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Information on EC 1.2.1.12 - glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and Organism(s) Escherichia coli and UniProt Accession P0A9B2
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1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)IUBMB Comments
Also acts very slowly on D-glyceraldehyde and some other aldehydes; thiols can replace phosphate.
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Word Map
- 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
-
2.7.1.11
-
glyceraldehyde-phosphate
-
nephritogenic
-
4.1.2.13
- plr
-
2.7.2.3
-
endocapillary
- drug development
- agriculture
- biofuel production
- analysis
- synthesis
- biotechnology
- pharmacology
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-phosphoglyceraldehyde dehydrogenase
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-
-
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BARS-38
-
-
-
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CP 17/CP 18
-
-
-
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dehydrogenase, glyceraldehyde phosphate
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-
-
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dihydrogenase, glyceraldehyde phosphate
-
-
-
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G3PD
-
-
-
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GAPDH
GAPDH1
-
-
-
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GAPDH2
-
-
-
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glyceraldehyde phosphate dehydrogenase (NAD)
-
-
-
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glyceraldehyde-3-P-dehydrogenase
-
-
-
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glyceraldehyde-3-phosphate dehydrogenase (NAD)
-
-
-
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GPD
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-
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Gra3PDH
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-
-
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GraP-DH
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-
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Larval antigen OVB95
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-
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Major larval surface antigen
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-
-
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NAD+-G-3-P dehydrogenase
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-
-
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NAD-dependent glyceraldehyde phosphate dehydrogenase
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-
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NAD-dependent glyceraldehyde-3-phosphate dehydrogenase
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-
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NAD-G3PDH
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-
-
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NADH-glyceraldehyde phosphate dehydrogenase
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-
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P-37
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-
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phosphoglyceraldehyde dehydrogenase
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-
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Plasmin receptor
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Plasminogen-binding protein
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-
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TLAb
-
-
-
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triose phosphate dehydrogenase
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-
-
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GAPDH
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+
B-specific oxidoreductase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
-
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oxidation
-
-
-
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reduction
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-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -
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
9001-50-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
substrate binding structure analysis, overview
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
key enzyme of glycolysis
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
key enzyme of glycolysis
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
binding site and binding structure, detailed overview. The NAD+ binding domain consist of six parallel and one anti-parallel beta-strands, surrounded by four alpha-helices, the typical structure of a Rossmann fold
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
trehalose
might be an inhibitor, trehalose induces a conformational change in ecGAPDH in the current structure. The rotation of GAPDH also induced a conformational change in its active site. This suggests that the binding of trehalose to GAPDH induced a conformational change in its active site to prevent the binding of NAD+, although the NAD+- and trehalose-binding sites differ from one another
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 10.5
over 40% of maximal activity within this range, profile overview
7.5 - 8.5
-
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 buffer
8.3 - 9.3
-
85% of maximal activity at pH 8.3 and pH 9.3, 50 mM sodium diphosphate buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45 - 60
over 50% of maximal activity within this range, profile overview
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wild-type and mutant enzymes N313T, Y317A, Y317G and N313T/Y317G
UniProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
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
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
when the cell is exposed to high levels of H2O2, GAPDH is irreversibly inhibited presumably by the formation of sulphenic acid in the active site cysteine, becoming a switch that balances the equilibrium between the glycolytic cycle and the pentose phosphate metabolic pathway and promoting the formation of NADPH to combat ROS-produced cell stress
metabolism
physiological function
malfunction
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GAPDH-deficient cells are more sensitive to bleomycin or methyl methanesulfonate. In cells challenged with these genotoxic agents, GAPDH deficiency results in reduced cell viability and filamentous growth
metabolism
physiological function
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GAPDH is required for the efficient repair of DNA lesions in Escherichia coli. Interaction occur between GAPDH and enzymes of the base excision repair pathway, namely the AP-endonuclease Endo IV and uracil DNA glycosylase. GAPDH is a component of a protein complex dedicated to the maintenance of genomic DNA integrity. Interaction of GAPDH with the single-stranded DNA binding protein may recruit GAPDH to the repair sites and implicates GAPDH in DNA repair pathways activated by profuse DNA damage, such as homologous recombination or the SOS response.
additional information
metabolism
the EMP pathway can be controlled through the glyceraldehyde 3-phosphate node by NAD+-GAPDH activity, recombinant NADP+-GAPDH heterologous activity can also exert a similar response, which modulates the glucose uptake and also the acetic acid production rate
metabolism
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key enzyme in the glycolytic pathway that catalyzes the conversion of D-glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate
physiological function
apart from its glycolytic function, GAPDH displays a battery of moonlighting activities. Primary location of the tetrameric GAPDH is in the cytoplasm, where it conducts its canonical role in glycolysis
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) catalyses the conversion of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate using NAD+ as a cofactor. It is a moonlighting enzyme playing multiple roles in the regulation of mRNA stability, intracellular membrane trafficking, iron uptake and transport, DNA replication and repair, and nuclear RNA transport
physiological function
glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key enzyme in the glycolytic pathway that catalyzes the conversion of D-glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate
metabolism
-
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 strains
metabolism
-
GAPDH is a component of a multiprotein complex that repairs DNA lesions through the base excision repair pathway
additional information
each GAPDH monomer contains a molecule of glyceraldehyde-3 phosphate in a non-previously identified site. The catalytic Cys149 is covalently attached to an about 300 Da molecule, possibly glutathione. This modification alters the conformation of an adjacent alpha-helix in the catalytic domain, right opposite to the NAD+ binding site. The conformation of the alpha-helix is stabilized after soaking the crystals with NAD+. Enzyme structure analysis, structure modeling, detailed overview
additional information
the S-loop of GAPDH is required for interaction of the enzyme with its cofactor and with other proteins. NAD+-bound GAPDH S-loop fixation occurs by the formation of a complex with the coenzyme NAD+. The structure of trehalose-bound ecGAPDH is compared with the structures of both NAD+-free and NAD+-bound ecGAPDH. At the S-loop, the bound trehalose in the GAPDH structure induces a 2.4° rotation compared with the NAD+-free ecGAPDH structure and a 3.1° rotation compared with the NAD+-bound ecGAPDH structure
additional information
-
the S-loop of GAPDH is required for interaction of the enzyme with its cofactor and with other proteins. NAD+-bound GAPDH S-loop fixation occurs by the formation of a complex with the coenzyme NAD+. The structure of trehalose-bound ecGAPDH is compared with the structures of both NAD+-free and NAD+-bound ecGAPDH. At the S-loop, the bound trehalose in the GAPDH structure induces a 2.4° rotation compared with the NAD+-free ecGAPDH structure and a 3.1° rotation compared with the NAD+-bound ecGAPDH structure
additional information
three-dimensional structure analysis of EcGAPDH1 compared with the structures of HuGAPDH and MrsaGAPDH shows that the main difference is the loop conformation, especially the S-loop
additional information
-
three-dimensional structure analysis of EcGAPDH1 compared with the structures of HuGAPDH and MrsaGAPDH shows that the main difference is the loop conformation, especially the S-loop
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
-
x * 35000, high speed equilibrium sedimentation after treatment with 5 M guanidine hydrochloride containing 0.01 M dithiothreitol
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
?
-
x * 35000, high speed equilibrium sedimentation after treatment with 5 M guanidine hydrochloride containing 0.01 M dithiothreitol
tetramer
4 * 32400, engineered recombinant enzyme, SDS-PAGE, 4 * 35500, non-modified wild-type enzyme, SDS-PAGE
tetramer
each of the subunits can be divided into two domains: the N-terminal NAD+-binding domain and the C-terminal catalytic domain. The NAD+-binding domain is typically a Rossman fold containing eight beta-strands, namely beta1 (Lys3-Asn7), beta2 (Asp28-Asn33), beta3 (Val58-Phe60), beta4 (Ser64-Val67), beta5 (Lys70-Tyr75), beta6 (Ile92-Glu95), beta7 (Lys116-Ile119) and beta8 (Ile144-Ser146). The strands are connected by either helices or short loops. beta3 and beta5 are antiparallel to the other six parallel beta-strands. There are four alpha-helices in this domain: alpha1 (Gly10-Val23), alpha2 (Ser37-His47), alpha3 (Ser102-Ser106) and alpha4 (Gln107-Ala112). The catalytic domain contains eight mixed beta-sheets, beta9 (Ile168-Ala178), beta10 (Ile205-His207), beta11 (Leu226-Val231), beta12 (Ser239-Leu247), beta13 (Phe270-Thr273), beta14 (Ser289-Asp292), beta15 (Glu297-Val301) and beta16 (Leu304-Tyr313), and three long alpha-helices, alpha5 (Ser149-Gly167), alpha6 (Thr252-Thr264) and alpha7 (Gln317-Lys332). The catalytically active residues Cys150 and His177 are situated in alpha5 and beta9, respectively
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
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+
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native, non-modified and selenium-modified enzymes, 5.5 mg/ml protein in 10 mM HEPES, pH 7.5, and 1.43 M sodium citrate, 18°C, 3 days, method optimization, crystals from the selenium modified enzyme are soaked for 10 min in 5 mM NAD+ dissolved in mother liquor with or without 25% trehalose, X-ray diffraction structure determination and analysis at 1.64-2.14 A resolution using single-wavelength anomalous dispersion (SAD) phasing with a selenium-modified enzyme, molecular replacement
purified recombinant enzyme GAPDH complexed with trehalose, hanging drop vapour diffusion method, mixing of 20 mg/ml protein in 20 mM Tris, 130 mM NaCl pH 7.5, with reservoir solution containing 2.8 M ammonium sulfate, 0.1 M MES, pH 5.5-6.5, 4°C, two to three weeks, GAPDH crystals are treated with a cryoprotectant consisting of 15% v/v trehalose at -173°C, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement using the Escherichia coli GAPDH structure (PDB ID 1s7c) as a starting model
purified recombinant isozyme EcGAPDH1, sitting drop vapour diffusion method, mixing of 240 nl of 30 mg/ml protein in 4 mM NaCl, and 5 mM Tris-HCl pH 8.0, with 240 nl of reservoir solution containing reservoir solution consisting of 100 mM sodium acetate, pH 4.6, 30% w/v PEG 400,and 200 mM calcium acetate, and equilibration against 0.1 ml of reservoir solution, 1 week, method optimization, X-ray diffraction structure determination and analysis at 1.88 A resolution, molecular replacement using the structure of GAPDH from methicillin-resistant Staphylococcus aureus MRSA252 (PDB ID 3lvf) as search model, model building
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 NAD
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N313T/Y317G
dissociation 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 conformer
Y317A
dissociation constant for NAD+ is 5times higher than that of the wild-type enzyme. Wild-type syn orientation of bound nicotinamide remains unchanged
Y317G
dissociation constant for NAD+ is 13times higher than that of the wild-type enzyme. Wild-type syn orientation of bound nicotinamide remains unchanged
C149A
additional information
additional information
the gapA gene from Escherichia coli strain MG1655 is replaced by the gene gapN from Streptococcus mutans, EC 1.2.1.9, UniProt ID Q59931. The specific NADP+-GAPDH activity of the strain MG1655DgapA::gapN is 4.6times lower relative to strain MG1655DELTAgapA::gapN/pTrcgapN and no NAD+-GAPDH activity is detected. The specific NADP+-GAPDH activity levels in the derivative strain reveal that growth rate and glucose uptake differences are attributable to gapN expression level. The NADH/NAD+ ratio in the strain MG1655DELTAgapA::gapN/pTrcgapN decreases by 25% as compared to wild-type strain. In contrast, the NADPH/NADP+ ratio increases 2times indicating that the alteration in the turnover of NAD(P)H via glyceraldehyde 3-phosphate oxidation affects the redox levels of the strain MG1655DELTAgapA::gapN/pTrcgapN, which increases 2.8times the NADPH/NADH ratio
additional information
generation of an engineered synthetic Escherichia coli codon optimized sequence of a human gene that codifies for a 32.4 kDa protein for recombinant expression
additional information
-
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 strains
additional information
-
construction of a gapA-deficient strain MC4100 DELTAgapA
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged engineered enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, gel filtration, and ultrafiltratioon
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene gapA, complementation of the mutant Escherichia coli strain MG1655DELTAgapA by the Streptococcus mutans gapN gene, EC 1.2.1.9, UniProt ID Q59931, expressed from plasmid pTrcgapN
gene gapA, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene gapA, recombinant expression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene gapA, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene gapA, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Eyschen, J.; Vitoux, B.; Marraud, M.; Cung, M.T.; Branlant, G.
Engineered glycolytic glyceraldehyde-3-phosphate dehydrogenase binds the anti conformation of NAD+ nicotinamide but does not experience A-specific hydride transfer
Arch. Biochem. Biophys.
364
219-227
1999
Escherichia coli (P0A9B2), Escherichia coli
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
-
D'Alessio, G.; Josse, J.
Glyceraldehyde phosphate dehydrogenase of Escherichia coli. Structural and catalytic properties
J. Biol. Chem.
246
4326-4333
1971
Escherichia coli
Olivier, L.; Buisson, G.; Fanchon, E.; Corbier, C.; Branlant, G.; Dideberg, O.
Crystallization and preliminary x-ray diffraction studies of Escherichia coli glyceraldehyde-3-phosphate dehydrogenase
Acta Crystallogr. Sect. D
51
245-247
1995
Escherichia coli
Egea, L.; Aguilera, L.; Gimenez, R.; Sorolla, M.A.; Aguilar, J.; Badia, J.; Baldoma, L.
Role 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
Int. J. Biochem. Cell Biol.
39
1190-1203
2007
Escherichia coli
Aguilera, L.; Gimenez, R.; Badia, J.; Aguilar, J.; Baldoma, L.
NAD+-dependent post-translational modification of Escherichia coli glyceraldehyde-3-phosphate dehydrogenase
Int. Microbiol.
12
187-192
2009
Escherichia coli
Frayne, J.; Taylor, A.; Cameron, G.; Hadfield, A.T.
Structure of insoluble rat sperm glyceraldehyde-3-phosphate dehydrogenase (GAPDH) via heterotetramer formation with Escherichia coli GAPDH reveals target for contraceptive design
J. Biol. Chem.
284
22703-22712
2009
Escherichia coli (P0A9B2), Escherichia coli, Rattus norvegicus (Q9ESV6)
Martinez, I.; Zhu, J.; Lin, H.; Bennett, G.N.; San, K.Y.
Replacing Escherichia coli NAD-dependent glyceraldehyde 3-phosphate dehydrogenase (GAPDH) with a NADP-dependent enzyme from Clostridium acetobutylicum facilitates NADPH dependent pathways
Metab. Eng.
10
352-359
2008
Escherichia coli
Centeno-Leija, S.; Utrilla, J.; Flores, N.; Rodriguez, A.; Gosset, G.; Martinez, A.
Metabolic and transcriptional response of Escherichia coli with a NADP+-dependent glyceraldehyde 3-phosphate dehydrogenase from Streptococcus mutans
Antonie van Leeuwenhoek
104
913-924
2013
Escherichia coli (P0A9B2)
Ferreira, E.; Gimenez, R.; Canas, M.A.; Aguilera, L.; Aguilar, J.; Badia, J.; Baldoma, L.
Glyceraldehyde-3-phosphate dehydrogenase is required for efficient repair of cytotoxic DNA lesions in Escherichia coli
Int. J. Biochem. Cell Biol.
60
202-212
2015
Escherichia coli
Kim, Y.J.
A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase
Acta Crystallogr. Sect. F
74
277-282
2018
Escherichia coli (P0A9B2), Escherichia coli
Zhang, L.; Liu, M.; Yao, Y.; Bostrom, I.; Wang, Y.; Chen, A.; Li, J.; Gu, S.; Ji, C.
Characterization and structure of glyceraldehyde-3-phosphate dehydrogenase type 1 from Escherichia coli
Acta Crystallogr. Sect. F
76
406-413
2020
Escherichia coli (P0A9B2), Escherichia coli
Rodriguez-Hernandez, A.; Romo-Arevalo, E.; Rodriguez-Romero, A.
A novel substrate-binding site in the X-ray structure of an oxidized E. coli glyceraldehyde 3-phosphate dehydrogenase elucidated by single-wavelength anomalous dispersion
Crystals
9
622
2019
Escherichia coli (P0A9B2)
-
EXTERNAL LINKS (specific for EC-Number 1.2.1.12)
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