Information on EC 1.2.1.59 - glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
1.2.1.59
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RECOMMENDED NAME
GeneOntology No.
glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+ = 3-phospho-D-glyceroyl phosphate + NAD(P)H + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
photosynthesis
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Glycolysis / Gluconeogenesis
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Carbon fixation in photosynthetic organisms
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde 3-phosphate:NAD(P)+ oxidoreductase (phosphorylating)
NAD+ and NADP+ can be used as cofactors with similar efficiency, unlike EC 1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and EC 1.2.1.13 glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating), which are NAD+- and NADP+-dependent, respectively.
CAS REGISTRY NUMBER
COMMENTARY hide
39369-25-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
isoform GapA-1, EC 1.2.1.13
SwissProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
strain PCC 7601
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Manually annotated by BRENDA team
containing the point mutation Q298G in the lysC gene and mutation N917G in the ppc gene
UniProt
Manually annotated by BRENDA team
containing the point mutation Q298G in the lysC gene and mutation N917G in the ppc gene
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain PCC 7107
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain PCC 7437
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
strain PCC 7942
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Manually annotated by BRENDA team
strain PCC 6803
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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 + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
show the reaction diagram
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
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 + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
show the reaction diagram
D-glyceraldehyde-3-phosphate + phosphate + NAD(P)+
1,3-diphosphoglycerate + NAD(P)H
show the reaction diagram
D-glyceraldehyde-3-phosphate + phosphate + NADP+
1,3-diphosphoglycerate + NADPH
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
show the reaction diagram
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
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 + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
show the reaction diagram
additional information
?
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possible amphibolic role: anabolic in photosynthetic carbon assimilation and catabolic in carbohydrate degradative pathways
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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activates NADP+-dependent activity, inhibits NAD+-dependent activity
NADP+
additional information
GAPDH catalyzes the oxidative phosphorylation of D-glyceraldehyde 3-phosphate using NAD+ or NADP+ as a cofactor
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-phospho-D-glyceroyl phosphate
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ATP
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activates NADP+-dependent activity, inhibits NAD+-dependent activity
D-glyceraldehyde 3-phosphate
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additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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enhances activity
2-mercaptopropanol
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enhances activity
dithiothreitol
glutathione
lipoic acid
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enhances activity
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.8
3-phospho-D-glyceroyl phosphate
pH 8.0, 60°C
0.21 - 0.77
D-glyceraldehyde 3-phosphate
0.03
NAD(P)+
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0.058 - 16.8
NAD+
0.01
NADH
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0.003 - 1.46
NADP+
0.002 - 0.18
NADPH
107
phosphate
pH 8.0, 60°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.45 - 6.37
NAD+
1.58 - 8
NADP+
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.94 - 49.48
NAD+
1.08 - 101.86
NADP+
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
49.1
3-phospho-D-glyceroyl phosphate
pH 8.0, 60°C
2.8 - 13.1
D-glyceraldehyde 3-phosphate
10.7
NAD+
pH 8.0, 60°C
0.75
NADP+
pH 8.0, 60°C
0.035 - 0.081
NADPH
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
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considerable activity in the range of pH 7 to pH 10
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expression of isoforms GapA-1, GapB and phosphoribulokinase and peptide Cp12-2 is co-ordinately regulated with the same organ specificity, all four genes being mostly expressed in leaf and flower stalk, less expressed in flower, and little or not expressed in roots and siliques. Expression in leaf is terminated during prolonged darkness or following sucrose treatment, and their transcripts decay with similar kinetics
Manually annotated by BRENDA team
expression of isoforms GapA-1, GapB and phosphoribulokinase and peptide Cp12-2 is co-ordinately regulated with the same organ specificity, all four genes being mostly expressed in leaf and flower stalk, less expressed in flower, and little or not expressed in roots and siliques. Expression in leaf is terminated during prolonged darkness or following sucrose treatment, and their transcripts decay with similar kinetics
Manually annotated by BRENDA team
additional information
expression of isoforms GapA-1, GapB and phosphoribulokinase and peptide Cp12-2 is co-ordinately regulated with the same organ specificity, all four genes being mostly expressed in leaf and flower stalk, less expressed in flower, and little or not expressed in roots and siliques. Expression in leaf is terminated during prolonged darkness or following sucrose treatment, and their transcripts decay with similar kinetics
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
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4 * 45000, SDS-PAGE
142000
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FPLC gel filtration
160000
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FPLC gel filtration
200000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild type and mutant enzyme C150S, sitting drop vapor diffusion method, using 25% (w/v) PEG 1K, 175 mM sodium/potassium tartrate and 100 mM sodium acetate pH 4.5
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crystal structure is determined to 1.81 A resolution. The crystal belongs to space group C222(1), with unit-cell parameters a = 83.4, b = 152.0, c = 118.6 A. Crystallization is performed using the microbatch-under-oil method at 18°C
purified His-tagged enzyme in complex with NAD+, microseeding method, mixing of 8.9 mg/ml protein in 25 mM HEPES, pH 7.35, 0.1 M NaCl, and 5 mM 2-mercaptoethanol, with crystallization solution containing 26-36% PEG 4000, 0.1 M MES, pH 6.5, the needle-like crystals are used for microseeding by mixing 0.002 ml of protein plus cofactor mixture, 500 nl water and 500 nl reservoir solution containing seed suspension in 28% PEG 4000, 0.1 M MES, pH 6.5, X-ray diffraction structure determination and analysis at 2.46 A resolution, molecular replacement and modelling
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75
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pH 7.0, 30 min, stable
100
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half-life: 44 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
NADP+ stabilizes against thermal inactivation, NAD+ has no effect
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salts stabilize against thermal inactivation in the order: potassium phosphate > sodium phosphate > K2SO4 > sodium citrate > KCl > NaCl
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several salts stabilize against thermal inactivation, K+-citrate is most effective
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hi-Trap nickel Sepharose column chromatography
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recombinant N-terminal His6-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS Rosetta by nickel affinity chromatography, ultrafiltration, and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned by functional complementation of an Escherichia coli gap mutant
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expressed in Escherichia coli Rosetta DE3 cells
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expressed in phosphoglucose isomerase-disrupted Escherichia coli (KS002) cells
expression at high levels in Escherichia coli, the primary structure exhibits a strikingly high proportion of aromatic amino acids
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expression in Escherichia coli
gene gapA, recombinant overexpression of mutant enzymes in Escherichia coli strain BL21(DE3)
gene gapC, recombinant overexpression in Corynebacterium glutamicum strain ATCC 13032, coexpression with Bacillus subtilis gene rocG encoding NAD+-dependent glutamate dehydrogenase, leading to increased L-ornithine biosynthesis in the engineered strain, overview. Quantitative real-time PCR expression analysis. Effects of overexpression of genes encoding enzymes in the upstream pathway of glutamate biosynthesis on L-ornithine production in Corynebacterium glutamicum DELTAAP. Overexpression of Clostridium acetobutylicum gapC increases the production of CoQ10
recombinant expression of N-terminal His6-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS Rosetta
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of isoforms GapA-1, GapB and phosphoribulokinase and peptide Cp12-2 is co-ordinately regulated with the same organ specificity, all four genes being mostly expressed in leaf and flower stalk, less expressed in flower, and little or not expressed in roots and siliques. Expression in leaf is terminated during prolonged darkness or following sucrose treatment, and their transcripts decay with similar kinetics
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D35G
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ , the catalytic efficiency with NADP+ is 3fold lower than with NAD+
D35G/L36R/P192S
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ with similar catalytic efficiency
D35G/L36T/T37K
site-directed mutagenesis, introducing a third mutation T37K into the mutant D35G/L36T completely reverses the coenzyme specificity of the enzyme
D35G/L36T/T37K/P192S
site-directed mutagenesis, the mutant shows high catalytic efficiency with NADP+ while the catalytic efficiency with NAD+ also increases. The replacement of Pro192 to Ser benefits the binding affinity of both NAD+ and NADP+
L36T
site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ , the catalytic efficiency with NADP+ is lower than with NAD+
D35G
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site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ , the catalytic efficiency with NADP+ is 3fold lower than with NAD+
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D35G/L36R/P192S
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site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ with similar catalytic efficiency
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D35G/L36T/T37K
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site-directed mutagenesis, introducing a third mutation T37K into the mutant D35G/L36T completely reverses the coenzyme specificity of the enzyme
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L36T
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site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ , the catalytic efficiency with NADP+ is lower than with NAD+
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D35G
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site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ , the catalytic efficiency with NADP+ is 3fold lower than with NAD+
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D35G/L36R/P192S
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site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ with similar catalytic efficiency
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D35G/L36T/T37K
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site-directed mutagenesis, introducing a third mutation T37K into the mutant D35G/L36T completely reverses the coenzyme specificity of the enzyme
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L36T
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site-directed mutagenesis, the mutant enzyme accepts both NAD+ and NADP+ , the catalytic efficiency with NADP+ is lower than with NAD+
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additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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