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
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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
strain 7119
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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
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UniProt
Manually annotated by BRENDA team
strain PCC 7601
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-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
Dermocarpa sp.
strain PCC 7437
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Manually annotated by BRENDA team
strain UTEX 1829
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Manually annotated by BRENDA team
strain UTEX 1829
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-
Manually annotated by BRENDA team
strain PCC 7107
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-
Manually annotated by BRENDA team
strain PCC6903
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Manually annotated by BRENDA team
strain PCC6903
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Manually annotated by BRENDA team
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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
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+
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
Asp
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activates
Cys
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activates
dithiothreitol
glutathione
Gly
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activates
His
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activates
lipoic acid
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enhances activity
Ser
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activates
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, 60C
0.21 - 0.77
D-glyceraldehyde 3-phosphate
0.03
NAD(P)+
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0.65 - 16.8
NAD+
0.01
NADH
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-
0.003 - 0.28
NADP+
0.002 - 0.18
NADPH
107
phosphate
pH 8.0, 60C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
49.1
3-phospho-D-glyceroyl phosphate
pH 8.0, 60C
2.8 - 13.1
D-glyceraldehyde 3-phosphate
10.7
NAD+
pH 8.0, 60C
0.75
NADP+
pH 8.0, 60C
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
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 18C
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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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
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
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