Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.2.1.12 - glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and Organism(s) Oryctolagus cuniculus and UniProt Accession P46406

for references in articles please use BRENDA:EC1.2.1.12
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Also acts very slowly on D-glyceraldehyde and some other aldehydes; thiols can replace phosphate.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Oryctolagus cuniculus
UNIPROT: P46406
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Oryctolagus cuniculus
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
D-glyceraldehyde-3-phosphate dehydrogenase
-
glyceraldehyde-3-phosphate dehydrogenase
-
3-phosphoglyceraldehyde dehydrogenase
-
-
-
-
BARS-38
-
-
-
-
CP 17/CP 18
-
-
-
-
cytosolic NAD-dependent glyceraldehyde 3-P dehydrogenase
-
-
D-glyceraldehyde-3-phosphate dehydrogenase
-
-
dehydrogenase, glyceraldehyde phosphate
-
-
-
-
dihydrogenase, glyceraldehyde phosphate
-
-
-
-
G3PD
-
-
-
-
GAPD
-
somatic isoenzyme of glyceraldehyde-3-phosphate dehydrogenase
GAPDH
GAPDH1
-
-
-
-
GAPDH2
-
-
-
-
GAPDS
-
sperm-specific isoenzyme of glyceraldehyde-3-phosphate dehydrogenase
glyceraldehyde phosphate dehydrogenase (NAD)
-
-
-
-
glyceraldehyde-3-P-dehydrogenase
-
-
-
-
glyceraldehyde-3-phosphate dehydrogenase
-
-
glyceraldehyde-3-phosphate dehydrogenase (NAD)
-
-
-
-
GPD
-
-
-
-
Gra3PDH
-
-
-
-
GraP-DH
-
-
-
-
Larval antigen OVB95
-
-
-
-
Major larval surface antigen
-
-
-
-
NAD+-G-3-P dehydrogenase
-
-
-
-
NAD-dependent glyceraldehyde phosphate dehydrogenase
-
-
-
-
NAD-dependent glyceraldehyde-3-phosphate dehydrogenase
-
-
-
-
NAD-G3PDH
-
-
-
-
NADH-glyceraldehyde phosphate dehydrogenase
-
-
-
-
P-37
-
-
-
-
phosphoglyceraldehyde dehydrogenase
-
-
-
-
Plasmin receptor
-
-
-
-
Plasminogen-binding protein
-
-
-
-
TLAb
-
-
-
-
triose phosphate dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
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
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
-
-
-
?
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
show the reaction diagram
-
-
-
-
r
D-glyceraldehyde 3-phosphate + 3-acetylpyridine hypoxanthine nucleotide + phosphate
3-phospho-D-glyceroyl phosphate + ?
show the reaction diagram
-
3.2% of activity with NAD+
-
-
?
D-glyceraldehyde 3-phosphate + 3-acetylpyridine NAD+ + phosphate
3-phospho-D-glyceroyl phosphate + ?
show the reaction diagram
-
4.5% of activity with NAD+
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NAD+
3-phospho-D-glyceroyl arsenate + NADH
show the reaction diagram
D-glyceraldehyde 3-phosphate + N6-(2-carboxyethyl)-NAD+ + phosphate
3-phospho-D-glyceroyl phosphate + N6-(2-carboxyethyl)-NADH
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
-
-
-
-
?
D-glyceraldehyde 3-phosphate + poly(ethylene glycol)-bound NAD+ + phosphate
3-phospho-D-glyceroyl phosphate + poly(ethylene glycol)-bound NADH
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde 3-phosphate + thio-NAD+ + phosphate
3-phospho-D-glyceroyl phosphate + thio-NADH
show the reaction diagram
-
9.3% of activity with NAD+
-
-
?
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
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-acetylpyridine hypoxanthine nucleotide
-
3.2% of activity with NAD+
3-acetylpyridine-NAD+
-
4.5% of activity with NAD+ as cofactor
N6-(2-carboxyethyl)-NAD+
-
can replace NAD+ as cofactor
thio-NAD+
-
9.3% of activity with NAD+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide
-
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 manner
1-hydroxy-2-oxo-3,3-bis(2-aminoethyl)-1-triazene
-
-
Agaricic acid
-
0.14 mM, 50% inhibition in absence of NAD+. 2 mM, 35% loss of activity in presence of 0.017 mM NAD+
Fe2+
-
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 reactions
FK506-binding protein 36
-
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 GAPDH
-
fumarate
-
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 fumarate
glutathione
-
inactivation with 10 mM glutathione is reversible upon addition of 20 mM dithiothreitol
monoclonal antibody 8B7
-
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 tRNA
-
N-(phenoxyacetyl)-L-cysteine
N-(phenylacetyl)-glutathione
N-ethylmaleimide
-
1 mM completely inactivates the enzyme in 10 min
oxidized glutathione
-
inactivation, at least partially reversible upon addition of dithiothreitol
pentalenolactone
-
irreversible
pyridoxal 5'-phosphate
-
-
S-nitrosoglutathione
sodium nitroprusside
-
inhibition in presence of NAD+ is due primarily to active-site nitrosylation, covalent binding of NAD+ through a NO-dependent thiol intermediate
Trinitrobenzenesulfonic acid
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.158
3-acetyl-NAD+
-
-
1.43
3-acetylpyridine hypoxanthine nucleotide
-
-
0.13
3-phospho-D-glyceroyl phosphate
-
-
0.082 - 0.09
D-glyceraldehyde 3-phosphate
0.0674
N6-(2-carboxyethyl)-NAD+
-
-
0.013 - 0.06
NAD+
0.0033 - 0.012
NADH
0.0435
thio-NAD+
-
-
additional information
additional information
-
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 ones
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
-
purified enzyme
101
-
pH 8.9, 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
activity assay
8.9
-
activity assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
activity assay
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
100% thermoinactivation of GAPDH in the absence and in the presence of GroEL after 80 and 60 min, respectively, at 45°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
mechanism of NADH-channeling from D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) to L-lactate dehydrogenase (LDH). Enzyme kinetics studies show that LDH activity with free NADH and GAPDH-NADH complex always take place in parallel. The channeling is observed only in assays that mimic cytosolic conditions where free NADH concentration is negligible and the GAPDH-NADH complex is dominant. Molecular dynamics and protein-protein interaction studies show that LDH and GAPDH can form a leaky channeling complex only at the limiting NADH concentrations. Surface calculations show that positive electric field between the NAD(H) binding sites on LDH and GAPDH tetramers can merge in the LDH-GAPDH complex. NAD(H)-channeling within the LDH-GAPDH complex can be an extension of NAD(H)-channeling within each tetramer. In the case of a transient LDH-(GAPDH-NADH) complex, the relative contribution from the channeled and the diffusive paths depends on the overlap between the off-rates for the LDH-(GAPDH-NADH) complex and the GAPDH-NADH complex. The GAPDH complex can be observed in cell extracts, and with purified proteins in conditions that mimic high protein concentrations in cytosol
physiological function
apurinic/apyrimidinic (AP) sites are some of the most frequent DNA damages and the key intermediates of base excision repair. Certain proteins can interact with the deoxyribose of the AP site to form a Schiff base, which can be stabilized by NaBH4 treatment. The enzyme interacts with single-stranded AP DNA and AP DNA duplex with both 5' and 3' dangling ends. The protein forming this adduct is an isoform of glyceraldehyde-3-phosphate dehydrogenase called uracil-DNA glycosylase. GAPDH, at least partially, is covalently linked with the AP site by a mechanism other than the Schiff base formation. In spite of the ability to form a Schiff-base intermediate with the deoxyribose of the AP site, GAPDH does not display the AP lyase activity. In addition, along with the borohydride-dependent adducts with AP DNAs containing single-stranded regions, GAPDH was also shown to form the stable borohydride-independent crosslinks with these AP DNAs. GAPDH crosslinks preferentially to AP DNAs cleaves via the beta-elimination mechanism (spontaneously or by AP lyases) as compared to DNAs containing the intact AP site. The level of GAPDH–AP DNA adduct formation depends on oxidation of the protein SH-groups. Disulfide bond reduction in GAPDH leads to the loss of its ability to form the adducts with AP DNA
additional information
docking and molecular dynamics simulations of the interaction between rabbit muscle GAPDH and rabbit muscle or porcine heart LDH, structure analysis and calculation of the rm(ph)LDH-rmGAPDH complex, overview. Multiscale MD calculations and molecular docking studies showed that rmLDH and rmGAPDH can form a dynamic complex facing each other with their NAD(H) binding sites. The complex breaks apart when the two enzymes are saturated with NAD(H) molecules. The complex breaks apart when the two enzymes are saturated with NAD(H) molecules. When rmLDH and rmGAPDH form a complex, the positive cavities on the surface of each enzyme merge to form a central positive cavity under the protein surface. The cavity connects four NAD(H) binding sites with an average separation of 2.9 nm between the adjacent sites. Thus, NADH channeling within the rmLDH-rmGAPDH complex can be an extension of NADH channeling between the two adjacent monomers in rmLDH and rmGAPDH tetramers. Analysis of interaction between phLDH and byGAPDH by analytical ultracentrifugation, on velocity experiments for detection of interaction between phLDH and byGAPDH. It is a transient protein-protein interactions and NADH channeling in cells
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
G3P_RABIT
333
0
35780
Swiss-Prot
Mitochondrion (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
144000
36000
37000
-
x * 37000, SDS-PAGE
40000
-
SDS-PAGE
70000
-
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 Da
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 45000, SDS-PAGE, isozyme uracil-DNA glycosylase
?
-
x * 37000, SDS-PAGE
monomer
-
1 * 36000, SDS-PAGE
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
posttranslational modification of the enzyme with NADH is stimulated by thiols, possibly through superoxide, and is independent of NO
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C149S
-
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)
C149S/C281S
-
mutant shows a complete absence of aggregation in the presence of (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide
C153S
-
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 concentrations
C244A
-
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 concentrations
C281S
-
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-hexenamide
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
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 GAPDH
58
-
pH 7.0, 20 min, 50% inactivation
61.6
-
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)
66
-
melting temperature at 66°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
alpha-crystallin accelerates the thermal inactivation of GAPDH, while GroEL does not affect thermal inactivation and denaturation of GAPDH
-
freezing in liquid nitrogen results in partial loss of activity
-
OXIDATION STABILITY
ORGANISM
UNIPROT
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 restored
-
689409
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, crystalline suspension in 67% saturated ammonium sulfate containing EDTA, KCN, and dithioerythritol is stable for many months
-
5°C, stable for several months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity column chromatography and Sephadex G-100 gel filtration
-
ammonium sulfate precipitation and Q-Sepharose column chromatography
-
GAPDH is subjected to gel filtration on a Sephadex G-100 column
-
large-scale purification
-
Ni-NTA agarose resin chromatography and Hi-Load 16/60 Superdex gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain W3CG and in HeLa cells
-
expression in sf21 cell
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
GroEL-assisted reactivation after denaturation of GAPDH in the presence of guanidine hydrochloride
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
molecular evolution or metabolic engineering protocols can exploit substrate channeling of D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and L-lactate dehydrogenase (LDH) for metabolic flux control by fine-tuning substrate-binding affinity for the key enzymes in the competing reaction paths
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Scopes, R.K.; Stoter, A.
Purification of all glycolytic enzymes from one muscle extract
Methods Enzymol.
90
479-490
1982
Oryctolagus cuniculus
Manually annotated by BRENDA team
Lambeir, A.M.; Loiseau, A.M.; Kuntz, D.A.; Vellieux, F.M.; Michels, P.A.M.; Opperdoes, F.R.
The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic properties and comparison with homologous enzymes
Eur. J. Biochem.
198
429-435
1991
Geobacillus stearothermophilus, Oryctolagus cuniculus, Homo sapiens, Trypanosoma brucei
Manually annotated by BRENDA team
Canellas, P.F.; Cleland, W.W.
Carbon-13 and deuterium isotope effects on the reaction catalyzed by glyceraldehyde-3-phosphate dehydrogenase
Biochemistry
30
8871-8876
1991
Oryctolagus cuniculus
Manually annotated by BRENDA team
Katayama, N.; Hayakawa, K.; Urabe, I.; Okada, H.
Kinetic properties of N6-(2-carboxyethyl)-NAD(H) and poly(ethylene glycol)-bound NAD(H) for alcohol, lactate, malate and glyceraldehyde-3-phosphate dehydrogenase from different organisms
Enzyme Microb. Technol.
6
538-542
1984
Geobacillus stearothermophilus, Oryctolagus cuniculus, Thermus thermophilus
-
Manually annotated by BRENDA team
Scheek, R.M.; Slater, E.C.
Glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle
Methods Enzymol.
89
305-309
1982
Oryctolagus cuniculus
Manually annotated by BRENDA team
Dagher, S.M.; Deal, W.C.
Glyceraldehyde-3-phosphate dehydrogenase from pig liver
Methods Enzymol.
89
310-316
1982
Oryctolagus cuniculus, Sus scrofa
Manually annotated by BRENDA team
Harris, J.I.; Hocking, J.D.; Runswick, M.J.; Suzuki, K.; Walker, J.E.
D-glyceraldehyde-3-phosphate dehydrogenase. The purification and characterisation of the enzyme from the thermophiles Bacillus stearothermophilus and Thermus aquaticus
Eur. J. Biochem.
108
535-547
1980
Geobacillus stearothermophilus, Oryctolagus cuniculus, Thermus aquaticus
Manually annotated by BRENDA team
Ovadi, J.; Batke, J.; Bartha, F.; Keleti, T.
Effect of association-dissociation on the catalytic properties of glyceraldehyde 3-phosphate dehydrogenase
Arch. Biochem. Biophys.
193
28-33
1979
Oryctolagus cuniculus
Manually annotated by BRENDA team
Ghosh, S.; Mukherjee, K.; Ray, M.; Ray, S.
Identification 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
Eur. J. Biochem.
268
6037-6044
2001
Oryctolagus cuniculus, Mus musculus
Manually annotated by BRENDA team
Scheek, R.M.; Slater, E.C.
Preparation and properties of rabbit-muscle glyceraldehyde-phosphate dehydrogenase with equal binding parameters for the third and fourth NAD+ molecules
Biochim. Biophys. Acta
526
13-24
1978
Oryctolagus cuniculus
Manually annotated by BRENDA team
Rivera-Nieves, J.; Thompson, W.C.; Levine, R.L.; Moss, J.
Thiols mediate superoxide-dependent NADH modification of glyceraldehyde-3-phosphate dehydrogenase
J. Biol. Chem.
274
19525-19531
1999
Oryctolagus cuniculus
Manually annotated by BRENDA team
Harris, J.I.; Waters, M.
Glyceraldehyde-3-phosphate dehydrogenase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
13
1-49
1976
Geobacillus stearothermophilus, Bacillus cereus, Bos taurus, Saccharomyces cerevisiae, Canis lupus familiaris, Gallus gallus, Oryctolagus cuniculus, Escherichia coli, Felis catus, Hippoglossus sp., Homo sapiens, Lobster, Meleagris gallopavo, Pisum sativum, Rattus norvegicus, Acipenser sp., Sus scrofa, Thermus aquaticus
-
Manually annotated by BRENDA team
Amelunxen, R.E.; Carr, D.O.
Glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle-1
Methods Enzymol.
41
264-267
1975
Oryctolagus cuniculus
Manually annotated by BRENDA team
Hill, E.J.; Meriwether, B.P.; Harting Park, J.
Purification of rabbit muscle glyceraldehyde 3-phosphate dehydrogenase by gel filtration chromatography
Anal. Biochem.
63
175-182
1975
Oryctolagus cuniculus
Manually annotated by BRENDA team
Greene, F.C.; Feeney, R.E.
Properties of muscle glyceraldehyde-3-phosphate dehydrogenase from the cold-adapted antarctic fish Dissostichus mawsoni
Biochim. Biophys. Acta
220
430-442
1970
Oryctolagus cuniculus, Dissostichus mawsoni
Manually annotated by BRENDA team
McDonald, L.J.; Moss, J.
Stimulation by nitric oxide of an NAD linkage to glyceraldehyde-3-phosphate dehydrogenase
Proc. Natl. Acad. Sci. USA
90
6238-6241
1993
Oryctolagus cuniculus
Manually annotated by BRENDA team
Mann, K.H.; Mecke, D.
Inhibition of spinach glyceraldehyde-3-phosphate dehydrogenase by pentalenolactone
Nature
282
535-536
1979
Saccharomyces cerevisiae, Oryctolagus cuniculus, Spinacia oleracea
-
Manually annotated by BRENDA team
Cowan-Jacob, S.W.; Kaufmann, M.; Anselmo, A.N.; Stark, W.; Grutter, M.G.
Structure of rabbit-muscle glyceraldehyde-3-phosphate dehydrogenase
Acta Crystallogr. Sect. D
59
2218-2227
2003
Oryctolagus cuniculus
Manually annotated by BRENDA team
Arutyunova, E.I.; Danshina, P.V.; Domnina, L.V.; Pleten, A.P.; Muronetz, V.I.
Oxidation of glyceraldehyde-3-phosphate dehydrogenase enhances its binding to nucleic acids
Biochem. Biophys. Res. Commun.
307
547-552
2003
Oryctolagus cuniculus
Manually annotated by BRENDA team
Svedruzic, Z.M.; Spivey, H.O.
Interaction between mammalian glyceraldehyde-3-phosphate dehydrogenase and L-lactate dehydrogenase from heart and muscle
Proteins
63
501-511
2006
Cavia porcellus, Oryctolagus cuniculus
Manually annotated by BRENDA team
Naletova, I.N.; Muronetz, V.I.; Schmalhausen, E.V.
Unfolded, oxidized, and thermoinactivated forms of glyceraldehyde-3-phosphate dehydrogenase interact with the chaperonin GroEL in different ways
Biochim. Biophys. Acta
1764
831-838
2006
Oryctolagus cuniculus
Manually annotated by BRENDA team
Sojar, H.T.; Genco, R.J.
Identification of glyceraldehyde-3-phosphate dehydrogenase of epithelial cells as a second molecule that binds to Porphyromonas gingivalis fimbriae
FEMS Immunol. Med. Microbiol.
45
25-30
2005
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Kuravsky, M.L.; Muronetz, V.I.
Somatic and sperm-specific isoenzymes of glyceraldehyde-3-phosphate dehydrogenase: comparative analysis of primary structures and functional features
Biochemistry
72
744-749
2007
Bos taurus, Canis lupus familiaris, Homo sapiens, Mus musculus, Oryctolagus cuniculus
Manually annotated by BRENDA team
Shalova, I.N.; Cechalova, K.; Rehakova, Z.; Dimitrova, P.; Ognibene, E.; Caprioli, A.; Schmalhausen, E.V.; Muronetz, V.I.; Saso, L.
Decrease of dehydrogenase activity of cerebral glyceraldehyde-3-phosphate dehydrogenase in different animal models of Alzheimers disease
Biochim. Biophys. Acta
1770
826-832
2007
Oryctolagus cuniculus, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Khanova, H.A.; Markossian, K.A.; Kleimenov, S.Y.; Levitsky, D.I.; Chebotareva, N.A.; Golub, N.V.; Asryants, R.A.; Muronetz, V.I.; Saso, L.; Yudin, I.K.; Muranov, K.O.; Ostrovsky, M.A.; Kurganov, B.I.
Effect of alpha-crystallin on thermal denaturation and aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase
Biophys. Chem.
125
521-531
2007
Oryctolagus cuniculus
Manually annotated by BRENDA team
Blatnik, M.; Frizzell, N.; Thorpe, S.R.; Baynes, J.W.
Inactivation of glyceraldehyde-3-phosphate dehydrogenase by fumarate in diabetes: formation of S-(2-succinyl)cysteine, a novel chemical modification of protein and possible biomarker of mitochondrial stress
Diabetes
57
41-49
2008
Oryctolagus cuniculus, Rattus norvegicus
Manually annotated by BRENDA team
Hajdu, I.; Bothe, C.; Szilagyi, A.; Kardos, J.; Gal, P.; Zavodszky, P.
Adjustment of conformational flexibility of glyceraldehyde-3-phosphate dehydrogenase as a means of thermal adaptation and allosteric regulation
Eur. Biophys. J.
37
1139-1144
2008
Oryctolagus cuniculus, Thermotoga maritima
Manually annotated by BRENDA team
Schmalhausen, E.V.; Zhlobek, E.B.; Shalova, I.N.; Firuzi, O.; Saso, L.; Muronetz, V.I.
Antioxidant and prooxidant effects of quercetin on glyceraldehyde-3-phosphate dehydrogenase
Food Chem. Toxicol.
45
1988-1993
2007
Oryctolagus cuniculus
Manually annotated by BRENDA team
Nakajima, H.; Amano, W.; Fujita, A.; Fukuhara, A.; Azuma, Y.T.; Hata, F.; Inui, T.; Takeuchi, T.
The active site cysteine of the proapoptotic protein glyceraldehyde-3-phosphate dehydrogenase is essential in oxidative stress-induced aggregation and cell death
J. Biol. Chem.
282
26562-26574
2007
Oryctolagus cuniculus, Homo sapiens (P04406)
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
Van Meter, K.E.; Stuart, M.K.
A monoclonal antibody that inhibits translation in Sf21 cell lysates is specific for glyceraldehyde-3-phosphate dehydrogenase
Arch. Insect Biochem. Physiol.
69
107-117
2008
Oryctolagus cuniculus
Manually annotated by BRENDA team
Naletova, I.; Schmalhausen, E.; Kharitonov, A.; Katrukha, A.; Saso, L.; Caprioli, A.; Muronetz, V.
Non-native glyceraldehyde-3-phosphate dehydrogenase can be an intrinsic component of amyloid structures
Biochim. Biophys. Acta
1784
2052-2058
2008
Oryctolagus cuniculus
Manually annotated by BRENDA team
Jarczowski, F.; Jahreis, G.; Erdmann, F.; Schierhorn, A.; Fischer, G.; Edlich, F.
FKBP36 is an inherent multifunctional glyceraldehyde-3-phosphate dehydrogenase inhibitor
J. Biol. Chem.
284
766-773
2009
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Markossian, K.A.; Golub, N.V.; Chebotareva, N.A.; Asryants, R.A.; Naletova, I.N.; Muronetz, V.I.; Muranov, K.O.; Kurganov, B.I.
Comparative analysis of the effects of alpha-crystallin and GroEL on the kinetics of thermal aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase
Protein J.
29
11-25
2010
Oryctolagus cuniculus
Manually annotated by BRENDA team
Chernorizov, K.A.; Elkina, J.L.; Semenyuk, P.I.; Svedas, V.K.; Muronetz, V.I.
Novel inhibitors of glyceraldehyde-3-phosphate dehydrogenase: covalent modification of NAD-binding site by aromatic thiols
Biochemistry
75
1444-1449
2010
Oryctolagus cuniculus
Manually annotated by BRENDA team
Chernorizov, K.A.; Elkina, J.L.; Semenyuk, P.I.; Svedas, V.K.; Muronetz, V.I.
Novel inhibitors of glyceraldehyde-3-phosphate dehydrogenase: covalent modification of NAD-binding site by aromatic thiols
Biochemistry (Moscow)
75
1444-1449
2010
Oryctolagus cuniculus
Manually annotated by BRENDA team
Kosova, A.A.; Khodyreva, S.N.; Lavrik, O.I.
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) interacts with apurinic/apyrimidinic sites in DNA
Mutat. Res.
779
46-57
2015
Homo sapiens (P04406), Oryctolagus cuniculus (P46406)
Manually annotated by BRENDA team
Svedruzic, Z.M.; Odorcic, I.; Chang, C.H.; Svedruzic, D.
Substrate channeling via a transient protein-protein complex The case of D-glyceraldehyde-3-phosphate dehydrogenase and L-lactate dehydrogenase
Sci. Rep.
10
10404
2020
Oryctolagus cuniculus (P46406)
Manually annotated by BRENDA team