1.2.1.12: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
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For detailed information about glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), go to the full flat file.
Word Map on EC 1.2.1.12
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1.2.1.12
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tetramer
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chloroplast
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gapcs
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streptococcal
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stearothermophilus
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glomerulonephritis
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nadp-dependent
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genorm
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normfinder
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medicine
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3-phosphoglycerate
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phosphofructokinase
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flagellum
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poststreptococcal
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1,3-bisphosphoglycerate
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bestkeeper
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lobster
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glycosomal
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2.7.1.11
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glyceraldehyde-phosphate
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nephritogenic
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4.1.2.13
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plr
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2.7.2.3
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endocapillary
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drug development
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agriculture
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biofuel production
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analysis
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synthesis
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biotechnology
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pharmacology
- 1.2.1.12
- tetramer
- chloroplast
-
gapcs
- streptococcal
- stearothermophilus
- glomerulonephritis
-
nadp-dependent
-
genorm
-
normfinder
- medicine
- 3-phosphoglycerate
-
phosphofructokinase
- flagellum
-
poststreptococcal
- 1,3-bisphosphoglycerate
-
bestkeeper
- lobster
- glycosomal
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2.7.1.11
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glyceraldehyde-phosphate
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nephritogenic
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4.1.2.13
- plr
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2.7.2.3
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endocapillary
- drug development
- agriculture
- biofuel production
- analysis
- synthesis
- biotechnology
- pharmacology
Reaction
Synonyms
3-phosphoglyceraldehyde dehydrogenase, A4-GAPDH, A4-glyceraldehyde-3-phosphate dehydrogenase, AB-GAPDH, AnBn-GAPDH, AsGAPDH, At3g04120, BARS-38, CbbG, CgGAP, Clo1313_2095, complement-C3-binding protein, CP 17/CP 18, Ctherm_Gapdh, cytosolic NAD-dependent glyceraldehyde 3-P dehydrogenase, cytosolic phosphorylating glyceraldehyde-3-phosphate dehydrogenase, D-glyceraldehyde-3-phosphate dehydrogenase, D-glyceraldehyde-3-phosphate: NAD+ oxidoreductase (phosphorylating), dehydrogenase, glyceraldehyde phosphate, dihydrogenase, glyceraldehyde phosphate, EcGAPDH, EcGAPDH1, FgGAPDH, FhGAPDH, G3PD, G3PDH, Ga3P dehydrogenase, Ga3PDHase, GADPH, GAP, GAP1, gap2, GapA, GapB, GAPC, GapC-1, GapC1, GapC2, GAPCp, GAPCp1, GAPCp2, GAPD, GAPDH, GAPDH type 1, GAPDH1, GAPDH2, GAPDH3, GAPDHS, GAPDS, GAPN, GBS GAPDH, glyceraldehyde 3-phosphate dehydrogenase, glyceraldehyde 3-phosphate dehydrogenase-S, glyceraldehyde phosphate dehydrogenase (NAD), glyceraldehyde-3 phosphate dehydrogenase, glyceraldehyde-3-P-dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase (NAD), glyceraldehyde-3-phosphate dehydrogenase 1, glyceraldehyde-3-phosphate dehydrogenase, type I, glyceraldehyde-3-phosphate dehydrogenase-spermatogenic protein, glyceraldehyde-3-phosphate dehydrogenase-spermatogenic protein GAPDHS, glyceraldehyde-3-phosphate dehydrogenases, GPD, GPD2, Gra3PDH, GraP-DH, H.c-C3BP, hGAPDH, HsGAPDH, kmGAPDH1p, Larval antigen OVB95, Major larval surface antigen, Mtb-GAPDH, NAD+-dependent GAPDH, NAD+-dependent glyceraldehyde 3-phosphate dehydrogenase, NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase, NAD+-G-3-P dehydrogenase, NAD+-GAPDH, NAD-dependent Ga3PDHase, NAD-dependent glyceraldehyde 3-phosphate dehydrogenase, NAD-dependent glyceraldehyde phosphate dehydrogenase, NAD-dependent glyceraldehyde-3-phosphate dehydrogenase, NAD-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase, NAD-dependent phosphorylating glyceraldehyde-3-phosphate dehydrogenase, NAD-G3PDH, NAD-GAPDH, NADH-glyceraldehyde phosphate dehydrogenase, P-37, p-GAPDH, PfGAPDH, phosphoglyceraldehyde dehydrogenase, phosphorylating NAD+-dependent GAPDH, Plasmin receptor, Plasminogen-binding protein, plastidial glyceraldehyde-3-phosphate dehydrogenase, pmGAPDH, PyGapdh, rmGAPDH, Rv1436, somatic GAPD, somatic glyceraldehyde 3-phosphate dehydrogenase, sperm-specific GAPDS, sperm-specific glyceraldehyde 3-phosphate dehydrogenase, sperm-specific glyceraldehyde-3-phosphate dehydrogenase, TaeNAD-GAPDH, TagapC, TDH1, TDH2, TDH3, TLAb, triose phosphate dehydrogenase, UDG, uracil-DNA glycosylase, vGPD
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1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)Advanced search results
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Application on EC 1.2.1.12 - glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
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
analysis
GAPDH is a multi-functional protein that is used as a control marker for basal function, it is known to undergo cysteine oxidation under different types of cellular stress
biofuel production
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proteome analysis as well as enzyme assays performed in cell-free extracts demonstrates that glycerol is degraded via glyceraldehyde-3-phosphate, which is further metabolized through the lower part of glycolysis leading to formation of mainly ethanol and hydrogen. Fermentation of glycerol to ethanol and hydrogen by this bacterium represents a remarkable option to add value to the biodiesel industries by utilization of surplus glycerol
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
drug development
medicine
pharmacology
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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 antigen
synthesis
additional information
drug development
as an essential enzyme for the survival of GBS, GAPDH may be a potential target for developing antibacterial drugs
drug development
development of GAPDH inhibitors as anti-cancer and anti-parasitic agents
drug development
Gapdh can be an effective target for anti-malarial chemotherapeutics
drug development
Gapdh can be an effective target for anti-malarial chemotherapeutics. Enzyme PfGapdh shows an extra ligand binding capacity in the vicinity of the NAD+ binding region of the active site that may offer an opportunity to design and develop novel antimalarials
drug development
the conformation of FgGAPDH in this region is similar to the human enzyme. Therefore, GAPDH may not be a suitable target for drug discovery against fascioliasis caused by Fasciola gigantica
drug development
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Gapdh can be an effective target for anti-malarial chemotherapeutics
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medicine
crystallography may provide structural detail for the development of lead compounds and drug design of novel antimalarials
medicine
functions are of chemotherapeutic interest, structure is a necessity for structure-based drug design
medicine
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pathogenesis of Porphyromonas gingivalis involves interaction with oral mucosal epithelial cells, mediated by binding glyceraldehyde-3-phosphate dehydrogenase
medicine
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pathogenesis of Porphyromonas gingivalis involves interaction with oral mucosal epithelial cells, mediated by binding glyceraldehyde-3-phosphate dehydrogenase
medicine
the pathogenic fungus causes paracoccidioidomycosis, GAPDH is reported as an adhesin, which can be related to fungus adhesion and invasion
medicine
the Plr-SDH-GAPDH complex participates in invasive streptococcal infections
medicine
G3PDH is a potential target for antimalarial drug development
medicine
G3PDH is a potential target for antimalarial drug development
medicine
G3PDH is a potential target for antimalarial drug development
medicine
G3PDH is a potential target for antimalarial drug development
medicine
G3PDH is a potential target for antimalarial drug development
medicine
G3PDH is a potential target for antimalarial drug development
medicine
G3PDH is a potential target for antimalarial drug development
medicine
G3PDH is a potential target for antimalarial drug development
medicine
G3PDH is a potential target for antimalarial drug development
medicine
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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 score
medicine
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glyceraldehyde 3-phosphate dehydrogenase from malignant sources shows altered properties compared with enzyme from healthy subjects
medicine
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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 antigen
medicine
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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 enzyme
medicine
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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 encephalomyelitis
medicine
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non-native forms of GAPDH may be involved in the formation of amyloid structures during Alzheimer's disease, binding to soluble amyloid-beta peptide
medicine
the Porphyromonas gingivalis client proteins tonB-dependent receptor protein RagA4, 4-hydroxybutyryl-coenzyme A dehydratase AbfD, GAPDH, NAD-dependent glutamate dehydrogenase GDH, and malate dehydrogenase MDH function as regulators in Porphyromonas gingivalis biofilm formation with oral streptococci
medicine
GAPDHS, which is regulated by SOX10, controls glycolysis and contributes to uveal melanoma tumorigenesis, is a therapeutic target in cancer therapy
medicine
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G3PDH is a potential target for antimalarial drug development
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medicine
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G3PDH is a potential target for antimalarial drug development
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medicine
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G3PDH is a potential target for antimalarial drug development
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medicine
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G3PDH is a potential target for antimalarial drug development
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medicine
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G3PDH is a potential target for antimalarial drug development
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medicine
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G3PDH is a potential target for antimalarial drug development
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medicine
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G3PDH is a potential target for antimalarial drug development
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synthesis
generation of a de novo NADPH generation pathway by altering the coenzyme specificity of native NAD-dependent glyceraldehyde 3-phosphate dehydrogenase (GAPDH) to NADP, to produce additional NADPH in the glycolytic pathway. Increasing the catalytic efficiency of GAPDH towards NADP enhances lysine production in all of the tested mutants, the most significant improvement of lysine production (60%) is achieved with the mutant showing similar preference towards both NAD and NADP. There is no significant change of flux towards the pentose phosphate pathway and the increased lysine yield is mainly attributed to the NADPH generated by the mutated GAPDH
synthesis
engineering the coenzyme specificity of (GAPDH) as a promising NADPH source is of interest for the metabolic engineering of NADPH-dependent bioproduction systems, e.g. for lysine production
synthesis
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engineering the coenzyme specificity of (GAPDH) as a promising NADPH source is of interest for the metabolic engineering of NADPH-dependent bioproduction systems, e.g. for lysine production
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synthesis
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engineering the coenzyme specificity of (GAPDH) as a promising NADPH source is of interest for the metabolic engineering of NADPH-dependent bioproduction systems, e.g. for lysine production
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synthesis
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generation of a de novo NADPH generation pathway by altering the coenzyme specificity of native NAD-dependent glyceraldehyde 3-phosphate dehydrogenase (GAPDH) to NADP, to produce additional NADPH in the glycolytic pathway. Increasing the catalytic efficiency of GAPDH towards NADP enhances lysine production in all of the tested mutants, the most significant improvement of lysine production (60%) is achieved with the mutant showing similar preference towards both NAD and NADP. There is no significant change of flux towards the pentose phosphate pathway and the increased lysine yield is mainly attributed to the NADPH generated by the mutated GAPDH
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additional information
selective inhibition of GAPDHS, one of the glycolytic isozymes with restricted expression during spermatogenesis, is a potential strategy for the development of a non-hormonal contraceptive that directly blocks sperm function. Detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme can facilitate the identification of selective GAPDHS inhibitors for contraceptive development
additional information
selective inhibition of GAPDHS, one of the glycolytic isozymes with restricted expression during spermatogenesis, is a potential strategy for the development of a non-hormonal contraceptive that directly blocks sperm function. Detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme can facilitate the identification of selective GAPDHS inhibitors for contraceptive development
additional information
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selective inhibition of GAPDHS, one of the glycolytic isozymes with restricted expression during spermatogenesis, is a potential strategy for the development of a non-hormonal contraceptive that directly blocks sperm function. Detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme can facilitate the identification of selective GAPDHS inhibitors for contraceptive development
