH (1npt)Geobacillus stearothermophilus
1nq5, downloadSCOP (1nq5)CATH (1nq5)Geobacillus stearothermophilus
1nqa, downloadSCOP (1nqa)CATH (1nqa)Geobacillus stearothermophilus
1nqo, downloadSCOP (1nqo)CATH (1nqo)Geobacillus stearothermophilus
2dbv, downloadSCOP (2dbv)CATH (2dbv)Geobacillus stearothermophilus
2gd1, downloadSCOP (2gd1)CATH (2gd1)Geobacillus stearothermophilus
3cmc, downloadSCOP (3cmc)CATH (3cmc)Geobacillus stearothermophilus
3dbv, downloadSCOP (3dbv)CATH (3dbv)Geobacillus stearothermophilus
4dbv, downloadSCOP (4dbv)CATH (4dbv)Geobacillus stearothermophilus
1gpd, downloadSCOP (1gpd)CATH (1gpd)Homarus americanus
4gpd, downloadSCOP (4gpd)CATH (4gpd)Homarus americanus
1u8f, downloadSCOP (1u8f)CATH (1u8f)Homo sapiens
1znq, downloadSCOP (1znq)CATH (1znq)Homo sapiens
2feh, downloadSCOP (2feh)CATH (2feh)Homo sapiens
3gpd, downloadSCOP (3gpd)CATH (3gpd)Homo sapiens
3h9e, downloadSCOP (3h9e)CATH (3h9e)Homo sapiens
3pfw, downloadSCOP (3pfw)CATH (3pfw)Homo sapiens
2i5p, downloadSCOP (2i5p)CATH (2i5p)Kluyveromyces marxianus
1a7k, downloadSCOP (1a7k)CATH (1a7k)Leishmania mexicana
1gyp, downloadSCOP (1gyp)CATH (1gyp)Leishmania mexicana
1gyq, downloadSCOP (1gyq)CATH (1gyq)Leishmania mexicana
1i32, downloadSCOP (1i32)CATH (1i32)Leishmania mexicana
1i33, downloadSCOP (1i33)CATH (1i33)Leishmania mexicana
1cf2, downloadSCOP (1cf2)CATH (1cf2)Methanothermus fervidus
1j0x, downloadSCOP (1j0x)CATH (1j0x)Oryctolagus cuniculus
3e5r, downloadSCOP (3e5r)CATH (3e5r)Oryza sativa subsp. japonica
3e6a, downloadSCOP (3e6a)CATH (3e6a)Oryza sativa subsp. japonica
3v1y, downloadSCOP (3v1y)CATH (3v1y)Oryza sativa subsp. japonica
1crw, downloadSCOP (1crw)CATH (1crw)Panulirus versicolor
1dss, downloadSCOP (1dss)CATH (1dss)Panulirus versicolor
1ihx, downloadSCOP (1ihx)CATH (1ihx)Panulirus versicolor
1ihy, downloadSCOP (1ihy)CATH (1ihy)Panulirus versicolor
1szj, downloadSCOP (1szj)CATH (1szj)Panulirus versicolor
1ywg, downloadSCOP (1ywg)CATH (1ywg)Plasmodium falciparum
2b4r, downloadSCOP (2b4r)CATH (2b4r)Plasmodium falciparum
2b4t, downloadSCOP (2b4t)CATH (2b4t)Plasmodium falciparum
2vyn, downloadSCOP (2vyn)CATH (2vyn)Rattus norvegicus
2vyv, downloadSCOP (2vyv)CATH (2vyv)Rattus norvegicus
3pym, downloadSCOP (3pym)CATH (3pym)Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
3hq4, downloadSCOP (3hq4)CATH (3hq4)Staphylococcus aureus (strain MRSA252)
3k73, downloadSCOP (3k73)CATH (3k73)Staphylococcus aureus (strain MRSA252)
3k9q, downloadSCOP (3k9q)CATH (3k9q)Staphylococcus aureus (strain MRSA252)
3ksd, downloadSCOP (3ksd)CATH (3ksd)Staphylococcus aureus (strain MRSA252)
3ksz, downloadSCOP (3ksz)CATH (3ksz)Staphylococcus aureus (strain MRSA252)
3kv3, downloadSCOP (3kv3)CATH (3kv3)Staphylococcus aureus (strain MRSA252)
3l4s, downloadSCOP (3l4s)CATH (3l4s)Staphylococcus aureus (strain MRSA252)
3l6o, downloadSCOP (3l6o)CATH (3l6o)Staphylococcus aureus (strain MRSA252)
3lc1, downloadSCOP (3lc1)CATH (3lc1)Staphylococcus aureus (strain MRSA252)
3lc2, downloadSCOP (3lc2)CATH (3lc2)Staphylococcus aureus (strain MRSA252)
3lc7, downloadSCOP (3lc7)CATH (3lc7)Staphylococcus aureus (strain MRSA252)
3lvf, downloadSCOP (3lvf)CATH (3lvf)Staphylococcus aureus (strain MRSA252)
1b7g, downloadSCOP (1b7g)CATH (1b7g)Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
1hdg, downloadSCOP (1hdg)CATH (1hdg)Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
1cer, downloadSCOP (1cer)CATH (1cer)Thermus aquaticus
2g82, downloadSCOP (2g82)CATH (2g82)Thermus aquaticus
1vc2, downloadSCOP (1vc2)CATH (1vc2)Thermus thermophilus
3sth, downloadSCOP (3sth)CATH (3sth)Toxoplasma gondii
2x0n, downloadSCOP (2x0n)CATH (2x0n)Trypanosoma brucei brucei
1k3t, downloadSCOP (1k3t)CATH (1k3t)Trypanosoma cruzi
1ml3, downloadSCOP (1ml3)CATH (1ml3)Trypanosoma cruzi
1qxs, downloadSCOP (1qxs)CATH (1qxs)Trypanosoma cruzi
3dmt, downloadSCOP (3dmt)CATH (3dmt)Trypanosoma cruzi
3ids, downloadSCOP (3ids)CATH (3ids)Trypanosoma cruzi

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
36000-Arabidopsis thaliana-monomer, determined by SDS-PAGE663144
36000-Plasmodium falciparum-monomer671063
36000-Oryctolagus cuniculus-monomer, determined by SDS-PAGE672402
36000-Homo sapiens-subunit, SDS-PAGE684120
36000-Escherichia coli-SDS-PAGE687114
36000-Homo sapiens, Oryctolagus cuniculus-SDS-PAGE, native enzyme687602
36000-Tetrahymena pyriformis-subunit, SDS-PAGE688066
36140-Spinacia oleracea-theoretical mass of the A subunit673587
36200-Lentinus polychrousD3K1B6calculated from amino acid sequence710790
36600-Plasmodium falciparumQ8IKK7monomer677046
37000-Homo sapiens--672330
37000-Rattus norvegicus-endogenously expressed in COS7L cells, immunoblot674503
37000-Camelus dromedarius-SDS-PAGE684127
37000-Entamoeba histolyticaQ27646ADP-ribosylated enzyme subunit, SDS-PAGE686607
38000-Homo sapiens-determined by SDS-PAGE and Western Blot analysis676259
39000-Paracoccidioides brasiliensisQ8X1X3determined by SDS-PAGE and Western Blot analysis673986
39360-Spinacia oleracea-theoretical mass of the B subunit673587
40000-Homo sapiens, Oryctolagus cuniculus-SDS-PAGE673706
40000-Lactobacillus plantarum-SDS-PAGE687344
58000-Homo sapiensO14556full length subunit685294
70000-Oryctolagus cuniculus-SDS-PAGE, treatment of GAPDH with (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide at 0.01 mM for 10 min at 37°C results in formation of three bands (66, 68, and 76 kDa) corresponding roughly to a dimer of 70000 Da687602
98000-Homo sapiens-enzyme form E6.6, gel filtration287913
120000-Homo sapiens-enzyme form E8.5, gel filtration287913
120000-Arabidopsis thaliana-tetramer, determined by gel filtration663144
128000-Thermus thermophilus-equilibrium sedimentation287968
130000-Plasmodium falciparum-tetramer, estimated by gel filtration671063
130000-Kluyveromyces marxianus-tetramer, determined by gel filtration674688
131000-Caenorhabditis elegans-gel filtration287928
133000-Homo sapiens-enzyme form E9.0, gel filtration287913
135000-Thermus thermophilus-gel filtration287968
137000-Euglena gracilis-gel filtration287973
138600-Euglena gracilis-sucrose density gradient centrifugation287973
140000150000Trypanosoma brucei-sucrose density gradient centrifugation287901
140000-Apis mellifera-gel filtration287971
140500-Euglena gracilis-equilibrium sedimentation287973
142000-Cyanophora paradoxa-gel filtration11542
142000-Bos taurus-gel filtration287911
142000-Homo sapiens-enzyme form E6.8, gel filtration287913
142000-Homo sapiens-equilibrium sedimentation287932
142000-Dissostichus mawsoni-low speed equilibrium sedimentation287978
142000-Bos taurus-gel filtration287979
142000-Oryctolagus cuniculus--670846
144000-Homo sapiens-gel filtration287950
144000-Oryctolagus cuniculus-tetramer, calculated672402
145000148000Sus scrofa-equilibrium sedimentation, velocity sedimentation287934
145000-Pisum sativum-velocity sedimentation287936
145000-Saccharomyces cerevisiae-gel filtration287937
146000-Camelus dromedarius-non-denaturing PAGE684127
146800-Bacillus coagulans-equilibrium sedimentation287963
147000-Glycine max-gel filtration287902
148000-Thermotoga maritima-equilibrium sedimentation287906
148000-Sus scrofa-equilibrium sedimentation287966
148700-Geobacillus stearothermophilus-equilibrium sedimentation287970
150000-Spinacia oleracea--287961
150000-Zymomonas mobilis-gel filtration3241
150000-Homo sapiensO14556N-terminally truncated enzyme after trypsin-treatment, Blue Native PAGE685294
150000-Mus musculus-SDS-PAGE688791
150000-Homo sapiens-PAGE695298
152000-Hypocrea koningii-gel filtration287908
180000-Streptomyces arenae-gel filtration, pentalenolactone-sensitive enzyme287930
180000-Spinacia oleracea--287935
180000-Saccharomyces cerevisiae-gel filtration287948
190000-Haloarcula vallismortis-gel filtration287907
200000-Neisseria meningitidis-SDS-PAGE688953
208000-Neisseria meningitidis-native PAGE slab gels with varying acrylamide concentrations of 5-10% (w/v) in the absence of SDS688953
209200-Neisseria meningitidis-calculated from amino acid sequence688953
290000-Streptomyces arenae-gel filtration, pentalenolactone-insensitive enzyme287930
315000-Pseudomonas aeruginosa-non-denaturing PAGE287919
additional information-Rattus norvegicus-unusually low His content compared to other mammalian muscle acetaldehyde phosphate dehydrogenases287960
additional information-Spinacia oleracea-Cys content is higher than that found in analogous enzymes287961
additional information-Geobacillus stearothermophilus-the enzyme possesses precise 222 symmetry. Pairs of active sites are linked through a flexible polypeptide loop which probably mediates the structural changes giving rise to cooperative effects. Three additional salt bridges made by each subunit to others would make a major contribution to thermostability of the tetramer287962
additional information-Bacillus cereus-high content of beta-structure, 45%287974
additional information-Apis mellifera, Bombus appositus, Bombus nevadensis, Bombus occidentalis, Psithyrus suckleyi-comparison of structural properties287976

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Saccharomyces cerevisiae-x * 36000, SDS-PAGE287899
?Bos taurus-x * 38000, SDS-PAGE287905
?Zymomonas mobilis-x * 41000, SDS-PAGE287916
?Pinus sylvestris-x * 36000, SDS-PAGE287922
?Drosophila melanogaster-x * 35500 + x * 37000, SDS-PAGE287924
?Mus musculus-x * 37000, SDS-PAGE287958
?Spinacia oleracea-x * 14000 + x * 37000, SDS-PAGE287961
?Escherichia coli-x * 35000, high speed equilibrium sedimentation after treatment with 5 M guanidine hydrochloride containing 0.01 M dithiothreitol287977
?Ascaris suumQ95YJ4x * 40000, SDS-PAGE656745
?Bacillus megateriumP23722x * 35914, calculated from sequence682151
?Staphylococcus aureusQ6GIL8x * 37600, calculated, x * 37500, SDS-PAGE695363
?Antheraea mylitta-x * 37600, calculated and SDS-PAGE695391
?Oryctolagus cuniculus-x * 37000, SDS-PAGE695902
?Dunaliella salinaB1PL92x * 40270, calculated697508
?Oplegnathus fasciatusB5AAJ5, B5AAJ6x * 35960, calculated; x * 35990, calculated698019
?Pseudomonas sp.A7LHM7x * 36100, calculated698639
?Starmerella bombicolaB3FPE3x * 35673, calculated699355
dimerHomo sapiens-1 * 58000 + 1 * 61000, enzyme form E6.6, SDS-PAGE287913
dimerKluyveromyces marxianus-the final crystallographic model consists of a dimer674688
dimerEntamoeba histolytica-x-ray crystallography687842
heteromerArabidopsis thaliana-GAPDH-AnBn heteromer of GapA and GapB subunits676334
heterotetramerSpinacia oleracea-A2B2-GAPDH, light conformation, B subunits are almost identical to A subunits, expect for the presence of a C-terminal extension containing a pair of cysteines, which is the target of TRX regulation673587
homotetramerArabidopsis thaliana--663144
homotetramerPlasmodium falciparum--671063
homotetramerHomo sapiens--671066
homotetramerArabidopsis thaliana-A4-GAPDH673587
homotetramerArabidopsis thaliana, Spinacia oleracea-GAPDH-A4, homotetramer GapA subunits676334
homotetramerSardina pilchardus-4 * 37000, denaturing SDS-PAGE; 4 * 38500, non-denaturing PAGE684121
homotetramerCamelus dromedarius-4 * 36500, non-denaturing PAGE; 4 * 37000, SDS-PAGE684127
homotetramerHomo sapiensO145564 * 40000, N-terminally truncated enzyme after trypsin treatment, SDS-PAGE685294
homotetramerEntamoeba histolyticaQ27646-686053
homotetramerMus musculus-4 * 37000, SDS-PAGE688791
homotetramerNeisseria meningitidis-4 * 50000, SDS-PAGE; 4 * 51000, native PAGE slab gels with varying acrylamide concentrations of 5-10% (w/v) in the absence of SDS688953
homotetramerStaphylococcus aureusQ6GIL8x-ray crystallography710757, 712766
homotetramerCryptosporidium parvum-x-ray crystallography711617
homotetramerOryctolagus cuniculus--713466
multimerSpinacia oleracea-A8B8-GAPDH, dark conformation, B subunits are almost identical to A subunits, expect for the presence of a C-terminal extension containing a pair of cysteines, which is the target of TRX regulation673587
octamerStreptomyces arenae-8 * 43000, pentalenolactone-insensitive enzyme, gel filtration287930
tetramerCyanophora paradoxa-4 * 36000, SDS-PAGE11542
tetramerTrypanosoma brucei-4 * 33500, cytosolic enzyme, SDS-PAGE; 4 * 38000, glyoxysomal enzyme, SDS-PAGE287901
tetramerGlycine max-4 * 37000, SDS-PAGE287902
tetramerThermotoga maritima-4 * 37000, SDS-PAGE287906
tetramerHaloarcula vallismortis-4 * 40000, SDS-PAGE287907
tetramerHypocrea koningii-4 * 38000, GAPDH I and GAPDH II, SDS-PAGE287908
tetramerBos taurus-4 * 35000, SDS-PAGE287911
tetramerHomo sapiens-4 * 29500, enzyme form E8.5, SDS-PAGE; 4 * 33000, enzyme form E9.5, SDS-PAGE; x * 36000 + x * 38000, enzyme form E6.8, SDS-PAGE287913
tetramerCaenorhabditis elegans-4 * 38500, SDS-PAGE287928
tetramerStreptomyces arenae-4 * 43000, pentalenolactone-sensitive enzyme, gel filtration287930
tetramerOryctolagus cuniculus--287934, 287946, 670846, 672402
tetramerSus scrofa-4 * 38000, glyoxysomal enzyme, SDS-PAGE287934
tetramerPisum sativum-4 * 36000-37000, SDS-PAGE287936
tetramerSaccharomyces cerevisiae-4 * 35000, SDS-PAGE287937
tetramerThermus thermophilus-4 * 33500, SDS-PAGE287938
tetramerGeobacillus stearothermophilus-4 * 36000, SDS-PAGE287946, 287970
tetramerThermus aquaticus-4 * 36000, SDS-PAGE287946
tetramerSaccharomyces cerevisiae-4 * 37000, SDS-PAGE287948
tetramerHomo sapiens-4 * 36000, SDS-PAGE287950, 695298
tetramerBacillus coagulans-4 * 36000, SDS-PAGE287963
tetramerSus scrofa-4 * 38000, SDS-PAGE287966
tetramerThermus thermophilus-4 * 33700, SDS-PAGE287968
tetramerEuglena gracilis-4 * 37000, SDS-PAGE287973
tetramerBacillus cereus-4 * 36000, SDS-PAGE287974
tetramerZymomonas mobilis-4 * 40000-42000, SDS-PAGE3241
tetramerPleurodeles waltlQ8AXB54 * 37000, SDS-PAGE655270
tetramerXenopus laevis-4 * 35000, SDS-PAGE655270
tetramerCavia porcellus--670846
tetramerGeobacillus stearothermophilus--672306
tetramerHomo sapiens--673629, 688250
tetramerKluyveromyces marxianus-determined by gel filtration674688
tetramerPlasmodium falciparumQ8IKK7-677046
tetramerOryctolagus cuniculus-sedimentation analysis685613
monomerHomo sapiens, Oryctolagus cuniculus-1 * 36000, SDS-PAGE687602
additional informationSaccharomyces cerevisiae-subunit interactions are involved in regulation of activity287931
additional informationSaccharomyces cerevisiae-immobilized enzyme can exist as a trimer287943
additional informationOryctolagus cuniculus-enzyme exists as an equilibrium mixture of different oligomeric states. Rapid equilibrium between monomer - dimer - tetramer, the tetramer is inactive287953
additional informationGeobacillus stearothermophilus-dimers generated from the tetrameric enzyme are inactive but exhibit cooperativity in NAD+ binding287985
additional informationArabidopsis thalianaP25858, Q56WJ4enzyme can bind top a partial gene sequence of NADP-dependent malated dehydrogenase EC 1.2.1.37; enzyme can bind top a partial gene sequence of NADP-dependent malated dehydrogenase EC 1.2.1.37689409
additional informationHomo sapiens-recombinant glyceraldehyde 3-phosphate dehydrogenase binds to hepatitis B virus regulatory element RNA in vitro and inhibits hepatitis B virus regulatory element function. Overexpression of glyceraldehyde 3-phosphate dehydrogenase depresses the expression of hepatitis B virus antigen695939
additional informationOryctolagus cuniculus-non-native forms of GAPDH obtained by cold denaturation, oxidation of the enzyme, or its unfolding in guanidine hydrochloride efficiently bind to soluble amyloid-beta peptide (1-42) yielding a stable complex. Native tetrameric GAPDH does not interact with soluble amyloid-beta peptide (1-42), neither non-native forms of GAPDH interact with aggregated amyloid-beta peptide (1-42)696421
additional informationStreptococcus oralis-interaction of GAPDH with Porphyromonas gingivalis major fimbrae plays an important role in Porphyromonas gingivalis colonization. Amino acid residues 166 to 183 of Streptococcus oralis GAPDH exhibit the strongest binding activity toward rFimA, and the synthetic peptide corresponding to amino acid residues 166 to 183 of GAPDH, peptide DNFGVVEGLMTTIHAYTG inhibits Streptococcus oralis-Porphyromonas gingivalis biofilm formation in a dose-dependent manner. The peptide inhibits interbacterial biofilm formation by several oral streptococci and Porphyromonas gingivalis strains with different types of FimA698256
additional informationHomo sapiens-recombinant GAPDH binds directly with high affinity to a single-stranded oligonucleotide comprising three telomeric DNA repeats. Nucleotides T1, G5, and G6 of the TTAGGG repeat are essential for binding.The stoichiometry of the interaction is 2:1 DNA:GAPDH, and GAPDH appears to form a high-molecular-weight complex when bound to the oligonucleotide699592

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
glutathionylationArabidopsis thaliana--673587
phosphorylationHomo sapiens--688661
side-chain modificationHomo sapiens-dimethylation, deamidation, and methionine oxidation688661
glycoproteinKluyveromyces marxianus-N-glycosylated674688
ribosylationEntamoeba histolyticaQ27646mono-ADP-ribosylation does not affect GADPH activity686607
additional informationEscherichia coli-GAPDH of enterohemorrhagic and enteropathogenic Escherichia coli-strains is ADP-ribosylated either in the cytoplasm or in the extracellular medium. GAPDH catalyzes its own modification involving residue C149 at the active site, reaction requires NAD+698374
additional informationHomo sapiens-4-hydroxy-2-nonenal-modified GAPDH is degraded by cathepsin G686867
phosphoproteinMammalia-suggested for enzymatic mechanismn which modifiy GAPDHc to GAPDHn675023
additional informationOryctolagus cuniculus-posttranslational modification of the enzyme with NADH is stimulated by thiols, possibly through superoxide, and is independent of NO287965
proteolytic modificationPinus sylvestris-the precursor has a MW of 40000 Da, the processed polypeptide has a MW of 36000 Da287922
additional informationRattus norvegicusP04797O-GlcNAcylation at residue T227 interrupts the hydrophobic interfaces formed between the enzyme monomers in its terameric state and allows for nucleic translocation of the cytoplasmic enzyme696464
phosphoproteinRattus norvegicus-phosphorylated by protein kinase Ciota /lambda656072
additional informationTetrahymena pyriformis-posttranslational modification of the enzyme by nitrogen oxide688066

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
resolution to 2.2 A. space group I222Antheraea mylitta-695391
-Apis mellifera-287971
-Bacillus coagulans-287963
crystalline enzyme does not contain NAD+Bos taurus-287979
GAPDH in the apo and holo (enzyme in complex with NAD+) state, hanging drop vapor diffusion method, using 16-20% (w/v) PEG 3000 and 0.2 M NaCl in 0.1 M HEPES, pH 7.5Cryptosporidium parvum-711617
structure in absence and presence of NAD+ and structure of the ternary enzyme-cofoactor-substrate complex to 2.0 A resolution. The active site can accomodate the substrate in multiple conformations at multiple locations during the initial encounter. the C-3 phosphate group clearly prefers the so-called new phosphate site for initial bindingCryptosporidium parvum-697008
GADPH in complex wit NAD+, computational modellingEntamoeba histolytica-687842
-Escherichia coli-287983
after addition of NAD+ to the apoproteinEscherichia coli-287977
structure determination by formation of soluble recombinant rat sperm glyceraldehyde-3-phosphate dehydrogenase as a heterotetramer with the Escherichia coli glyceraldehyde-3-phosphate dehydrogenase in a ratio of 1:3. Glyceraldehyde 3-phosphate binds in the Ps pocket in the active site of the sperm enzyme subunit in the presence of NADEscherichia coliP0A9B2698925
-Geobacillus stearothermophilus-287909, 287962, 287970
hanging-drop vapor-diffusion method, enzyme in complex with NAD+ and D-glyceraldehyde 3-phosphate. C149A GAPDH and C149S GAPDH ternary complexes are obtained by soaking the crystals of the corresponding binary complexes (enzyme -NAD+) in a solution containing D-glyceraldehyde 3-phosphateGeobacillus stearothermophilus-656119
holoenzyme and apoenzymeGeobacillus stearothermophilus-287946
structure at 1.8 A resolutionGeobacillus stearothermophilus-287917
-Homo sapiens-287932
a high-resolution structure of 1.75 A is reportedHomo sapiens-671070
the structure is presented at 2.5 A resolutionHomo sapiens-671066
diffraction data to 2.3 A resolution are collectedKluyveromyces marxianus-674688
-Leishmania mexicana-287986
-Oryctolagus cuniculus-287969
sitting-drop vapour-diffusion method, crystallized in space group P2(1)2(1)2(1) with a tetramer in the asymmetric unit, crystals solved at 2.4 AOryctolagus cuniculus-654080
-Palinurus vulgaris-287951
enzyme carrying a fluorescent NAD+ derivative at 2.7 A resolutionPanulirus versicolor-287987
structures of D-glyceraldehyde-3-phosphate dehydrogenase complexed with coenzyme analogues ADPribose and thio-NAD+. The crystals of both GAPDH complexes belong to the same space group C2 as holeenzyme or apoenzyme, but with different unit-cell parametersPanulirus versicolorP56649654051
crystals of tag-free protein diffracts X-rays to 2.6 A resolution, of the His-tagged protein to 4.0 APlasmodium falciparum-671063
the crystal structure is solved at 2.25 A resolutionPlasmodium falciparumQ8IKK7677046
structure determination by formation of soluble recombinant rat sperm glyceraldehyde-3-phosphate dehydrogenase as a heterotetramer with the Escherichia coli glyceraldehyde-3-phosphate dehydrogenase in a ratio of 1:3. Refinement to 2.2 A for the holo enzyme, to 2.4 A for the complex with glyceraldehyde 3-phosphate. Glyceraldehyde 3-phosphate binds in the Ps pocket in the active site of the sperm enzyme subunit in the presence of NADRattus norvegicusQ9ESV6698925
-Saccharomyces cerevisiae-287975
hanging drop vapor diffusion method, using 0.1 M Tris-HCl pH 8.2, 28% (w/v) PEG 3350, at 25°CStaphylococcus aureus-710757
to 2.0 A resolution. Space group P21Staphylococcus aureusQ6GIL8695363
wild type holo and apoenzymes and mutant enzymes C151S, C151G and C151S/H178N in complex with NAD+ and D-glyceraldehyde 3-phosphate, hanging drop vapor diffusion method, the wild-type holoenzyme and apoenzyme are crystallized from 0.1 M Tris-HCl, pH 8.5, and 20% (w/v) PEG 4000 at 4°C and from 0.1 M Tris-HCl, pH 8.2, and 32% (w/v) PEG 3350 at 25°C, respectively. Crystals of active-site mutants in complex with NAD+ (C151S, C151G, and C151S/H178N) grow at 25°C from 0.1 M Tris-HCl, pH 8.5, and 28% (w/v) PEG 4000, from 0.1 M Tris-HCl, pH 8.2, and 30% (w/v) PEG 4000, and from 0.1 M Tris-HCl, pH 8.5, and 30% (w/v) PEG 4000, respectively, while mutant H178N in complex with NAD+ crystallizes from 0.1 M Tris-HCl, pH 8.2, and 30% (w/v) PEG 4000 at 4°CStaphylococcus aureus-712766
-Sus scrofa-287934, 287966
-Thermotoga maritima-287906
-Thermus thermophilus-287938, 287968
hanging drop vapour diffusion method, enzyme in complex with the covalently bound GAP analogue, 3-(p-nitrophenoxycarboxyl)-3-ethylene propyl dihydroxyphosphonate, at an improved resolution of 2.0-2.5 ATrypanosoma cruzi-654711

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
4.511Saccharomyces cerevisiae-rapid inactivation below pH 4.5 and above pH 11.0287937
5.6-Lactobacillus crispatus-GAPDH interacts with lipoteichoic acids at acidic pH values but not at pH values higher than 5.6687380
8-Glycine max-very labile, especially above pH 8.0287920
8.5-Saccharomyces cerevisiae-27°C, half-life: 2 days287937

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
1560Sardina pilchardus-pre-incubation for 10 min at temperatures varying between 15°C and 30°C does not irreversibly affect the enzyme activity, thermal inactivation occurs above 35°C and results in total activity loss at 60°C684121
1570Camelus dromedarius-pre-incubation for 10 min at temperatures varying between 20 and 32°C does not irreversibly affect the enzyme activity, thermal inactivation occurs above 35°C and results in total activity loss at 70°C684127
15-Pseudomonas aeruginosa-5 min, stable287919
27-Saccharomyces cerevisiae-pH 8.5, half-life: 2 days287937
35-Dissostichus mawsoni-30 min, stable up to287978
43-Rattus norvegicus-30 min, 50% inactivation, irreversible287929
45-Oryctolagus cuniculus-GAPDH is inactivated at 45°C, alpha-crystallin accelerates the thermal inactivation of GAPDH at 45°C and reduces thermostability of the enzyme, while GroEL does not affect thermal inactivation and denaturation of GAPDH713466
50-Saccharomyces cerevisiae-pH 7.5, half-life: 3 h287937
50-Bacillus cereus-pH 7.5, 60 min, stable287974
55-Pseudomonas aeruginosa-5 min, complete loss of activity287919
55-Bacillus coagulans-5 min, 96-98% loss of activity. No inactivation if the ionic strength is increased to 1.8 by addition of NaCl or (NH4)2SO4287963
55-Dissostichus mawsoni-30 min, 50% loss of activity287978
58-Oryctolagus cuniculus-pH 7.0, 20 min, 50% inactivation287946
6070Geobacillus stearothermophilus-retains structural integrity and enzymatic activity up to287962
60-Bacillus cereus-pH 7.5, 30 min, about 40% loss of activity287974
61.6-Oryctolagus cuniculus-thermal unfolding of GAPDH is characterized by sharp thermal transition with a maximum at 61.6°C, GAPDH stability is diminished in the presence of alpha-crystallin (0.4 mg/ml)685613
62-Geobacillus stearothermophilus-maximum of thermal transition peak of tetrameric form of mutant apoenzyme N313T654653
64.8-Geobacillus stearothermophilus-maximum of thermal transition peak of dimeric mutant apoenzyme T34Q/T39S/L43Q; maximum of thermal transition peak of tetrameric mutant apoenzyme T34Q/T39S/L43Q654653
65.4-Geobacillus stearothermophilus-maximum of thermal transition peak of dimeric mutant apoenzyme Y46G/S48G654653
65.5-Geobacillus stearothermophilus-maximum of thermal transition peak of dimeric mutant apoenzyme Y46G/R52G654653
66-Oryctolagus cuniculus-melting temperature at 66°C686481
68.4-Geobacillus stearothermophilus-maximum of thermal transition peak of tetrameric mutant apoenzyme Y283V654653
70-Bacillus cereus-loss of activity within a few min287974
70.3-Geobacillus stearothermophilus-maximum of thermal transition peak of tetrameric mutant apoenzyme D283G654653
70.7-Geobacillus stearothermophilus-maximum of thermal transition peak of tetrameric mutant apoenzyme W310F654653
71-Geobacillus stearothermophilus-maximum of thermal transition peak of dimeric mutant apoenzyme D282G654653
73.5-Geobacillus stearothermophilus-maximum of thermal transition peak of dimeric mutant apoenzyme Y283V654653
75-Geobacillus stearothermophilus-pH 7.0, 20 min, 50% inactivation287946
78.5-Geobacillus stearothermophilus-maximum of thermal transition peak of tetrameric form of wild-type apoenzyme654653
80102Thermotoga maritima-the enzyme is fully active at temperatures near 80°C but has very low activity at room temperature, the melting temperature is at 102°C686481
85-Thermus thermophilus-pH 8.5, protein concentration 2.1 mg/ml, 10 min, stable287968
90-Thermus thermophilus-slow inactivation287938
90-Thermus thermophilus-pH 8.5, protein concentration 2.1 mg/ml, 10 min, about 20% loss of acticity287968
90-Geobacillus stearothermophilus-10 min, about 10% inactivation287970
95-Thermotoga maritima-t1/2 at pH 5.0: 25 min, t1/2 at pH 6.0: more than 120 min, t1/2 at pH 7.5: 50 min287906
95-Thermus thermophilus-pH 8.5, protein concentration 2.1 mg/ml, 10 min, about 85% loss of acticity287968
100-Thermotoga maritima-t1/2: above 120 min at pH 6287906
100-Thermus aquaticus-pH 7.0, 20 min, 50% inactivation287946
109-Thermotoga maritima-transition temperature287906
additional information-Thermotoga maritima-incubation at 70-85°C results in an apparent activation287906
additional information-Haloarcula vallismortis-temperature of 50% inactivation increases by 15°C, when KCl concentration is increased from 1 M to 4 M or when 1 M KCl is replaced by 1 M (NH4)2SO4287907
additional information-Geobacillus stearothermophilus-three salt bridges made by each subunit to others would make a major contribution to thermostability of the tetramer287962

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
8 M urea, 30°C, 0.05 M phosphate buffer, 50% loss of activity after 1 minBacillus coagulans-287963
5.0 M guanidine-HCl, rapid and irreversible inactivation at 30°CGeobacillus stearothermophilus-287970
8.0 M urea, unusually resistant at 30°C, 40°C and 50°C. Rapid inactivation at 55°C and at 60°CGeobacillus stearothermophilus-287970
very stable in 4 M KCl. Inactivated within 12 h in 0.5 M KCl, 50 mM Tris-HCl, pH 8.0, at 25°CHaloarcula vallismortis-287907
acetylleucine chloromethyl ketone binds to GAPDH to modulate the conformation of the enzyme, the modified enzyme is susceptible to chymotrypsin-like protease activity, cleavage at TRp195-Arg196Homo sapiens-654926
binding to erythrocyte membranes stabilizes the enzyme at 4°CHomo sapiens-287950
alpha-crystallin accelerates the thermal inactivation of GAPDH, while GroEL does not affect thermal inactivation and denaturation of GAPDHOryctolagus cuniculus-713466
freezing in liquid nitrogen results in partial loss of activityOryctolagus cuniculus-287933
5 M, 0°C, 1 h, complete loss of activity, 5 mM NAD+ protectsSus scrofa-287966
1% SDS, fully activeThermus thermophilus-287938
8 M urea, 40% inactivationThermus thermophilus-287938, 287968
repeated freezing and thawing brings about 10-20% inactivationThermus thermophilus-287968
rapid loss of activity without protection by a thiolZymomonas mobilis-3241

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
stable after reactivation and desalting for at least 2 h when incubated in the presence of 20 mM dithiothreitol, but less stable when both, NAD+ and the reductant, are omitted in the pre-incubation assays, under this condition the enzymes seem to be very sensitive towards traces of oxygen in the media, but upon addition of 20 mM dithiothritol after 1 h, the full activity is restoredArabidopsis thalianaP25858, Q56WJ4689409
stable after reactivation and desalting for at least 2 h when incubated in the presence of 20 mM dithiothreitol, but less stable when both, NAD+ and the reductant, are omitted in the pre-incubation assays, under this condition the enzymes seem to be very sensitive towards traces of oxygen in the media, but upon addition of 20 mM dithiothritol after 1 h, the full activity is restoredOryctolagus cuniculus, Saccharomyces cerevisiae, Spinacia oleracea-689409
the purified enzyme remains mostly unmodified or without any sign of degradation after exposure to NO or H2O2Tetrahymena pyriformis-688066

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
2°C, stable for several monthsApis mellifera-287971
4°C, in 67% saturated ammonium sulfate solution containing EDTA and dithiothreitol, stable for monthsGeobacillus stearothermophilus-287970
-20°C, 50 mM potassium phosphate buffer, pH 7.4, stable for at least 2 weeksGlycine max-287902
at -20°C storage after dialysis following the first (NH4)2SO4 fractionation step during purification, normal muscle and leukocyte enzyme is stable. Enzyme from chronic myeloid leukemia patients and sarcoma tissue loses about 80% of activity.Homo sapiens-696174
-20°CLactococcus lactis-712937
4°C, crystalline suspension in 67% saturated ammonium sulfate containing EDTA, KCN, and dithioerythritol is stable for many monthsOryctolagus cuniculus-287969
5°C, stable for several monthsOryctolagus cuniculus-287933
0-4°C, no substantial loss of activity after several monthsPisum sativum-287936
-80°C, HEPES buffer, pH 7.25, 500 mM NaCl, 5% glycerol, 2 mM DTT, 0.025% sodium azidePlasmodium falciparumQ8IKK7677046
4°C, 1 mM EDTA, 75% glycerol, stablePseudomonas aeruginosa-287919
-20°C, 30% of the original activity remains after 6 monthsSpinacia oleracea-287935
4°C, pentalenolactone-insensitive enzyme stable up to 6 months. Pentalenolactone-sensitive enzyme loses activity with a half-life of 7 daysStreptomyces arenae-287930
-20°C, stable for at least 2 yearsThermus thermophilus-287938, 287968
-80°C, triethanolamine (100 mM, pH 7.5), containing 1.0 mM beta-mercaptoethanol, 1.0 mM EDTA, 30 mM sodium arsenate heptahydrate, 1.0 mM phenylmethylsulfonyl fluoride, 50 mM NAD+, 1.0 mM pepstatin, 1.0 mM leupeptin, 0.5 M KCl, and glycerol 10% (v/v), 8 months, 1% loss of activityTrypanosoma cruzi-684427
25°C, free enzyme in Tris-HCl (50 mM, pH 8.6), containing 1.0 mM beta-mercaptoethanol, 30 mM sodium arsenate heptahydrate, and 1.0 mM EDTA, 99% of the enzymatic activity is retained after 24 h and 57% after 120 hTrypanosoma cruzi-684427
4°C, free enzyme in buffer 8, 55% of the enzymatic activity is retained after dialysis and after 48 h the calculated activity has fallen to 7%Trypanosoma cruzi-684427
4°C, free enzyme in Tris-HCl (50 mM, pH 8.6), containing 1.0 mM beta-mercaptoethanol, 30 mM sodium arsenate heptahydrate, and 1.0 mM EDTA, 55% of the enzymatic activity is retained after dialysis and after 48 h the calculated activity has fallen to 25%Trypanosoma cruzi-684427

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Apis mellifera-287971
-Arabidopsis thaliana-673587
ammonium sulfate precipitation and Q-Sepharose column chromatographyArabidopsis thalianaP25858, Q56WJ4689409
purification protocol comprises two anion-exchange chromatographic steps and removing of the His tagArabidopsis thaliana-663144
histidine fusion protein in Escherichia coli TOP 10 strainAscaris suumQ95YJ4656745
-Bacillus cereus-287974
-Bacillus coagulans-287963
active-site CNBr peptideBacillus coagulans-287944
-Bos taurus-287905, 287979
hydrophobic chromatography on immobilized colchicineBos taurus-287911
isoenzyme 1 and 2Caenorhabditis elegans-287928
ammonium sulfate fractionation and Blue Sepharose column chromatographyCamelus dromedarius-684127
Ni-NTA column chromatography, SP Sepharose column chromatography, and Superdex 200 gel filtrationCryptosporidium parvum-711617
-Cyanophora paradoxa-11542
-Dissostichus mawsoni-287978
-Drosophila melanogaster-287924
-Escherichia coli-287983
glutathione Sepharose 4B resin column chromatographyEscherichia coli-687114
-Euglena gracilis-287973
-Geobacillus stearothermophilus-287946, 287947, 287970
mutant enzyme C149selenocysteineGeobacillus stearothermophilus-287984
using gel filtration on a AcA-34 column, and a Q-Sepharose and phenyl-Sepharose columnGeobacillus stearothermophilus-672306
-Glycine max-287902
-Haloarcula vallismortis-287907
-Homo sapiens-287932, 287950, 654926
4 enzyme forms: E6.6, E6.8, E8.5 and E9.0Homo sapiens-287913
analytical centrifugationHomo sapiens-687584
by affinity chromatography on a Hi-Trap chelating column charged with nickel sulfate, the His tag is cleaved and the enzyme is purified by an additional gel filtration stepHomo sapiens-671066
DEAE-Sepharose column chromatography, ammonium sulfate precipitation, phenyl-Sepharose 6 column chromatography, and Superose 6 gel filtrationHomo sapiens-686867
from normal leukocytes of healthy subjects, leukocytes of chronic myeloid leukemia patients and from sarcoma tissueHomo sapiens-696174
GST-fusion proteins are expressed in Escherichia coli and subsequently purified by absorption to glutathione-Sepharose beads, GST is seperated by digestion with thrombin proteaseHomo sapiens-676259
Ni-NTA agarose resin chromatography and Hi-Load 16/60 Superdex gel filtrationHomo sapiens-687602
Ni2+-NTA agarose resin chromatographyHomo sapiens-684972
phenyl Sepharose column chromatographyHomo sapiensO14556685294
red blood cell cytosol is prepared by hypotonic shock or freeze-thawing cycles, membranes are prepared by hypotonic lysisHomo sapiens-673629
use of immunoaffinity column chromatographyHomo sapiens-695298
using Ni-NTA resin and a HiTrap Blue column, the His tag is removedHomo sapiens-671070
using a nickel-nitrilo-triacetic acid-agarose columnKluyveromyces marxianus-674688
NAD affinity chromatographyLactobacillus crispatus-687380
DEAE-Toyopearl column chromatography and hydroxyapatite column chromatographyLactobacillus plantarum-687344
-Lactococcus lactis-712937
use of glyceraldehyde-3-phosphate dehydrogenase-depleted human erythrocyte ghosts as specific high affinity adsorbents for the purificationMus musculus-287958
ammonium sulfate precipitation, DEAE-cellulose DE-52 column chromatography, and Cibacron Blue Sepharose column chromatographyNeisseria meningitidis-688953
-Oryctolagus cuniculus-287969
affinity column chromatography and Sephadex G-100 gel filtrationOryctolagus cuniculus-685613
ammonium sulfate precipitation and Q-Sepharose column chromatographyOryctolagus cuniculus-689409
GAPDH is subjected to gel filtration on a Sephadex G-100 columnOryctolagus cuniculus-672402
large-scale purificationOryctolagus cuniculus-287972
Ni-NTA agarose resin chromatography and Hi-Load 16/60 Superdex gel filtrationOryctolagus cuniculus-687602
purified on a Ni-nitrilotriacetic acid resin columnParacoccidioides brasiliensisQ8X1X3673986
-Pisum sativum-287936
purified on Superflow NTA nickel resin and gel chromatography, Superdex 75 26/60Plasmodium falciparumQ8IKK7677046
the filtered supernatant of the centrifuged cell lysate is applied onto 3 ml Talon resin, the His-tag is removed, further purification by gel filtrationPlasmodium falciparum-671063
-Pleurodeles waltlQ8AXB5655270
radiommunoprecipitation with protein agarose A/G beadRattus norvegicus-686305
-Saccharomyces cerevisiae-287937, 287975
ammonium sulfate precipitation and Q-Sepharose column chromatographySaccharomyces cerevisiae-689409
high-affinity cAMP-binding protein I and IISaccharomyces cerevisiae-287948
isoenzyme TLAb-1 and TLAb-2Saccharomyces cerevisiae-287899
ammonium sulfate fractionation and Blue Sepharose column chromatographySardina pilchardus-684121
-Spinacia oleracea-287935, 287961
ammonium sulfate precipitation and Q-Sepharose column chromatographySpinacia oleracea-689409
native GAPDH is purified from spinach chloroplastsSpinacia oleracea-673587
Ni-Sepharose column chromatography and Superdex 75 gel filtrationStaphylococcus aureus-710757
recombinant protein is purified using glutathione-Sepharose 4B and PreScission proteaseStreptococcus pyogenesP0C0G6674559
-Streptomyces arenae-287930
-Sus scrofa-287934, 287966, 3246
ammonium sulfate precipitation and DEAE-cellulose DE-52 column chromatographyTetrahymena pyriformis-688066
-Thermotoga maritima-287906
-Thermus aquaticus-287946
-Thermus thermophilus-287938, 287968
cytosolic isoenzymeTrypanosoma brucei-287900
-Trypanosoma cruzi-684427
-Vigna radiata var. radiata-287949
-Xenopus laevis-655270

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
expression in Escherichia coliAntheraea mylitta-695391
expressed in Escherichia coli BL21(DE3)pLysS cellsArabidopsis thalianaP25858, Q56WJ4689409
for expression in Escherichia coli BL21DEArabidopsis thaliana-673587
into the pET28a vector for expression in Escherichia coli BL21DE3 cells, amplificatied in Escherichia coli HB101 cellsArabidopsis thaliana-663144
expressed as a histidine fusion protein in Escherichia coli TOP 10 strainAscaris suumQ95YJ4656745
expression in Escherichia coliBacillus megateriumP23722679982
determination of complete nucleotide sequence of the coding as well as the noncoding flanking regions of the geneCaenorhabditis elegans-287918
expressed in Escherichia coliCryptosporidium parvum-711617
expression in Escherichia coliCryptosporidium parvum-697008
genome contains two unlinked genes for D-glyceraldehyde 3-phosphate dehydrogenase: one of them encodes a protein of 37000 Da and the other a protein of 35500 DaDrosophila melanogaster-287924
expression in Escherichia coliDunaliella salinaB1PL92697508
-Emericella nidulans-287915
-Escherichia coli-698374
expressed in Escherichia coli strain BL21(DE3)Escherichia coli-687114
cloned into the pBluescript vector for expression in Escherichia coli GM-109 cellsGeobacillus stearothermophilus-672306
expression of wild-type and mutant enzyme W84F in Escherichia coliGeobacillus stearothermophilus-287947
-Homo sapiens-287925
expressed in Escherichia coliHomo sapiens-684972
expressed in Escherichia coli strainW3CG and in HeLa cellsHomo sapiens-687602
expressed in Escherichia coli TRG8 cellsHomo sapiens-686080
expressed in HEK-293T cellsHomo sapiens-688661
expressed in MCF-7 cellsHomo sapiens-684120
expressed in prostate cancer cell lines PC-3 and LNCaPHomo sapiens-687584
expression in 293Tcells and HepG2.2.15 cellsHomo sapiens-695939
expression in COS-7 cellHomo sapiens-698989
expression in Escherichia coliHomo sapiens-699592
into a pGEX-5X-3 and a pGFP-C2 vectorHomo sapiens-676259
subcloned into a pET14b vector for expression in Escherichia coli BL21DE3 cellsHomo sapiens-671070
subcloned into the pET15b vector for expression in Escherichia coli cellsHomo sapiens-671066
cloned into the pQE32 vector for expression in Escherichia coli M15 cellsKluyveromyces marxianus-674688
expressed in Escherichia coli JM109 cellsLentinus polychrousD3K1B6710790
expressed in Escherichia coli XL1-blue cells transformed with pNeis2Neisseria meningitidis-688953
expressed in Escherichia coli strain W3CG and in HeLa cellsOryctolagus cuniculus-687602
expression in sf21 cellOryctolagus cuniculus-695902
into the TOPO pET100 expression vector for transformation of Escherichia coli XL1-Blue competent cellsParacoccidioides brasiliensisQ8X1X3673986
expression in Escherichia coliPinus sylvestris-287956
nuclear-encoded, plastid specific enzymePinus sylvestris-287922
into the pET14b vector for expression in Escherichia coli BL21 Star cellsPlasmodium falciparumQ8IKK7677046
into the pET15b vector for expression in Escherichia coli BL21DE3 cellsPlasmodium falciparum-671063
-Pleurodeles waltlQ8AXB5655270
expression in Escherichia coliPseudomonas sp.A7LHM7698639
-Rattus norvegicus-287925, 698925
expression in INS-1 cellsRattus norvegicusP04797696464
the rat cDNA library is cloned in the target vector pTRG, Escherichia coli is used as a reporter strainRattus norvegicus-674503
-Saccharomyces cerevisiae-287952, 287954
-Sinapis alba-287923
a 1200 bp fragment of the phosphorylating GAPC encoding cDNA is cloned in the antisense orientation under control of the CaMV 35S promoter into the plasmid pBinAR for transformation of Agrobacterium tumefaciensSolanum tuberosumQ8LK04675137
-Staphylococcus aureusQ6GIL8695363
expressed in Escherichia coli M15 cellsStaphylococcus aureus-710757
a 1008 bp DNA fragment from the plr-sdh-gapdh gene is ligated into the vector pGEX-6P-1 for expression of the protein in Escherichia coli BL212DE3 cellsStreptococcus pyogenesP0C0G6674559
-Trypanosoma cruzi-684427
two genes for glyceraldehyde-3-phosphate dehydrogenaseTrypanosoma cruzi-287912
-Xenopus laevis-655270
-Zymomonas mobilis-287916

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
isoform GAPC-1, expression is strong and ubiquitous, insensitive to dark treatments, and unaffected by sucrose; isoform GAPCp-1, expression is ubiquitous, but at lower level than expression of cytosolic isoform GAPC-1. Expression in leaf slowly decreases in the dark and is stable in sucrose-treated leavesArabidopsis thaliana-656414
GAPDH transcript levels are greatly increased by H2O2 treatmentArabidopsis thaliana-700672
GAPDH-small interfering RNA knockdown sensitizes the cells to methyl methane sulfonate and bleomycin, which generate lesions that are repaired by APE1, but cells show normal sensitivity to 254-nm UV. GAPDH knockdown cells exhibit an increased level of spontaneous abasic sites in the genomic DNA as a result of diminished APE1 endonuclease activityHomo sapiens-698825
24 h after irradiation at 5 gray, nuclear GAPDH levels increase 2.6fold, whereas total GAPDH increases only 1.2fold. Knockdown of GAPDH by siRNA leads to sensitization to X-ray-induced cell deathHomo sapiens-696824
heat (45°C) and cold (10°C) treatments for 6 h increase the expression level of GAPDH gene approximately 6fold, whereas ethanol (6% (v/v)) and salt (1 M) treatments for 6 h increase the expression of the GAPDH gene about 3fold, as compared to the control conditionLentinus polychrousD3K1B6710790
transcription of GAPDH1 is affected by neither bacterial like Escherichia coli, Edwardsiella tarda, Vibrio anguillarum or Streptococcus iniae nor viral such as rockbream iridovirus, RBIV challengesOplegnathus fasciatusB5AAJ5, B5AAJ6698019
mRNA expression of rbGAPDH2 is up to 25fold up-regulated in liver resulting from bacterial infections andmore than sixfold upregulated in liver and up to fivefold in kidney upon viral infectionOplegnathus fasciatusB5AAJ5, B5AAJ6698019

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
C153SArabidopsis thaliana-mutant, having only one cysteine in the catalytic site, is oxidized and glutathionylated similarly to the wild-type enzyme673587
D32ABacillus subtilis-activity of mutant enzyme D32A with NAD+ is equal to that of the wild-type enzyme, mutant enzyme also shows activity with NADP+, about 3% of the activity with NAD+287980
D32A/L187NBacillus subtilis-wild-type enzyme has no activity with NADP+, the mutant enzyme D32A/L187N shows catalytic efficiency with NADP+ higher than that with NAD+287980
L187NBacillus subtilis-activity of mutant L187N with NAD+ is higher than that of the wild-type enzyme, mutant enzyme also shows activity with NADP+, about 7% of the activity with NAD+287980
C153SCryptosporidium parvum-about 450fold decrease in activity697008
C153SCryptosporidium parvum-the specific activity of the mutant enzyme is approximately 450fold lower than that of the wild type enzyme711617
N313T/Y317GEscherichia coliP0A9B2dissociation constant for NAD+ is 300times higher than that of the wild-type enzyme. Conformational equilibrium between the syn and the anti forms with a preference for the anti conformer287927
Y317AEscherichia coliP0A9B2dissociation constant for NAD+ is 5times higher than that of the wild-type enzyme. Wild-type syn orientation of bound nicotinamide remains unchanged287927
Y317GEscherichia coliP0A9B2dissociation constant for NAD+ is 13times higher than that of the wild-type enzyme. Wild-type syn orientation of bound nicotinamide remains unchanged287927
C149AGeobacillus stearothermophilus-mutant enzyme displays no significant dehydrogenase activity656119
C149SGeobacillus stearothermophilus-low but significant phosphorylating dehydrogenase activity656119
C149selenocysteineGeobacillus stearothermophilus-mutant enzyme has selenoperoxidase activity287984
D186GGeobacillus stearothermophilus-behavior in NAD+ binding is similar to that of the wild type enzyme287985
D186G/E276GGeobacillus stearothermophilus-positive cooperativity in binding the coenzyme NAD+287985
D282GGeobacillus stearothermophilus-enzyme exists as dimer and tetramer, the tetramer is inactive, the dimer is slightly active, 650fold decrease in turnover number for NAD+, 5.8fold increase in Km-value for NAD+ compared to wild-type enzyme654653
E276GGeobacillus stearothermophilus-behavior in NAD+ binding is similar to that of the wild type enzyme287985
L187A/P188SGeobacillus stearothermophilus-the mutant is catalytically active not only with NAD+, as the wild-type enzyme, but also with NADP+287909
N313TGeobacillus stearothermophilus-mutant enzyme with a drastic decrease in thermostability, weakening of cooperative interactions between the catalytic and the cofactor domains and an inefficient binding of NAD+, mutant enzyme exists only as tetramer, 65fold decrease in turnover number for NAD+, 50fold increase in Km-value for NAD+ compared to wild-type enzyme654653
T34Q/T39S/L43QGeobacillus stearothermophilus-drastic decrease in thermostability, inefficient NAD+ binding, enzyme exists as dimer and tetramer, the tetramer is inactive, the dimer is slightly active, 650fold decrease in turnover number for NAD+, 4fold increase in Km-value for NAD+ compared to wild-type enzyme654653
W310FGeobacillus stearothermophilus-mutant enzyme with a drastic decrease in thermostability, mutant enzyme exists only as tetramer, 2fold increase of Km-value for NAD+, 1.3fold decrease in turnover number compared to wild-type enzyme654653
W84FGeobacillus stearothermophilus-slightly lower Km-values for NAD+ and glyceraldehyde 3-phosphate, slightly higher Km-value for phosphate. The construction of the mutant permitts the identification of the individual fluorescence and phosphorescence characteristics of the two Trp residues W84 and W310 in the native enzyme287947
Y283VGeobacillus stearothermophilus-mutant enzyme with a drastic decrease in thermostability, dimeric form is inactive, KM-value and turnover-number of tetramer are nearly identical to that of the wild-type654653
Y46GGeobacillus stearothermophilus-behavior in NAD+ binding is similar to that of the wild type enzyme287985
Y46G/R52GGeobacillus stearothermophilus-inactive mutant enzyme, only exists as dimer654653
Y46G/S48GGeobacillus stearothermophilus-positive cooperativity in binding the coenzyme NAD+287985
Y46G/S48GGeobacillus stearothermophilus-inactive mutant enzyme, only exists as dimer654653
C149AHomo sapiens-mutant has almost completely lost the ability to bind telomere. Upon expression in A-549 cells, mutant localizes to the nucleus but is unable to confer any significant protection of telomeres against chemotherapy-induced degradation or growth inhibition699592
C152GHomo sapiens-mutant retains the ability to interact with but is unable to reactivate DNA repair enzyme APE1698825
C156GHomo sapiens-mutant retains the ability to interact with but is unable to reactivate DNA repair enzyme APE1698825
A229VMus musculus-exhibits 50-55% residual activity in blood compared to the wild type enzyme688791
C281WMus musculus-exhibits 50-55% residual activity in blood compared to the wild type enzyme688791
G166DMus musculus-exhibits 50-55% residual activity in blood compared to the wild type enzyme688791
V239IMus musculus-exhibits 50-55% residual activity in blood compared to the wild type enzyme688791
Y327NMus musculus-exhibits 50-55% residual activity in blood compared to the wild type enzyme688791
C149SOryctolagus cuniculus-treatment of with (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide at 0.1 mM leads to low levels of aggregation (5% of wild type)687602
C149S/C281SOryctolagus cuniculus-mutant shows a complete absence of aggregation in the presence of (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide687602
C153SOryctolagus cuniculus-aggregation can be detected at low concentrations of (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide (0.001 mM) and is enhanced at higher concentrations687602
C244AOryctolagus cuniculus-aggregation can be detected at low concentrations of (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide (0.001 mM) and is enhanced at higher concentrations687602
C281SOryctolagus cuniculus-the levels of aggregation in C281S are reduced to 45% of wild type at 0.1 mM (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide687602
T227ARattus norvegicusP04797mutation at site of O-GlcNAcylation. Mutation induces the cytoplasmic accumulation of glyceraldehyde 3-phosphate dehydrogenase696464
C151/H178NStaphylococcus aureus-the rate of the forward reaction is decreased by 47000 times compared to the wild type enzyme with similar affinity for the substrate and the coenzyme712766
C151GStaphylococcus aureus-the mutant is completely inactive712766
C151SStaphylococcus aureus-the mutant shows drastically reduced kcat values compared to the wild type enzyme712766
H178NStaphylococcus aureus-the mutant shows no significant difference in the Km values of D-glyceraldehyde 3-phosphate, phosphate, and NAD+ compared to the wild type enzyme, however, the mutation results in the reduction of kcat of oxidative phosphorylation by 1400times712766
C159SArabidopsis thalianaP25858, Q56WJ4the mutant C159S of the isozyme GapC2 shows decreased specific activity689409
additional informationArabidopsis thaliana-GAPC-1 antisense line shows a delay in growth, morpholigical alterations in siliques, and low seed number. Embryo development is altered, showing abortions and empty embryonic sacs in basal and apical siliques, respectively. Mutant shows a decrease in the expression and activity of aconitase and succinate dehydrogenase and reduced levels of pyruvate and several Krebs cycle intermediates, and increased reactive oxygen species levels700811
C149AEscherichia coli-mutation abolishes NAD+-dependent ADP-ribosylation of the enzyme698374
additional informationEscherichia coli-replacement of Escherichia coli GapA glyceraldehyde 3-phosphate dehydrogenase by Clostridium acetobutylicum GapC glyceraldehyde 3-phosphate dehydrogenase, EC 1.2.1.9 results in significant reduction of flux through the pentose phosphate pathway. Recombinant strains display increased NADPH availability, and consistently higher productivity than parent strains699988
D32AHomo sapiens-mutant is unable to bind NAD+, is enzymatically inactive and has almost completely lost the ability to bind telomere. Upon expression in A-549 cells, mutant localizes to the nucleus but is unable to confer any significant protection of telomeres against chemotherapy-induced degradation or growth inhibition699592
additional informationHomo sapiens-mutant htt shows co-localization of GAPDH with N-terminus of huntingtin aggregates684120
I308SMus musculus-exhibits 50-55% residual activity in blood compared to the wild type enzyme688791
additional informationMus musculus-mutants Gapdhm1Neu (Y91stop truncated protein of 89 amino acids), Gapdhm2Neu (truncated/altered protein of 9 amino acids), and Gapdhm8Neu (truncated/altered protein of 73 amino acids) exhibit 50-55% residual activity in blood compared to the wild type enzyme688791

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
GroEL-assisted reactivation after denaturation of GAPDH in the presence of guanidine hydrochlorideOryctolagus cuniculus-672402
lysis buffer contains 6 M guanidine hydrochloride, during purification bound proteins are eluted with native elution buffer to refold the proteinParacoccidioides brasiliensisQ8X1X3673986

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
medicineHomo sapiens-functions are of chemotherapeutic interest, structure is a necessity for structure-based drug design671066
medicineHomo sapiens-target for the design of antitrypanosomatid and anti-apoptosis drugs671070
medicineHomo sapiens-pathogenesis of Porphyromonas gingivalis involves interaction with oral mucosal epithelial cells, mediated by binding glyceraldehyde-3-phosphate dehydrogenase673706
medicineHomo sapiens-action as a selective insulin receptor modulator688250
medicineHomo sapiens-glyceraldehyde 3-phosphate dehydrogenase may be involved in the postranscriptional regulation of hepatitis B virus. Recombinant glyceraldehyde 3-phosphate dehydrogenase binds to hepatitis B virus regulatory element RNA in vitro and inhibits hepatitis B virus regulatory element function. Overexpression of glyceraldehyde 3-phosphate dehydrogenase depresses the expression of hepatitis B virus antigen695939
medicineHomo sapiens-glyceraldehyde 3-phosphate dehydrogenase from malignant sources shows altered properties compared with enzyme from healthy subjects696174
medicineHomo sapiens-among 256 ovarian and fallopian tube cancer specimens, GAPDH is regulated, with almost 50% of specimens having no GAPDH staining.Low GAPDH staining is associated with a low macrophage colony stimulating factor CSF-1 score700133
medicineMus musculus-in experimental autoimmune encephalomyelitis, the proportion of S-nitrosylated neurofilament proteins, NMDA receptors, alpha/beta-tubulin, beta-actin, and GAPDH is increased. Neuronal specific enolase is the major S-nitrosylated protein in acute experimental autoimmune encephalomyelitis699686
medicineOryctolagus cuniculus-pathogenesis of Porphyromonas gingivalis involves interaction with oral mucosal epithelial cells, mediated by binding glyceraldehyde-3-phosphate dehydrogenase673706
medicineOryctolagus cuniculus-non-native forms of GAPDH may be involved in the formation of amyloid structures during Alzheimer's disease, binding to soluble amyloid-beta peptide696421
medicineParacoccidioides brasiliensisQ8X1X3the pathogenic fungus causes paracoccidioidomycosis, GAPDH is reported as an adhesin, which can be related to fungus adhesion and invasion673986
medicinePlasmodium brasilianumB0F3R1G3PDH is a potential target for antimalarial drug development687069
medicinePlasmodium coatneyiB0F3R2G3PDH is a potential target for antimalarial drug development687069
medicinePlasmodium cynomolgiB0F3R8G3PDH is a potential target for antimalarial drug development687069
medicinePlasmodium falciparum-potential antimalarial target671063
medicinePlasmodium falciparumQ8IKK7crystallography may provide structural detail for the development of lead compounds and drug design of novel antimalarials677046
medicinePlasmodium falciparumB0F3R3G3PDH is a potential target for antimalarial drug development687069
medicinePlasmodium fragileB0F3R4G3PDH is a potential target for antimalarial drug development687069
medicinePlasmodium knowlesi strain HB0F3R5G3PDH is a potential target for antimalarial drug development687069
medicinePlasmodium malariaeB0F3R6G3PDH is a potential target for antimalarial drug development687069
medicinePlasmodium reichenowiB0F3R7G3PDH is a potential target for antimalarial drug development687069
medicinePlasmodium vivaxB0F3R9G3PDH is a potential target for antimalarial drug development687069
medicineRattus norvegicus-in diabetic rats, modification of GAPDH by S-(2-succinyl)cysteine is increased in muscle, and the extent of succination correlates strongly with the decrease in specific activity of the enzyme695595
pharmacologySchistosoma mansoni-lung-stage schistosomula immunofluorescence reactivity is diminished following antiserum absorption with reconbinant glyceraldehyde 3-phosphate dehydrogenase. Discussion of glyceraldehyde 3-phosphate dehydrogenase as a candidate vaccine antigen698033
medicineStreptococcus pyogenesP0C0G6the Plr-SDH-GAPDH complex participates in invasive streptococcal infections674559

DISEASETITLE OF PUBLICATIONLINK TO PUBMED
6-phosphofructokinase deficiencyIodoacetate inhibition of glyceraldehyde-3-phosphate dehydrogenase as a model of human myophosphorylase deficiency (McArdle's disease) and phosphofructokinase deficiency (Tarui's disease). PubMed
AcidosisEffects of ketoacidosis on rat apolipoprotein A1 gene expression: a link with acidosis but not with ketones. PubMed
AcidosisEffects of treatment with pyruvate and tromethamine in experimental myocardial ischemia. PubMed
Acidosis, LacticRegulation of glyceraldehyde 3-phosphate dehydrogenase expression by metformin in HepG2 cells. PubMed
Acquired Immunodeficiency SyndromeHaemophilus influenzae uses the surface protein E to acquire human plasminogen and to evade innate immunity. PubMed
ACTH-Secreting Pituitary AdenomaExpression of the pituitary transcription factor Ptx-1, but not that of the trans-activating factor prop-1, is reduced in human corticotroph adenomas and is associated with decreased alpha-subunit secretion. PubMed
Acute Kidney InjuryThe modifier protein of glyceraldehyde-3-phosphate dehydrogenase reduces free radical-mediated renal damage in a rat model of acute kidney injury. PubMed
AdenocarcinomaAssociation of glyceraldehyde-3-phosphate dehydrogenase expression with cell motility and metastatic potential of rat prostatic adenocarcinoma. PubMed
AdenocarcinomaInactivation of metabolic enzymes by photo-treatment with zinc meta N-methylpyridylporphyrin. PubMed
AdenocarcinomaIncreased expression of glycolysis-associated genes in oncogene-transformed and growth-accelerated states. PubMed
AdenocarcinomaIncreased glyceraldehyde-3-phosphate dehydrogenase gene expression in human pancreatic adenocarcinoma. PubMed
AdenocarcinomaThe cytotoxic ribonuclease onconase targets RNA interference (siRNA). PubMed
AdenomaBim-23244, a somatostatin receptor subtype 2- and 5-selective analog with enhanced efficacy in suppressing growth hormone (GH) from octreotide-resistant human GH-secreting adenomas. PubMed
AdenomaHistochemical profile of mouse hepatocellular adenomas and carcinomas induced by a single dose of diethylnitrosamine. PubMed
AlkalosisEffects of ketoacidosis on rat apolipoprotein A1 gene expression: a link with acidosis but not with ketones. PubMed
alpha-ThalassemiaA New 5' Terminal Murine GAPDH Exon Identified Using 5'RACE LaNe. PubMed
Alzheimer DiseaseAssociation and heterogeneity at the GAPDH locus in Alzheimer's disease. PubMed
Alzheimer DiseaseDecrease of dehydrogenase activity of cerebral glyceraldehyde-3-phosphate dehydrogenase in different animal models of Alzheimer's disease. PubMed
Alzheimer DiseaseExploring the association of glyceraldehyde-3-phosphate dehydrogenase gene and Alzheimer disease. PubMed
Alzheimer DiseaseIsolation of glyceraldehyde 3-phosphate dehydrogenase (Gapdh) cDNA from the distal half of mouse chromosome 16: further indication of a link between Alzheimer's disease and glycolysis. PubMed
Alzheimer DiseaseOxidatively Modified Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) and Alzheimer's Disease: Many Pathways to Neurodegeneration. PubMed
Alzheimer DiseaseQuantifying mRNA in postmortem human brain: influence of gender, age at death, postmortem interval, brain pH, agonal state and inter-lobe mRNA variance. PubMed
Alzheimer DiseaseReduction of glyceraldehyde-3-phosphate dehydrogenase activity in Alzheimer's disease and in Huntington's disease fibroblasts. PubMed
Alzheimer DiseaseSubcellular alteration of glyceraldehyde-3-phosphate dehydrogenase in Alzheimer's disease fibroblasts. PubMed
Amyotrophic Lateral SclerosisDetermination of protein and RNA expression levels of common housekeeping genes in a mouse model of neurodegeneration. PubMed
AnaphylaxisGlyceraldehyde-3-phosphate dehydrogenase as a major allergen in rambutan-induced anaphylaxis. PubMed
AnemiaIncreased membrane activity of glyceraldehyde 3-phosphate dehydrogenase in erythrocytes of patients with homozygous sickle cell anaemia. PubMed
Anemia[Activity of the enzymes phosphoglyceraldehyde dehydrogenase, lactate dehydrogenase and glucose-6-phosphate dehydrogenase in the erythrocytes in deficiency anemia] PubMed
Anemia, Sickle CellIncreased membrane activity of glyceraldehyde 3-phosphate dehydrogenase in erythrocytes of patients with homozygous sickle cell anaemia. PubMed
AnthraxSurface localized and extracellular Glyceraldehyde-3-phosphate dehydrogenase of Bacillus anthracis is a plasminogen binding protein. PubMed
ArthritisOxidation of articular cartilage glyceraldehyde-3-phosphate dehydrogenase (G3PDH) occurs in vivo during carrageenin-induced arthritis. PubMed
AvitaminosisVitamin B6 deficiency causes activation of RNA polymerase and general enhancement of gene expression in rat liver. PubMed
AzoospermiaQuantification of cyclin A1 and glyceraldehyde-3-phosphate dehydrogenase expression in testicular biopsies of infertile patients by fluorescence real-time RT-PCR. PubMed
Bacterial InfectionsDetermination of internal controls for quantitative real time RT-PCR analysis of the effect of Edwardsiella tarda infection on gene expression in turbot (Scophthalmus maximus). PubMed
Bacterial InfectionsInhibition of IL-10 production by maternal antibodies against Group B Streptococcus GAPDH confers immunity to offspring by favoring neutrophil recruitment. PubMed
beta-ThalassemiaAnalysis of Erythrocyte and Platelet Membrane Proteins in Various Forms of beta-Thalassemia. PubMed
Breast NeoplasmsCell-surface cytokeratin 8 is the major plasminogen receptor on breast cancer cells and is required for the accelerated activation of cell-associated plasminogen by tissue-type plasminogen activator. PubMed
Breast NeoplasmsCharacterization of transport protein expression in multidrug resistance-associated protein (Mrp) 2-deficient rats. PubMed
Breast NeoplasmsComparative expression of fibroblast growth factor mRNAs in benign and malignant breast disease. PubMed
Breast NeoplasmsGlyceraldehyde-3-phosphate dehydrogenase as a surface associated antigen on human breast cancer cell lines MACL-1 and MGSO-3. PubMed
Breast NeoplasmsGlyceraldehyde-3-phosphate dehydrogenase gene expression in human breast cancer. PubMed
Breast NeoplasmsGlycolaldehyde induces apoptosis in a human breast cancer cell line. PubMed
Breast NeoplasmsMeasurement of mRNA levels in tumor xenografts with quantitative autoradiography and in situ hybridization. PubMed
Breast NeoplasmsParallel assessment of circulatory cell-free DNA by PCR and nucleosomes by ELISA in breast tumors. PubMed
Breast NeoplasmsUp-regulation of glyceraldehyde-3-phosphate dehydrogenase gene expression by HIF-1 activity depending on Sp1 in hypoxic breast cancer cells. PubMed
Breast NeoplasmsVisualization of the plasmin receptor on sections of human mammary carcinoma cells. PubMed
BrucellosisBrucella abortus L7/L12 recombinant protein induces strong Th1 response in acute brucellosis patients. PubMed
Burkitt LymphomaThe mode of actions of glyceraldehyde-3-phosphate dehydrogenase identified as an immunoglobulin production stimulating factor. PubMed
CandidiasisSynthetic glycopeptide vaccines combining beta-mannan and peptide epitopes induce protection against candidiasis. PubMed
Candidiasis, InvasiveEvaluation of the usefulness of anti-glyceraldehyde-3-phosphate dehydrogenase antibodies as a treatment for invasive candidiasis in a murine model. PubMed
CarcinomaAlteration of glyceraldehyde-3-phosphate dehydrogenase activity and messenger RNA content by androgen in human prostate carcinoma cells. PubMed
CarcinomaAntisense oligodeoxynucleotide of glyceraldehyde-3-phosphate dehydrogenase gene inhibits cell proliferation and induces apoptosis in human cervical carcinoma cell lines. PubMed
CarcinomaChromatin-associated proteins HMGB1/2 and PDIA3 trigger cellular response to chemotherapy-induced DNA damage. PubMed
CarcinomaComparative proteomic analysis of esophageal squamous cell carcinoma. PubMed
CarcinomaCytokeratin 8 released by breast carcinoma cells in vitro binds plasminogen and tissue-type plasminogen activator and promotes plasminogen activation. PubMed
CarcinomaEnhanced gene expression in breast cancer cells in vitro and tumors in vivo. PubMed
CarcinomaEnzymes of carbohydrate metabolism in human breast carcinoma: relationship with serum hormones. PubMed
CarcinomaEvidence for the presence of a critical histidine residue at the active site in glyceraldehyde-3-phosphate dehydrogenase of Ehrlich ascites carcinoma cells. PubMed
CarcinomaExpression of human prostatic acid phosphatase and prostate specific antigen genes in neoplastic and benign tissues. PubMed
CarcinomaGene expression profiles in thyroid carcinomas. PubMed
CarcinomaGlyceraldehyde 3-phosphate dehydrogenase depletion induces cell cycle arrest and resistance to antimetabolites in human carcinoma cell lines. PubMed
CarcinomaGlyceraldehyde-3-phosphate dehydrogenase from Ehrlich ascites carcinoma cells its possible role in the high glycolysis of malignant cells. PubMed
CarcinomaHepatocellular glycogenosis and related pattern of enzymatic changes during hepatocarcinogenesis. PubMed
CarcinomaHistochemical profile of mouse hepatocellular adenomas and carcinomas induced by a single dose of diethylnitrosamine. PubMed
CarcinomaIdentification of a critical lysine residue at the active site in glyceraldehyde-3-phosphate dehydrogenase of Ehrlich ascites carcinoma cell. Comparison with the rabbit muscle enzyme. PubMed
CarcinomaIncreased glyceraldehyde-3-phosphate dehydrogenase expression in renal cell carcinoma identified by RNA-based, arbitrarily primed polymerase chain reaction. PubMed
CarcinomaInteraction of cytotoxic antibiotic dactylarin with glycolytic thiol enzymes in Ehrlich ascites carcinoma cells. PubMed
CarcinomaPurification of the plasmin receptor from human carcinoma cells and comparison to alpha-enolase. PubMed
CarcinomaReversible oxidation of glyceraldehyde 3-phosphate dehydrogenase thiols in human lung carcinoma cells by hydrogen peroxide. PubMed
CarcinomaSolubilization of the plasmin receptor from human carcinoma cells. PubMed
CarcinomaSpecific inhibition of glyceraldehyde-3-phosphate dehydrogenase by koningic acid (heptelidic acid). PubMed
CarcinomaThe bioenergetic signature of cancer: a marker of tumor progression. PubMed
CarcinomaThe prognostic value of tetranectin immunoreactivity and plasma tetranectin in patients with ovarian cancer. PubMed
CarcinomaVisualization of the plasmin receptor on carcinoma cells. PubMed
CarcinomaVisualization of the plasmin receptor on sections of human mammary carcinoma cells. PubMed
Carcinoma[Proteomic identification and comparison of differentiation-related proteins in gastric carcinoma cell lines] PubMed
Carcinoma, Ehrlich TumorInteraction of calcyclin and its cyanogen bromide fragments with annexin II and glyceraldehyde 3-phosphate dehydrogenase. PubMed
Carcinoma, Ehrlich TumorProperties of the glyceraldehyde-3-phosphate dehydrogenase from Ehrlich ascites tumor cells. PubMed
Carcinoma, HepatocellularComparison of glyceraldehyde-3-phosphate dehydrogenase and 28s-ribosomal RNA gene expression in human hepatocellular carcinoma. PubMed
Carcinoma, HepatocellularGlyceraldehyde-3-phosphate dehydrogenase mRNA expression in hepatocellular carcinoma. PubMed
Carcinoma, HepatocellularGlyceraldehyde-3-Phosphate Dehydrogenase: A Promising Target for Molecular Therapy in Hepatocellular Carcinoma. PubMed
Carcinoma, HepatocellularHuman hepatocellular carcinoma in a mouse model: assessment of tumor response to percutaneous ablation by using glyceraldehyde-3-phosphate dehydrogenase antagonists. PubMed
Carcinoma, HepatocellularInsulin stimulates glyceraldehyde-3-phosphate dehydrogenase gene expression through cis-acting DNA sequences. PubMed
Carcinoma, HepatocellularTargets of 3-Bromopyruvate, a New, Energy Depleting, Anticancer Agent. PubMed
Carcinoma, Non-Small-Cell LungChoice of endogenous control for gene expression in nonsmall cell lung cancer. PubMed
Carcinoma, Renal CellIncreased glyceraldehyde-3-phosphate dehydrogenase expression in renal cell carcinoma identified by RNA-based, arbitrarily primed polymerase chain reaction. PubMed
Carcinoma, Squamous CellComparative proteomic analysis of esophageal squamous cell carcinoma. PubMed
Cardiomyopathy, DilatedIdentification and expression of delta-isoforms of the multifunctional Ca2+/calmodulin-dependent protein kinase in failing and nonfailing human myocardium. PubMed
CataractRevival of inactive glyceraldehyde 3-phosphate dehydrogenase in human cataract lenses by reduction. PubMed
CataractThioredoxin, thioredoxin reductase, and alpha-crystallin revive inactivated glyceraldehyde 3-phosphate dehydrogenase in human aged and cataract lens extracts. PubMed
Chagas Disease3D QSAR studies on binding affinities of coumarin natural products for glycosomal GAPDH of Trypanosoma cruzi. PubMed
Chagas DiseaseDevelopment and characterization of an immobilized enzyme reactor (IMER) based on human glyceraldehyde-3-phosphate dehydrogenase for on-line enzymatic studies. PubMed
Chagas DiseaseDiscovery of novel Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase inhibitors. PubMed
Chagas DiseaseExpression, purification and kinetic characterization of His-tagged glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzi. PubMed
Chagas DiseaseTrypanosoma cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase: structure, catalytic mechanism and targeted inhibitor design. PubMed
ChoriocarcinomaNuclear beta-catenin and Ki-67 expression in choriocarcinoma and its pre-malignant form. PubMed
Colorectal Neoplasms[Expression of osteopontin mRNA and its protein in colorectal cancer and liver metastatic tissues] PubMed
Congenital HypothyroidismGlyceraldehyde-3-phosphate dehydrogenase activity in developing brain during experimental cretinism. PubMed
Connective Tissue DiseasesGlyceraldehyde 3-phosphate dehydrogenase is a novel autoantigen leading autoimmune responses to proliferating cell nuclear antigen multiprotein complexes in lupus patients. PubMed
ContractureMetabolic myopathy produced by acute inhibition of glyceraldehyde-3-phosphate dehydrogenase with ortho-iodosobenzoic acid. PubMed
ContractureMetabolic myopathy produced by dinitrofluorobenzene inhibition of creatine phosphokinase. PubMed
Cystic FibrosisMolecular and functional heterogeneity of cholangiocytes from rat liver after bile duct ligation. PubMed
DehydrationAntioxidative defense system, pigment composition, and photosynthetic efficiency in two wheat cultivars subjected to drought  PubMed
DengueRecombinant dengue virus-like particles from Pichia pastoris: efficient production and immunological properties. PubMed
Dental CariesValidation of reference genes for quantitative measurement of immune gene expression in shrimp. PubMed
Dermatitis, AtopicRelative importance of IL-4 and IL-13 in lesional skin of atopic dermatitis. PubMed
Diabetes ComplicationsMethylglyoxal can modify GAPDH activity and structure. PubMed
Diabetes ComplicationsRole of glyceraldehyde 3-phosphate dehydrogenase in the development and progression of diabetic retinopathy. PubMed
Diabetes ComplicationsThe pathogenesis of diabetic complications: the role of DNA injury and poly(ADP-ribose) polymerase activation in peroxynitrite-mediated cytotoxicity. PubMed
Diabetes Mellitus, Type 2Metabolism of [1,3-(13)C]glycerol-1,2,3-tris(methylsuccinate) and glycerol-1,2,3-tris(methyl[2,3-(13)C]succinate) in hepatocytes from Goto-Kakizaki rats. PubMed
Diabetic AngiopathiesRole of nitrosative stress in the pathogenesis of diabetic vascular dysfunction. PubMed
Diabetic RetinopathyGlyceraldehyde 3 phosphate dehydrogenase in retinal microvasculature: Implications for the development and progression of diabetic retinopathy. PubMed
Diabetic RetinopathyRole of glyceraldehyde 3-phosphate dehydrogenase in the development and progression of diabetic retinopathy. PubMed
Down SyndromeIncreased glyceraldehyde 3-phosphate dehydrogenase levels in the brain of patients with Down's syndrome. PubMed
Down Syndrome[Rapid diagnosis of Down's syndrome by multiplex real-time fluorescence relative quantitative PCR] PubMed
Encephalitis, JapaneseGlyceraldehyde-3-phosphate dehydrogenase (GAPDH) interaction with 3' ends of Japanese encephalitis virus RNA and colocalization with the viral NS5 protein. PubMed
Fatty LiverPeroxisome proliferator-activated receptor agonist treatment of alcohol-induced hepatic insulin resistance. PubMed
Fetal DiseasesMaternal diabetes in vivo and high glucose in vitro diminish GAPDH activity in rat embryos. PubMed
FibromaRegulation of proliferation and platelet-derived growth factor expression in palmar fibromatosis (Dupuytren contracture) by mechanical strain. PubMed
GanglioneuroblastomaExpression of the smg p25A (a ras p21-like GTP-binding protein) gene in human neuroblastoma cell lines and tumor tissues. PubMed
GanglioneuroblastomaReal-time analysis of tyrosine hydroxylase gene expression: a sensitive and semiquantitative marker for minimal residual disease detection of neuroblastoma. PubMed
GanglioneuromaReal-time analysis of tyrosine hydroxylase gene expression: a sensitive and semiquantitative marker for minimal residual disease detection of neuroblastoma. PubMed
GliomaHistone deacetylase inhibitor 4-phenylbutyrate suppresses GAPDH mRNA expression in glioma cells. PubMed
GliomaQuantitative reverse transcription-PCR measurement of tissue factor mRNA in glioma. PubMed
GlomerulonephritisA prolonged course of Group A streptococcus-associated nephritis: a mild case of dense deposit disease (DDD)? PubMed
GlomerulonephritisElevated urinary plasmin activity resistant to alpha2-antiplasmin in acute poststreptococcal glomerulonephritis. PubMed
GlomerulonephritisGlomerular plasmin-like activity in relation to nephritis-associated plasmin receptor in acute poststreptococcal glomerulonephritis. PubMed
GlomerulonephritisGroup A streptococcal antigen in the glomeruli of children with Henoch-Schönlein nephritis. PubMed
GlomerulonephritisIncreased mRNA expression of metalloproteinase-9 in peripheral blood monocytes from patients with immunoglobulin A nephropathy. PubMed
GlomerulonephritisIs the nephritogenic antigen in post-streptococcal glomerulonephritis pyrogenic exotoxin B (SPE B) or GAPDH? PubMed
GlomerulonephritisLocalization of nephritis-associated plasmin receptor in acute poststreptococcal glomerulonephritis. PubMed
GlomerulonephritisNephritis-associated plasmin receptor and acute poststreptococcal glomerulonephritis: characterization of the antigen and associated immune response. PubMed
GlomerulonephritisSequence and expression of NAPlr is conserved among group A streptococci isolated from patients with acute poststreptococcal glomerulonephritis (APSGN) and non-APSGN. PubMed
GlomerulonephritisThe potential role for nephritis-associated plasmin receptor in acute poststreptococcal glomerulonephritis. PubMed
Glomerulonephritis, IGAIncreased mRNA expression of metalloproteinase-9 in peripheral blood monocytes from patients with immunoglobulin A nephropathy. PubMed
Glomerulonephritis, MembranoproliferativeA case of idiopathic membranoproliferative glomerulonephritis with a transient glomerular deposition of nephritis-associated plasmin receptor antigen. PubMed
Glomerulonephritis, MembranousIncreased mRNA expression of metalloproteinase-9 in peripheral blood monocytes from patients with immunoglobulin A nephropathy. PubMed
Glomerulonephritis, MembranousTh2 cytokines increase and stimulate B cells to produce IgG4 in idiopathic membranous nephropathy. PubMed
Glomerulosclerosis, Focal SegmentalIncreased mRNA expression of metalloproteinase-9 in peripheral blood monocytes from patients with immunoglobulin A nephropathy. PubMed
glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) deficiencyA simple screening procedure for glucose phosphate isomerase, phosphofructokinase, aldolase and glyceraldehyde-3-phosphate dehydrogenase deficiencies. PubMed
glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) deficiencyPlastidial glyceraldehyde-3-phosphate dehydrogenase deficiency leads to altered root development and affects the sugar and amino Acid balance in Arabidopsis. PubMed
glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) deficiencyStudy of a kindred with hereditary spherocytosis and glyceraldehyde-3-phosphate dehydrogenase deficiency. PubMed
Glycogen Storage Disease Type VIodoacetate inhibition of glyceraldehyde-3-phosphate dehydrogenase as a model of human myophosphorylase deficiency (McArdle's disease) and phosphofructokinase deficiency (Tarui's disease). PubMed
Heart ArrestSelection of reference genes for quantitative real-time PCR in a rat asphyxial cardiac arrest model. PubMed
Heart FailureExpression of proinflammatory cytokines in the failing human heart: comparison of recent-onset and end-stage congestive heart failure. PubMed
Heart FailureProteomic analysis of left ventricular remodeling in an experimental model of heart failure. PubMed
Heart FailureReduced activity of enzymes coupling ATP-generating with ATP-consuming processes in the failing myocardium. PubMed
HemochromatosisLocalization of iron metabolism-related mRNAs in rat liver indicate that HFE is expressed predominantly in hepatocytes. PubMed
HepatitisSpecific interaction between the hepatitis delta virus RNA and glyceraldehyde 3-phosphate dehydrogenase: an enhancement on ribozyme catalysis. PubMed
Hepatitis AFunctional significance of the interaction of hepatitis A virus RNA with glyceraldehyde 3-phosphate dehydrogenase (GAPDH): opposing effects of GAPDH and polypyrimidine tract binding protein on internal ribosome entry site function. PubMed
Hepatitis AInteraction of glyceraldehyde-3-phosphate dehydrogenase with secondary and tertiary RNA structural elements of the hepatitis A virus 3' translated and non-translated regions. PubMed
Hepatitis ASpecific interaction of glyceraldehyde 3-phosphate dehydrogenase with the 5'-nontranslated RNA of hepatitis A virus. PubMed
Hepatitis BA yeast system for stable expression of hepatitis B surface antigen. PubMed
Hepatitis BControlled fed-batch fermentation of recombinant Saccharomyces cerevisiae to produce hepatitis B surface antigen. PubMed
Hepatitis BEvaluation of Aspergillus niger as host for virus-like particle production, using the hepatitis B surface antigen as a model. PubMed
Hepatitis BExpression of hepatitis B surface antigen in Saccharomyces cerevisiae utilizing glyceraldeyhyde-3-phosphate dehydrogenase promoter of Pichia pastoris. PubMed
Hepatitis BIdentification of glyceraldehyde-3-phosphate dehydrogenase as a cellular protein that binds to the hepatitis B virus posttranscriptional regulatory element. PubMed
Hepatitis BPhosphorylation of the hepatitis B virus core protein by glyceraldehyde-3-phosphate dehydrogenase protein kinase activity. PubMed
Hepatitis BProduction of hepatitis B virion-like particles in yeast. PubMed
Hepatitis BRole of glyceraldehyde-3-phosphate dehydrogenase binding to hepatitis B virus posttranscriptional regulatory element in regulating expression of HBV surface antigen. PubMed
Hepatitis CHuman hepatic glyceraldehyde-3-phosphate dehydrogenase binds to the poly(U) tract of the 3' non-coding region of hepatitis C virus genomic RNA. PubMed
Huntington DiseaseAlteration of nuclear glyceraldehyde-3-phosphate dehydrogenase structure in Huntington's disease fibroblasts. PubMed
Huntington DiseaseGlyceraldehyde 3-phosphate dehydrogenase abnormality in metabolically stressed Huntington disease fibroblasts. PubMed
Huntington DiseaseNeuronal death in cultured murine cortical cells is induced by inhibition of GAPDH and triosephosphate isomerase. PubMed
Huntington DiseaseOverexpression and nuclear accumulation of glyceraldehyde-3-phosphate dehydrogenase in a transgenic mouse model of Huntington's disease. PubMed
Huntington DiseaseReduction of glyceraldehyde-3-phosphate dehydrogenase activity in Alzheimer's disease and in Huntington's disease fibroblasts. PubMed
HypercholesterolemiaEffects and mechanism of turmeric vasorelaxation of the thoracic aorta in hypercholesterolemic rats. PubMed
HyperglycemiaHyperglycemia-induced mitochondrial superoxide overproduction activates the hexosamine pathway and induces plasminogen activator inhibitor-1 expression by increasing Sp1 glycosylation. PubMed
HyperglycemiaSirtuin 1-mediated cellular metabolic memory of high glucose via the LKB1/AMPK/ROS pathway and therapeutic effects of metformin. PubMed
HypertensionInfluence of pressure overload and ACE inhibitor therapy on constitutive protein mRNA expression in the spontaneously hypertensive rat. PubMed
Hypotension[Does nitric oxide stress exist?] PubMed
Infarction, Middle Cerebral ArteryGlyceraldehyde-3-phosphate dehydrogenase versus toluidine blue as a marker for infarct volume estimation following permanent middle cerebral artery occlusion in mice. PubMed
InfectionChanges in the contents of metabolites and enzyme activities in rice plants responding to Rhizoctonia solani Kuhn infection: activation of glycolysis and connection to phenylpropanoid pathway. PubMed
InfectionDifferential effects of rabies and borna disease viruses on immediate-early- and late-response gene expression in brain tissues. PubMed
InfectionEffect of acute infectious disease on human isometric muscle endurance. PubMed
InfectionEffects of a diabetogenic strain of encephalomyocarditis (EMC) virus on protein synthesis in mouse islets of Langerhans. PubMed
InfectionEvaluation of reference genes for real-time PCR studies of Brazilian Somalis sheep infected by gastrointestinal nematodes. PubMed
InfectionEvaluation of the suitability of six host genes as internal control in real-time RT-PCR assays in chicken embryo cell cultures infected with infectious bursal disease virus. PubMed
InfectionEvaluation of the usefulness of anti-glyceraldehyde-3-phosphate dehydrogenase antibodies as a treatment for invasive candidiasis in a murine model. PubMed
InfectionGlyceraldehyde-3-phosphate dehydrogenase of Edwardsiella tarda has protective antigenicity against Vibrio anguillarum in Japanese flounder. PubMed
InfectionImmunisation with Salmonella typhimurium-delivered glyceraldehyde-3-phosphate dehydrogenase protects mice against challenge infection with Echinococcus multilocularis eggs. PubMed
InfectionMucosal immunisation with novel Streptococcus pneumoniae protein antigens enhances bacterial clearance in an acute mouse lung infection model. PubMed
InfectionQuantitative detection for low levels of Helicobacter pylori infection in experimentally infected mice by real-time PCR. PubMed
InfectionRole of secreted glyceraldehyde-3-phosphate dehydrogenase in the infection mechanism of enterohemorrhagic and enteropathogenic Escherichia coli: interaction of the extracellular enzyme with human plasminogen and fibrinogen. PubMed
InfectionSecreted glyceraldehyde-3-phosphate dehydrogenase as a broad spectrum vaccine candidate against microbial infection in aquaculture. PubMed
InfectionSmall interfering RNAs that deplete the cellular translation factor eIF4H impede mRNA degradation by the virion host shutoff protein of herpes simplex virus. PubMed
InfectionThe major parasite surface antigen associated with human resistance to schistosomiasis is a 37-kD glyceraldehyde-3P-dehydrogenase. PubMed
InfectionTranslational control of viral and host protein synthesis during the course of herpes simplex virus type 1 infection: evidence that initiation of translation is the limiting step. PubMed
InfectionUsing host 28S ribosomal RNA as a housekeeping gene for quantitative real-time reverse transcription-PCR (qRT-PCR) in virus-infected animal cells. PubMed
InfectionVaccine efficacy of recombinant GAPDH of Edwardsiella tarda against Edwardsiellosis. PubMed
InfectionVACCINE-INDUCED PROTECTION AGAINST MURINE SCHISTOSOMIASIS MANSONI WITH LARVAL EXCRETORY-SECRETORY ANTIGENS AND PAPAIN OR TYPE-2 CYTOKINES. PubMed
InfertilityApproaches to post-testicular contraception. PubMed
Infertility, MaleGenome-wide profiling of gene expression in the epididymis of alpha-chlorohydrin-induced infertile rats using an oligonucleotide microarray. PubMed
Infertility, MaleGlyceraldehyde 3-phosphate dehydrogenase-S, a sperm-specific glycolytic enzyme, is required for sperm motility and male fertility. PubMed
Infertility, MaleThe plastidial glyceraldehyde-3-phosphate dehydrogenase is critical for viable pollen development in Arabidopsis. PubMed
Inflammatory Bowel Diseases5-aminosalicylic acid prevents oxidant mediated damage of glyceraldehyde-3-phosphate dehydrogenase in colon epithelial cells. PubMed
Influenza, HumanOn the mechanism of phenotypic conversion of human cervical adenocarcinoma HeLa cells surviving infection by influenza B virus: Potential implications for biological management of adenocarcinomas. PubMed
Insulin ResistanceSubmicromolar concentrations of palmitoyl-CoA specifically thioesterify cysteine 244 in glyceraldehyde-3-phosphate dehydrogenase inhibiting enzyme activity: a novel mechanism potentially underlying fatty acid induced insulin resistance. PubMed
Intellectual DisabilityA New 5' Terminal Murine GAPDH Exon Identified Using 5'RACE LaNe. PubMed
Intestinal VolvulusCloning, characterization and DNA immunization of an Onchocerca volvulus glyceraldehyde-3-phosphate dehydrogenase (Ov-GAPDH). PubMed
LeukemiaCharacterization of an immortalized oviduct cell line from the cynomolgus monkey (Macaca fascicularis). PubMed
LeukemiaStructure/function in neuroprotection and apoptosis. PubMed
Leukemia, Myelogenous, Chronic, BCR-ABL PositiveMolecular characterization of tumor associated glyceraldehyde-3-phosphate dehydrogenase. PubMed
Liver CirrhosisDown-regulation of hepatic and renal 11 beta-hydroxysteroid dehydrogenase in rats with liver cirrhosis. PubMed
Liver CirrhosisHigh serum glyceraldehyde-3-phosphate dehydrogenase levels in patients with liver cirrhosis. PubMed
Lung NeoplasmsChoice of endogenous control for gene expression in nonsmall cell lung cancer. PubMed
Lung NeoplasmsEnhanced expression of a glyceraldehyde-3-phosphate dehydrogenase gene in human lung cancers. PubMed
Lung NeoplasmsSimilarity between glyceraldehyde-3-phosphate dehydrogenase and a 37,000-dalton protein which is abundantly expressed in human lung cancers. PubMed
Lyme DiseaseA glyceraldehyde-3-phosphate dehydrogenase homolog in Borrelia burgdorferi and Borrelia hermsii. PubMed
LymphomaMolecular characterization of BCL6 breakpoints in primary diffuse large B-cell lymphomas of the central nervous system identifies GAPD as novel translocation partner. PubMed
Macular DegenerationStudies on the mechanism of early onset macular degeneration in cynomolgus (Macaca fascicularis) monkeys. I. Abnormal concentrations of two proteins in the retina. PubMed
Macular DegenerationStudies on the mechanism of early onset macular degeneration in cynomolgus monkeys. II. Suppression of metallothionein synthesis in the retina in oxidative stress. PubMed
MalariaCrystal structure of glyceraldehyde-3-phosphate dehydrogenase from Plasmodium falciparum at 2.25 A resolution reveals intriguing extra electron density in the active site. PubMed
MastitisCharacterization of two proteins of Staphylococcus aureus isolated from bovine clinical mastitis with homology to glyceraldehyde-3-phosphate dehydrogenase. PubMed
MelanomaGene expression profiling of melanocytic lesions. PubMed
MelanomaGlyceraldehyde-3-phosphate dehydrogenase expression is altered by hypoxia in melanoma cells and primary human melanocytes. PubMed
MelanomaRibosomal 18S RNA prevails over glyceraldehyde-3-phosphate dehydrogenase and beta-actin genes as internal standard for quantitative comparison of mRNA levels in invasive and noninvasive human melanoma cell subpopulations. PubMed
MelanomaSensitivity to extrinsically supplied interferon and the endogenous expression of interferon in melanoma cell lines. PubMed
MelanomaThe normalization of gene expression data in melanoma: investigating the use of glyceraldehyde 3-phosphate dehydrogenase and 18S ribosomal RNA as internal reference genes for quantitative real-time PCR. PubMed
MicrophthalmosBrachyury-related transcription factor Tbx2 and repression of the melanocyte-specific TRP-1 promoter. PubMed
Motor Neuron DiseaseEffects of gene therapy on muscle 18S rRNA expression in mouse model of ALS. PubMed
Multiple SclerosisInhibition of glyceraldehyde-3-phosphate dehydrogenase activity by antibodies present in the cerebrospinal fluid of patients with multiple sclerosis. PubMed
Muscular AtrophyProteomic analysis of muscle affected by motor neuron degeneration: The wobbler mouse model of amyotrophic lateral sclerosis. PubMed
Muscular DiseasesMetabolic myopathy produced by acute inhibition of glyceraldehyde-3-phosphate dehydrogenase with ortho-iodosobenzoic acid. PubMed
Muscular Disorders, AtrophicSpinocerebellar ataxia type-1 and spinobulbar muscular atrophy gene products interact with glyceraldehyde-3-phosphate dehydrogenase. PubMed
Myoclonic Epilepsies, ProgressiveGlyceraldehyde 3-phosphate dehydrogenase and endothelin-1 immunoreactivity is associated with cerebral white matter damage in dentatorubral-pallidoluysian atrophy. PubMed
Myoclonic Epilepsies, ProgressiveTissue transglutaminase-catalyzed formation of high-molecular-weight aggregates in vitro is favored with long polyglutamine domains: a possible mechanism contributing to CAG-triplet diseases. PubMed
Nasal PolypsExpression of neutrophil gelatinase-associated lipocalin in nasal polyps. PubMed
Neoplasm MetastasisPhosphoglycerate mutase-derived polypeptide inhibits glycolytic flux and induces cell growth arrest in tumor cell lines. PubMed
NeoplasmsA novel gene signature for molecular diagnosis of human prostate cancer by RT-qPCR. PubMed
NeoplasmsA reverse transcription-quantitative competitive polymerase chain reaction (RT-qcPCR) technique to measure cytokine gene expression in domestic mammals. PubMed
NeoplasmsAntisense oligodeoxynucleotide of glyceraldehyde-3-phosphate dehydrogenase gene inhibits cell proliferation and induces apoptosis in human cervical carcinoma cell lines. PubMed
NeoplasmsCancer abolishes the tissue type-specific differences in the phenotype of energetic metabolism. PubMed
NeoplasmsComparative proteomic analysis of esophageal squamous cell carcinoma. PubMed
NeoplasmsCorrelative histochemistry of some enzymes of carbohydrate metabolism in preneoplastic and neoplastic lesions in the rat liver. PubMed
NeoplasmsCytokine mRNA quantification in duodenal mucosa from dogs with chronic enteropathies by real-time reverse transcriptase polymerase chain reaction. PubMed
NeoplasmsCytokine profiles in eye muscle tissue and orbital fat tissue from patients with thyroid-associated ophthalmopathy. PubMed
NeoplasmsDecreased expression of cytochromes P450 1A2, 2E1, and 3A4 and drug transporters Na+-taurocholate-cotransporting polypeptide, organic cation transporter 1, and organic anion-transporting peptide-C correlates with the progression of liver fibrosis in chronic hepatitis C patients. PubMed
NeoplasmsDetection and quantitation of circulating cancer cells in the peripheral blood of lung cancer patients. PubMed
NeoplasmsDevelopment and validation of cytokine quantitative, real time RT-PCR assays for characterization of Asian elephant immune responses. PubMed
NeoplasmsDevelopment of a microarray for studying porcine cytokine production in blood mononuclear cells and intestinal biopsies. PubMed
NeoplasmsDifferential display and integrin alpha 6 messenger RNA overexpression in hepatocellular carcinoma. PubMed
NeoplasmsEnhanced gene expression in breast cancer cells in vitro and tumors in vivo. PubMed
NeoplasmsEnhancement of hammerhead ribozyme catalysis by glyceraldehyde-3-phosphate dehydrogenase. PubMed
NeoplasmsEnzyme activities at the surface of intact Ehrlich tumor cells with albumin in the isotonic assay medium. PubMed
NeoplasmsExpression of estrogen receptor (ER) subtypes and ERbeta isoforms in colon cancer. PubMed
NeoplasmsExpression of the pituitary transcription factor Ptx-1, but not that of the trans-activating factor prop-1, is reduced in human corticotroph adenomas and is associated with decreased alpha-subunit secretion. PubMed
NeoplasmsExpression of the smg p25A (a ras p21-like GTP-binding protein) gene in human neuroblastoma cell lines and tumor tissues. PubMed
NeoplasmsFunctional and molecular characterization of glioblastoma multiforme-derived cancer stem cells. PubMed
NeoplasmsGene expression profiles in thyroid carcinomas. PubMed
NeoplasmsGenes of glycolysis are ubiquitously overexpressed in 24 cancer classes. PubMed
NeoplasmsGlyceraldehyde 3-phosphate dehydrogenase depletion induces cell cycle arrest and resistance to antimetabolites in human carcinoma cell lines. PubMed
NeoplasmsGlyceraldehyde-3-phosphate dehydrogenase (GAPDH) induces cancer cell senescence by interacting with telomerase RNA component. PubMed
NeoplasmsGlyceraldehyde-3-phosphate dehydrogenase (GAPDH) is pyruvylated during 3-bromopyruvate mediated cancer cell death. PubMed
NeoplasmsGlyceraldehyde-3-phosphate dehydrogenase and other enzymatic activity in normal mouse lung and in lung tumors. PubMed
NeoplasmsGlyceraldehyde-3-phosphate dehydrogenase binds to the AU-Rich 3' untranslated region of colony-stimulating factor-1 (CSF-1) messenger RNA in human ovarian cancer cells: possible role in CSF-1 posttranscriptional regulation and tumor phenotype. PubMed
NeoplasmsGlyceraldehyde-3-phosphate dehydrogenase is a microtubule binding protein in a human colon tumor cell line. PubMed
NeoplasmsGlyceraldehyde-3-Phosphate Dehydrogenase: A Promising Target for Molecular Therapy in Hepatocellular Carcinoma. PubMed
NeoplasmsGlyceraldehyde-3-phosphate, a glycolytic intermediate, plays a key role in controlling cell fate via inhibition of caspase activity. PubMed
NeoplasmsHDM2-binding partners: interaction with translation elongation factor EF1alpha. PubMed
NeoplasmsHigh bad and bcl-xL gene expression and combined bad, bcl-xL, bax and bcl-2 mRNA levels: molecular predictors for survival of stage 2 soft tissue sarcoma patients. PubMed
NeoplasmsHigh level of ezrin mRNA expression in an osteosarcoma biopsy sample with lung metastasis. PubMed
NeoplasmsHuman hepatocellular carcinoma in a mouse model: assessment of tumor response to percutaneous ablation by using glyceraldehyde-3-phosphate dehydrogenase antagonists. PubMed
NeoplasmsIdentification of an additional hypoxia responsive element in the glyceraldehyde-3-phosphate dehydrogenase gene promoter. PubMed
NeoplasmsIdentification of underexpressed genes in early- and late-stage primary ovarian tumors by suppression subtraction hybridization. PubMed
NeoplasmsInactivation of glyceraldehyde-3-phosphate dehydrogenase of human malignant cells by methylglyoxal. PubMed
NeoplasmsIncreased glyceraldehyde-3-phosphate dehydrogenase gene expression in human cervical cancers. PubMed
NeoplasmsInteraction of calcyclin and its cyanogen bromide fragments with annexin II and glyceraldehyde 3-phosphate dehydrogenase. PubMed
NeoplasmsInvolvement of glyceraldehyde-3-phosphate dehydrogenase in tumor necrosis factor-related apoptosis-inducing ligand-mediated death of thyroid cancer cells. PubMed
NeoplasmsIsolation and characterization of complementary DNA clones corresponding to genes induced in mouse epidermis in vivo by tumor promoters. PubMed
NeoplasmsModulation of caspase-independent cell death leads to resensitization of imatinib mesylate-resistant cells. PubMed
NeoplasmsModulatory effect of mycobacterium cell wall extract (Regressin) on lymphocyte blastogenic activity and macrophage cytokine gene transcription in swine. PubMed
NeoplasmsMolecular characterization of tumor associated glyceraldehyde-3-phosphate dehydrogenase. PubMed
NeoplasmsMolecular diagnosis of sentinel lymph node metastases in cervical cancer using squamous cell carcinoma antigen. PubMed
NeoplasmsNovel insight into the role of GAPDH playing in tumor. PubMed
NeoplasmsOverexpression of osteopontin in hepatocellular carcinoma. PubMed
NeoplasmsPartial volume rat lung irradiation: Temporal fluctuations of in-field and out-of-field DNA damage and inflammatory cytokines following irradiation. PubMed
NeoplasmsPersistence of multiple tumor-specific T-cell clones is associated with complete tumor regression in a melanoma patient receiving adoptive cell transfer therapy. PubMed
NeoplasmsPhosphoglycerate mutase-derived polypeptide inhibits glycolytic flux and induces cell growth arrest in tumor cell lines. PubMed
NeoplasmsPotassium channel-blockers as therapeutic agents to interfere with bone resorption of periodontal disease. PubMed
NeoplasmsProperties of the glyceraldehyde-3-phosphate dehydrogenase from Ehrlich ascites tumor cells. PubMed
NeoplasmsProtein and gene expression of tumor-associated antigen RCAS1 in esophageal squamous cell carcinoma. PubMed
NeoplasmsQuantitation of O6-methylguanine-DNA methyltransferase gene messenger RNA in gliomas by means of real-time RT-PCR and clinical response to nitrosoureas. PubMed
NeoplasmsQuantitation of vascular endothelial growth factor mRNA levels in human breast tumors and metastatic lymph nodes. PubMed
NeoplasmsQuantitative real-time RT-PCR measurement of cytokine mRNA expression in the skin of normal cats and cats with allergic skin disease. PubMed
NeoplasmsRemoving the cells from adult bone marrow derived stem cell therapy does not eliminate cardioprotection. PubMed
NeoplasmsRetinoic acid receptors alpha, beta and gamma, and cellular retinol binding protein-I expression in breast fibrocystic disease and cancer. PubMed
NeoplasmsRole of endogenous nitric oxide in TNF-alpha and IL-1beta generation in hepatic ischemia-repefusion. PubMed
NeoplasmsSelection of candidate housekeeping controls in tomato plants using EST data. PubMed
NeoplasmsSolubilization of the plasmin receptor from human carcinoma cells. PubMed
NeoplasmsTelomerase RNA as a detection marker in the serum of breast cancer patients. PubMed
NeoplasmsThe prognostic value of tetranectin immunoreactivity and plasma tetranectin in patients with ovarian cancer. PubMed
NeoplasmsThioredoxin, a regulator of gene expression. PubMed
NeoplasmsTreatment of inflammatory bowel disease in a rodent model with the intestinal growth factor glucagon-like peptide-2. PubMed
NeoplasmsTwo-stage hepatectomy with effective perioperative chemotherapy does not induce tumor growth or growth factor expression in liver metastases from colorectal cancer. PubMed
NeoplasmsUpregulation of glyceraldehyde-3-phosphate dehydrogenase mRNA in the spleen of tumor-bearing mice. PubMed
Neoplasms[Proteomic analysis of morphine rabbit myocardium with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry] PubMed
Nephritis, HereditaryExpression of type IV c