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Information on EC 1.2.1.12 - glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and Organism(s) Arabidopsis thaliana

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IUBMB Comments
Also acts very slowly on D-glyceraldehyde and some other aldehydes; thiols can replace phosphate.
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Arabidopsis thaliana
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
gapdhs, d-glyceraldehyde-3-phosphate dehydrogenase, gapds, gadph, glyceraldehyde-3-phosphate dehydrogenases, plasmin receptor, gapc1, plasminogen-binding protein, gapcp, glyceraldehyde-3 phosphate dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-phosphoglyceraldehyde dehydrogenase
-
-
-
-
A4-glyceraldehyde-3-phosphate dehydrogenase
-
-
BARS-38
-
-
-
-
CP 17/CP 18
-
-
-
-
cytosolic NAD-dependent glyceraldehyde 3-P dehydrogenase
-
dehydrogenase, glyceraldehyde phosphate
-
-
-
-
dihydrogenase, glyceraldehyde phosphate
-
-
-
-
G3PD
-
-
-
-
GapB
-
resulting from the fusion of GapA with the C-terminal half of the regulatory peptide CP12
GapC1
GapC2
GAPDH
GAPDH1
-
-
-
-
GAPDH2
-
-
-
-
glyceraldehyde 3-phosphate dehydrogenase
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glyceraldehyde phosphate dehydrogenase (NAD)
-
-
-
-
glyceraldehyde-3-P-dehydrogenase
-
-
-
-
glyceraldehyde-3-phosphate dehydrogenase
glyceraldehyde-3-phosphate dehydrogenase (NAD)
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-
-
-
GPD
-
-
-
-
Gra3PDH
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-
-
-
GraP-DH
-
-
-
-
Larval antigen OVB95
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-
-
-
Major larval surface antigen
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-
-
-
NAD+-G-3-P dehydrogenase
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-
-
-
NAD-dependent glyceraldehyde phosphate dehydrogenase
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-
-
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NAD-dependent glyceraldehyde-3-phosphate dehydrogenase
NAD-G3PDH
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-
-
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NADH-glyceraldehyde phosphate dehydrogenase
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-
-
-
P-37
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-
-
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phosphoglyceraldehyde dehydrogenase
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-
-
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phosphorylating NAD+-dependent GAPDH
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Plasmin receptor
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-
-
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Plasminogen-binding protein
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-
-
-
plastidial glyceraldehyde-3-phosphate dehydrogenase
-
-
TLAb
-
-
-
-
triose phosphate dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating)
Also acts very slowly on D-glyceraldehyde and some other aldehydes; thiols can replace phosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-50-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-phospho-D-glyceroyl phosphate + NADH + H+
D-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
show the reaction diagram
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-phospho-D-glyceroyl phosphate + NADH + H+
D-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Diamide
-
1 mM
dithiothreitol
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DTT
glutathione
nitric oxide
isoform GAPC1 is irreversibly inhibited in a time- and concentration-dependent manner
oxidized glutathione
inactivation, 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 glutathionylated
S-nitrosoglutathione
inactivation, 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 dithiothreitol
Tyr-Asp
a proteogenic dipeptide Tyr-Asp acting as regulatory small molecule, which improves plant tolerance to oxidative stress by directly interfering with glucose metabolism. Tyr-Asp feeding induced a shift of glucose 6-phosphate (G6P) utilization from glycolysis to the pentose phosphate pathway (PPP), thereby altering redox equilibrium of the NADP(H) pool and improving tolerance to oxidative stress. 23% inhibition at 0.1 mM. Tyr-Asp treatment improves plant performance under stress conditions; a proteogenic dipeptide Tyr-Asp acting as regulatory small molecule, which improves plant tolerance to oxidative stress by directly interfering with glucose metabolism. Tyr-Asp feeding induced a shift of glucose 6-phosphate (G6P) utilization from glycolysis to the pentose phosphate pathway (PPP), thereby altering redox equilibrium of the NADP(H) pool and improving tolerance to oxidative stress. 23% inhibition at 0.1 mM. Tyr-Asp treatment improves plant performance under stress conditions
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additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
purified isozyme GapC1
33
purified GapC2 C159S mutant isozyme
60
purified isozyme GapC2
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.9
-
activity assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
activity assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
G3PC1_ARATH
338
0
36914
Swiss-Prot
other Location (Reliability: 4)
G3PP1_ARATH
422
0
44831
Swiss-Prot
Chloroplast (Reliability: 1)
G3PP2_ARATH
420
0
44846
Swiss-Prot
Chloroplast (Reliability: 2)
G3PC2_ARATH
338
0
36913
Swiss-Prot
other Location (Reliability: 4)
A0A168L4G8_ARATH
225
0
23993
TrEMBL
other Location (Reliability: 2)
Q56WJ4_ARATH
160
0
17309
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
-
tetramer, determined by gel filtration
36000
-
monomer, determined by SDS-PAGE
40000
x * 40000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 40000, SDS-PAGE
heteromer
-
GAPDH-AnBn heteromer of GapA and GapB subunits
homotetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glutathionylation
-
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C149S
C153S
C155S
nuclear relocalization of GAPC1 under cadmium-induced oxidative stress is stimulated, rather than inhibited, by mutation of the catalytic cysteine C155
C159S
the mutant C159S of the isozyme GapC2 shows decreased specific activity
additional information
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
isoform GapC1 is sensitive to oxidation by 0.05 mM H2O2, which appears to inhibit enzyme activity by converting the thiolate of Cys149 (S) into irreversible oxidized forms (SO2 and SO3) via a labile sulfenate intermediate (SO)
724236
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 restored
689409
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and Q-Sepharose column chromatography
native enzyme 142-175fold by ultracentrifugation, ammonium sulfate fractionation, hydrophobic interaction chromatography, ultrafiltration, and gel filtration
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purification protocol comprises two anion-exchange chromatographic steps and removing of the His tag
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)pLysS cells
for expression in Escherichia coli BL21DE
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gene gapc, targeted expression of plastidial glyceraldehyde-3-phosphate dehydrogenase (GAPCp) in a glyceraldehyde-3-phosphate dehydrogenase double mutant background gapcp1gapcp2
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into the pET28a vector for expression in Escherichia coli BL21DE3 cells, amplificatied in Escherichia coli HB101 cells
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recombinant expression of enzyme gapcp double mutants, gapcp1gapcp2, under the control of photosynthetic (Rubisco small subunit RBCS2B [RBCS]) or heterotrophic (phosphate transporter PHT1.2 [PHT]) cell-specific promoters. Expression of GAPCp1 under the control of RBCS in gapcp1gapcp2 has no significant effect on the metabolite profile or growth in the aerial part (AP). GAPCp1 expression under the control of the PHT promoter clearly affects Arabidopsis thaliana development by increasing the number of lateral roots and having a major effect on AP growth and metabolite profile. Recombinant expression of GFP-tagged isozyme GAPCp1 in Arabidopsis thaliana, quantitative real-time-PCR expression analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
72 h cadmium treatment has no stimulating effect on the extractable NADH-specific glyceraldehyde-3-phosphate dehydrogenase activity of whole seedlings
cadmium induces isoform GAPC1 accumulation in an inactive form. L-buthionine-sulfoximine induces both isoform GAPC1 promoter activity and protein accumulation in the seedling root tips
GAPDH transcript levels are greatly increased by H2O2 treatment
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isoform GAPC-1, expression is strong and ubiquitous, insensitive to dark treatments, and unaffected by sucrose
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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 leaves
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respiration, ATP levels, and the activity of NAD-dependent glyceraldehyde-3-phosphate dehydrogenase are enhanced in Arabidopsis thaliana grown in medium containing 0.1 mM selenium. Addition of an inhibitor of glutathione (GSH) synthesis to the medium abolishes both the Se-dependent growth promotion and enzyme NAD-GAPDH upregulation. Selenate-dependent variation in NAD-GAPDH levels
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
cadmium-induced stress in seedlings roots induces nitric oxide accumulation, cytosolic oxidation, activation of the GAPC1 promoter, GAPC1 protein accumulation in enzymatically inactive form, and strong relocalization of GAPC1 to the nucleus. All the effects are detected in the same zone of the root tip. In vitro, GAPC1 is inactivated by either nitric oxide donors or hydrogen peroxide, but no inhibition is directly provided by cadmium
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Marri, L.; Sparla, F.; Pupillo, P.; Trost, P.
Co-ordinated gene expression of photosynthetic glyceraldehyde-3-phosphate dehydrogenase, phosphoribulokinase, and CP12 in Arabidopsis thaliana
J. Exp. Bot.
56
73-80
2005
Arabidopsis thaliana
Manually annotated by BRENDA team
Marri, L.; Trost, P.; Pupillo, P.; Sparla, F.
Reconstitution and properties of the recombinant glyceraldehyde-3-phosphate dehydrogenase/CP12/phosphoribulokinase supramolecular complex of Arabidopsis
Plant Physiol.
139
1433-1443
2005
Arabidopsis thaliana
Manually annotated by BRENDA team
Zaffagnini, M.; Michelet, L.; Marchand, C.; Sparla, F.; Decottignies, P.; Le Marechal, P.; Miginiac-Maslow, M.; Noctor, G.; Trost, P.; Lemaire, S.D.
The thioredoxin-independent isoform of chloroplastic glyceraldehyde-3-phosphate dehydrogenase is selectively regulated by glutathionylation
FEBS J.
274
212-226
2007
Arabidopsis thaliana, Spinacia oleracea
Manually annotated by BRENDA team
Trost, P.; Fermani, S.; Marri, L.; Zaffagnini, M.; Falini, G.; Scagliarini, S.; Pupillo, P.; Sparla, F.
Thioredoxin-dependent regulation of photosynthetic glyceraldehyde-3-phosphate dehydrogenase: autonomous vs. CP12-dependent mechanisms
Photosynth. Res.
89
263-275
2006
Arabidopsis thaliana, Spinacia oleracea
Manually annotated by BRENDA team
Holtgrefe, S.; Gohlke, J.; Starmann, J.; Druce, S.; Klocke, S.; Altmann, B.; Wojtera, J.; Lindermayr, C.; Scheibe, R.
Regulation of plant cytosolic glyceraldehyde 3-phosphate dehydrogenase isoforms by thiol modifications
Physiol. Plant.
133
211-228
2008
Arabidopsis thaliana (P25858), Arabidopsis thaliana (Q56WJ4), Arabidopsis thaliana, Oryctolagus cuniculus, Saccharomyces cerevisiae, Spinacia oleracea
Manually annotated by BRENDA team
Baek, D.; Jin, Y.; Jeong, J.; Lee, H.; Moon, H.; Lee, J.; Shin, D.; Kang, C.; Kim, D.; Nam, J.; Lee, S.; Yun, D.
Suppression of reactive oxygen species by glyceraldehyde-3-phosphate dehydrogenase
Phytochemistry
69
333-338
2008
Arabidopsis thaliana
Manually annotated by BRENDA team
Rius, S.P.; Casati, P.; Iglesias, A.A.; Gomez-Casati, D.F.
Characterization of Arabidopsis lines deficient in GAPC-1, a cytosolic NAD-dependent glyceraldehyde-3-phosphate dehydrogenase
Plant Physiol.
148
1655-1667
2008
Arabidopsis thaliana
Manually annotated by BRENDA team
Munoz-Bertomeu, J.; Cascales-Minana, B.; Mulet, J.M.; Baroja-Fernandez, E.; Pozueta-Romero, J.; Kuhn, J.M.; Segura, J.; Ros, R.
Plastidial glyceraldehyde-3-phosphate dehydrogenase deficiency leads to altered root development and affects the sugar and amino acid balance in Arabidopsis
Plant Physiol.
151
541-558
2009
Arabidopsis thaliana (Q5E924), Arabidopsis thaliana (Q9SAJ6)
Manually annotated by BRENDA team
Bedhomme, M.; Adamo, M.; Marchand, C.H.; Couturier, J.; Rouhier, N.; Lemaire, S.D.; Zaffagnini, M.; Trost, P.
Glutathionylation of cytosolic glyceraldehyde-3-phosphate dehydrogenase from the model plant Arabidopsis thaliana is reversed by both glutaredoxins and thioredoxins in vitro
Biochem. J.
445
337-347
2012
Arabidopsis thaliana, Arabidopsis thaliana (P25858)
Manually annotated by BRENDA team
Vescovi, M.; Zaffagnini, M.; Festa, M.; Trost, P.; Lo Schiavo, F.; Costa, A.
Nuclear accumulation of cytosolic glyceraldehyde-3-phosphate dehydrogenase in cadmium-stressed Arabidopsis roots
Plant Physiol.
162
333-346
2013
Arabidopsis thaliana, Arabidopsis thaliana (P25858)
Manually annotated by BRENDA team
Guo, L.; Ma, F.; Wei, F.; Fanella, B.; Allen, D.; Wang, X.
Cytosolic phosphorylating glyceraldehyde-3-phosphate dehydrogenases affect Arabidopsis cellular metabolism and promote seed oil accumulation
Plant Cell
26
3023-3035
2014
Arabidopsis thaliana (P25858), Arabidopsis thaliana (Q9FX54), Arabidopsis thaliana
Manually annotated by BRENDA team
Takeda, T.; Fukui, Y.
Possible role of NAD-dependent glyceraldehyde-3-phosphate dehydrogenase in growth promotion of Arabidopsis seedlings by low levels of selenium
Biosci. Biotechnol. Biochem.
79
1579-1586
2015
Arabidopsis thaliana
Manually annotated by BRENDA team
Guo, L.; Ma, F.; Wei, F.; Fanella, B.; Allen, D.K.; Wang, X.
Cytosolic phosphorylating glyceraldehyde-3-phosphate dehydrogenases affect Arabidopsis cellular metabolism and promote seed oil accumulation
Plant Cell
26
3023-3035
2014
Arabidopsis thaliana (P25858), Arabidopsis thaliana (Q9FX54), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (P25858), Arabidopsis thaliana Col-0 (Q9FX54)
Manually annotated by BRENDA team
Anoman, A.D.; Munoz-Bertomeu, J.; Rosa-Tellez, S.; Flores-Tornero, M.; Serrano, R.; Bueso, E.; Fernie, A.R.; Segura, J.; Ros, R.
Plastidial glycolytic glyceraldehyde-3-phosphate dehydrogenase is an important determinant in the carbon and nitrogen metabolism of heterotrophic cells in Arabidopsis
Plant Physiol.
169
1619-1637
2015
Arabidopsis thaliana (Q5E924), Arabidopsis thaliana (Q9SAJ6)
Manually annotated by BRENDA team
Anoman, A.D.; Flores-Tornero, M.; Rosa-Tellez, S.; Munoz-Bertomeu, J.; Segura, J.; Ros, R.
The specific role of plastidial glycolysis in photosynthetic and heterotrophic cells under scrutiny through the study of glyceraldehyde-3-phosphate dehydrogenase
Plant Signal. Behav.
11
e1128614
2016
Arabidopsis thaliana
Manually annotated by BRENDA team
Moreno, J.C.; Rojas, B.E.; Vicente, R.; Gorka, M.; Matz, T.; Chodasiewicz, M.; Peralta-Ariza, J.S.; Zhang, Y.; Alseekh, S.; Childs, D.; Luzarowski, M.; Nikoloski, Z.; Zarivach, R.; Walther, D.; Hartman, M.D.; Figueroa, C.M.; Iglesias, A.A.; Fernie, A.R.; Skirycz, A.
Tyr-Asp inhibition of glyceraldehyde 3-phosphate dehydrogenase affects plant redox metabolism
EMBO J.
40
e106800
2021
Nicotiana tabacum (A0A0K2GN10), Nicotiana tabacum (A0A0K2GP10), Arabidopsis thaliana (P25858), Arabidopsis thaliana (Q9FX54)
Manually annotated by BRENDA team