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Information on EC 1.2.1.13 - glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating)
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EC Tree
1.2.1.13 glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating)Specify your search results
Word Map
- 1.2.1.13
- chloroplast
- gapdhs
- phosphoribulokinase
-
nadp-linked
-
calvin
-
4.1.1.39
-
2.7.2.3
- 1,3-bisphosphoglycerate
-
2.7.1.19
- sedoheptulose
-
triose-p
- medicine
-
nad-specific
-
calvin-benson
- ribulose-5-phosphate
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
glyceraldehyde-3-p dehydrogenase, nadp-glyceraldehyde-3-phosphate dehydrogenase, phosphorylating glyceraldehyde-3-phosphate dehydrogenase, nadp-gapdh, gapa-1, nadp-gpd, glyceraldehyde-3-dehydrogenase, photosynthetic gapdh, ov-gapdh, glyceraldehyde-p dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide phosphate phosphorylating)
-
-
-
-
GapA
GapB
GAPDH
glyceraldehyde 3-phosphate dehydrogenase (NADP)
-
-
-
-
glyceraldehyde phosphate dehydrogenase (nicotinamide adenine dinucleotide phosphate phosphorylating)
-
-
-
-
glyceraldehyde-3-dehydrogenase
glyceraldehyde-3-phosphate dehhydrogenase (NADP+) (phoshphorylating)
glyceraldehyde-3-phosphate dehydrogenase
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
glyceraldehyde-P dehydrogenase
-
-
-
-
NAD(P)-GAPDH
-
-
-
-
NADP(H)-glyceraldehyde-3-phosphate dehydrogenase
NADP+-dependent G-3-P dehydrogenase
-
-
-
-
NADP+-dependent gapB
NADP-dependent glyceraldehyde phosphate dehydrogenase
-
-
-
-
NADP-dependent glyceraldehydephosphate dehydrogenase
-
-
-
-
NADP-GAPDH
NADP-glyceraldehyde phosphate dehydrogenase
-
-
-
-
NADP-glyceraldehyde-3-phosphate dehydrogenase
-
-
-
-
NADP-GPD
-
-
-
-
NADP-triose phosphate dehydrogenase
-
-
-
-
NADPH-D-GA3P
-
-
-
-
phosphorylating GAP dehydrogenase
SSO0528
triosephosphate dehydrogenase (NADP+)
-
-
-
-
GAPDH
-
-
-
-
glyceraldehyde-3-phosphate dehhydrogenase (NADP+) (phoshphorylating)
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glyceraldehyde 3-phosphate + phosphate + NADP+ = 3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+ = 3-phospho-D-glyceroyl phosphate + NADPH + H+
uni uni ping pong mechanism with an apparent Theorell Chance displacement between 1,3-diphosphoglycerate and phosphate, NAD(P)H on, glyceraldehyde 3-phosphate off, 1,3-diphosphoglycerate on, phosphate off, NAD(P)+ off
-
D-glyceraldehyde 3-phosphate + phosphate + NADP+ = 3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate:NADP+ oxidoreductase (phosphorylating)
-
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CAS REGISTRY NUMBER
COMMENTARY
37250-87-6
-
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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
3-phospho-D-glyceroyl phosphate + NADH + H+
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
-
r
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
DL-glyceraldehyde 3-phosphate + phosphate + NADP+
-
-
-
-
r
D-glyceraldehyde + phosphate + NADP+
D-glyceroylphosphate + NADPH
-
with 10fold lower efficiency than D-glyceraldehyde 3-phosphate
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
Vmax/Km for NADP+ is 33fold higher compared to Vmax/Km for NAD+
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
DL-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
-
r
DL-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
r
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 + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
Q81L07
-
-
-
?
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
Q81L07
-
-
-
?
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
-
-
-
?
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
probable function in CO2 fixation
-
-
?
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
-
-
-
?
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
-
-
?
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
the enzyme retains the deuterium at the C4 HA position, removing the hydrogen atom and is therefore a B(pro-S) specific dehydrogenase
-
?
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
only reaction of the reductive pentose phosphate cycle in chloroplasts that uses as a substrate reducing power, NADPH, that is generated photochemically
-
-
-
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
enzyme of Benson-Calvin cycle
-
?
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
regulatory enzyme of the reductive pentose phosphate cycle
-
-
-
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
-
-
-
?
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
-
-
-
?
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
-
-
-
r
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
-
-
-
?
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
-
-
-
r
D-glyceraldehyde 3-phosphate + arsenate + NADP+
3-phospho-D-glyceroyl arsenate + NADPH
-
-
-
-
-
D-glyceraldehyde 3-phosphate + arsenate + NADP+
3-phospho-D-glyceroyl arsenate + NADPH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NADP+
3-phospho-D-glyceroyl arsenate + NADPH
-
-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NADP+
3-phospho-D-glyceroyl arsenate + NADPH
-
-
-
-
-
D-glyceraldehyde 3-phosphate + arsenate + NADP+
3-phospho-D-glyceroyl arsenate + NADPH
-
-
-
-
?
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
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
reversible conversion of the NADH-linked enzyme, EC 1.2.1.12, into a form which preferentially uses NADPH as coenzyme in response to cysteine and 1,3-diphosphoglycerate
-
-
-
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH
-
reversible conversion of the NADH-linked enzyme, EC 1.2.1.12, into a form which preferentially uses NADPH as coenzyme in response to cysteine and 1,3-diphosphoglycerate
-
-
-
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
activity is specific for NADP+ as an electron acceptor
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
Vmax/Km for NADP+ is 33fold higher compared to Vmax/Km for NAD+
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
r
additional information
?
-
Ankistrodesmus braunii
-
the daily progress of rise of the enzyme activity in synchronous culture in respect to short time increase of activity by light
-
-
-
additional information
?
-
-
the enzyme interacts with small chloroplast protein CP12, and a strong interaction between GAPDH-CP12 and ferredoxin-NADP+ reductase, FNR EC 1.18.1.1, with a very low dissociation constant is observed, protein complex interaction kinetics, overview. The GAPDH-CP12-FNR complex is disrupted with NADP+
-
-
-
additional information
?
-
-
light-induced synthesis of chlorophyll and NADP-glyceraldehyde 3-phosphate dehydrogenase is inhibited when acetate or ethanol is added at the time of exposure of dark-grown resting cells to light
-
-
-
additional information
?
-
-
the enzyme does not regulate the photosynthesis rhythm
-
-
-
additional information
?
-
-
the transcription of the gene is upregulated during growth on D-xylose, which suggests that the enzyme is involved in regeneration of NADPH needed for xylose assimilation
-
-
-
additional information
?
-
the transcription of the gene is upregulated during growth on D-xylose, which suggests that the enzyme is involved in regeneration of NADPH needed for xylose assimilation
-
-
-
additional information
?
-
-
the enzyme may be involved in the activation of hexose monophosphate shunt and consequently in regulation of superoxide generation
-
-
-
additional information
?
-
-
glycerate-1,3-bisphosphate may be channeled from the phosphoglycerate kinase to NADP-linked glyceraldehyde 3-phosphate dehydrogenase in vivo
-
-
-
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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
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
DL-glyceraldehyde 3-phosphate + phosphate + NADP+
-
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
DL-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
-
-
-
-
r
DL-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
r
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
probable function in CO2 fixation
-
-
?
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
only reaction of the reductive pentose phosphate cycle in chloroplasts that uses as a substrate reducing power, NADPH, that is generated photochemically
-
-
-
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
enzyme of Benson-Calvin cycle
-
?
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
regulatory enzyme of the reductive pentose phosphate cycle
-
-
-
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
-
-
-
?
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
-
-
-
r
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
-
-
-
?
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
O34425
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
O34425
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
r
additional information
?
-
Ankistrodesmus braunii
-
the daily progress of rise of the enzyme activity in synchronous culture in respect to short time increase of activity by light
-
-
-
additional information
?
-
-
the enzyme interacts with small chloroplast protein CP12, and a strong interaction between GAPDH-CP12 and ferredoxin-NADP+ reductase, FNR EC 1.18.1.1, with a very low dissociation constant is observed, protein complex interaction kinetics, overview. The GAPDH-CP12-FNR complex is disrupted with NADP+
-
-
-
additional information
?
-
-
light-induced synthesis of chlorophyll and NADP-glyceraldehyde 3-phosphate dehydrogenase is inhibited when acetate or ethanol is added at the time of exposure of dark-grown resting cells to light
-
-
-
additional information
?
-
-
the enzyme does not regulate the photosynthesis rhythm
-
-
-
additional information
?
-
-
the transcription of the gene is upregulated during growth on D-xylose, which suggests that the enzyme is involved in regeneration of NADPH needed for xylose assimilation
-
-
-
additional information
?
-
Q8J0C9
the transcription of the gene is upregulated during growth on D-xylose, which suggests that the enzyme is involved in regeneration of NADPH needed for xylose assimilation
-
-
-
additional information
?
-
-
the enzyme may be involved in the activation of hexose monophosphate shunt and consequently in regulation of superoxide generation
-
-
-
additional information
?
-
-
glycerate-1,3-bisphosphate may be channeled from the phosphoglycerate kinase to NADP-linked glyceraldehyde 3-phosphate dehydrogenase in vivo
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
activity with NADP+ is about 50fold higher than that determined for NAD+
NAD+
-
reaction stoichiometry of 8:1 for both coenzymes and substrates, formation of the characteristic Racker band upon binding of either NADP+ or NAD+ to the apoenzyme
NAD+
-
reversible conversion of the NADH-linked enzyme, EC 1.2.1.12, into a form which preferentially uses NADPH as coenzyme in response to cysteine and 1,3-diphosphoglycerate
NAD+
-
optimum stimulation of NADPH-dependent dehydrogenase actvity is achieved on incubation of the NADH-specific enzyme with dithiothreitol and NADPH, or dithiothreitol and a 1,3-diphosphoglycerate generating system
NAD+
-
activity with NADP+ is higher than with NAD+; cofactor
NAD+
-
cofactor; NADP+ and NAD+ react with the enzyme at the same catalytic site
NAD+
-
Vmax/Km for NADP+ is 33fold higher compared to Vmax/Km for NAD+
NAD+
-
the highest activity is almost equal for NADP+ and NAD+, whereas the affinity for NADP+ is higher than that for NAD+
NADH
-
the residues Thr33 and Ser188 are involved in NADPH over NADH selectivity
NADP+
-
cofactor; reaction stoichiometry of 8:1 for both coenzymes and substrates, formation of the characteristic Racker band upon binding of either NADP+ or NAD+ to the apoenzyme
NADP+
-
cofactor; reversible conversion of the NADH-linked enzyme, EC 1.2.1.12, into a form which preferentially uses NADPH as coenzyme in response to cysteine and 1,3-diphosphoglycerate
NADP+
-
cofactor; optimum stimulation of NADPH-dependent dehydrogenase actvity is achieved on incubation of the NADH-specific enzyme with dithiothreitol and NADPH, or dithiothreitol and a 1,3-diphosphoglycerate generating system
NADP+
-
cofactor; NADP+ and NAD+ react with the enzyme at the same catalytic site
NADP+
-
cofactor
287990, 287991, 287992, 287996, 288000, 288001, 288002, 288004, 288006, 288015, 288021, 288022, 288025, 288030, 288031, 288032, 288034
NADP+
-
Vmax/Km for NADP+ is 33fold higher compared to Vmax/Km for NAD+
NADP+
Q81L07
isoform GapB shows slight activity with NADP+. The activity is about 7-8 times less than NAD+-dependent GAPDH activity of isoform GapA
NADP+
-
the highest activity is almost equal for NADP+ and NAD+, whereas the affinity for NADP+ is higher than that for NAD+
NADPH
-
the residues Thr33 and Ser188 are involved in NADPH over NADH selectivity
NADPH
-
in the gluconeogenic direction, the enzyme shows a strong preference for NADPH, and only negligible activity is detected with NADH
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
chloroplast protein CP12
-
the chloroplast protein CP12 behaves as a negative regulator of GAPDH activity
-
H2O2
-
rapid reversible deactivation of untreated and GSH-treated enzyme preparation, GSH reverses the inhibition
iodoacetate
-
preincubation with glyceraldehyde-phosphate, 10fold molar excess over iodoacetate, prevents inactivation
NADH
-
strong inhibition with excess co-substrate s observed and no activity is observed with over 2 mM NADH
sulfite
-
non-competitive inhibitor with respect to both NADPH and 3-phosphoglycerate
thioredoxin
-
a regulatory disulfide between Cys359 and Cys358 of the C-terminal extension of GapB does form in presence of oxidized thioredoxin. This covalent modification is required for the NAD+-dependent association into higher oligomers and inhibition of the NADPH-dependent activity
additional information
-
the activity of the GAPDH-CP12 complex is not affected by addition of bovine serum albumin, Rubisco, EC 4.1.1.39, or phosphoribulokinase, PRK EC 2.7.1.19. Incubation of GAPDH alone with NADPH, DTT or NADP has no effect on its activity
-
GAPDH segregator
-
GAPDS stimulates insulin signaling by segregating the tetrameric GAPDH into monomers, and thereby suppresses the intrinsic GAPDH activation of phosphoinositide's phosphatase activity
-
GAPDH segregator
-
GAPDH segregator, GAPDS, stimulates insulin signaling by segregating the tetrameric GAPDH into monomers, and thereby suppresses the intrinsic GAPDH activation of phosphoinositide's phosphatase activity
-
NAD+
-
promotes association of the enzyme protomer of 160000 Da into a regulatory conformer of 600000 Da with low NADPH activity during dark deactivation
NAD+
-
a regulatory disulfide between Cys359 and Cys358 of the C-terminal extension of GapB does form in presence of oxidized thioredoxin. This covalent modification is required for the NAD+-dependent association into higher oligomers and inhibition of the NADPH-dependent activity
NADPH
-
NADPH can inhibit GAPDH in complex with chloroplast protein CP12 in the presence of NADP+ reductase ferredoxin-NADP+ reductase, FNR, EC 1.18.1.1, because FNR is inhibited by NADPH. NADPH can also directly inhibit GAPDH. In crude extracts, glyceraldehyde-3-phosphate dehydrogenase can be inhibited by NADPH under oxidizing conditions. DTT reactivates the enzyme. The addition of commercial FNR from Spinacia oleracea inhibits GAPDH activity by 40% under oxidizing conditions when NADPH is present, and the effect is abolished by the addition of DTT
NADPH
-
strong inhibition with excess co-substrate s observed and no activity is observed with over 2 mM NADPH
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ferredoxin
-
enzyme is present throughout the life cycle of the plants, inactive enzyme is converted during greening to an active state by light either via enzyme effectors or via the ferredoxin-thioredoxin system
-
glycerate 1,3-bisphosphate
-
most effective on a molar basis in stimulating NADPH-activity of dark chloroplast extracts and purified enzyme
GSH
-
activates in the physiological concentration range 0.1-2 mM
1,3-diphosphoglycerate
-
the role of the reduction of the enzyme in vivo is to increase its sensitivity towards the activator 1,3-bisphosphoglycerate. The actual activation and aggregation state of the enzyme in chloroplasts in light is regulated by the concentration of 1,3-diphosphoglycerate as activator in the stroma and its actual activity by the availability of 1,3-diphosphoglycerate as substrate
ATP
-
high concentrations required for stimulation, activation by ATP is unlikely of physiological significance
dithiothreitol
-
the role of the reduction of the enzyme in vivo is to increase its sensitivity towards the activator 1,3-bisphosphoglycerate
dithiothreitol
-
activation; when ATP is also present, the induced enzyme is stabilized
dithiothreitol
-
the rate of induction of NADH-dependent activity by dithiothreitol increases hyperbolically with respect to NADPH concentration, implying that NADPH has more than a stabilising role in the activating process
thioredoxin
-
enzyme is present throughout the life cycle of the plants, inactive enzyme is converted during greening to an active state by light either via enzyme effectors or via the ferredoxin-thioredoxin system
thioredoxin
-
enzyme is activated by thioredoxin that is reduced either photochemically with ferredoxin and ferredoxin-thioredoxin reductase or chemically with dithiothreitol
additional information
-
the light-induced activation of GAPDH is not associated with the presence of ATP
-
additional information
-
the enzyme requires a high ratio of substrate to phosphate for activation. Mg2+ inhibits light activation of enzymes in intact chloroplasts. The substrate:phosphate ratio in the chloroplast may modulate enzyme activation in the light
-
additional information
-
enzyme is present throughout the life cycle of the plants, inactive enzyme is converted during greening to an active state by light either via enzyme effectors or via the ferredoxin-thioredoxin system
-
additional information
-
activation being dependent on oligomer dissociating to give protomers. The activation/dissociation process may be brought about by nucleotide binding, by sulfur bridge reduction or modification and by depression of hydrophobic interactions
-
additional information
-
light activation of the enzyme within leaf chloroplast appears to be modulated by mediators which are reduced by photosynthetic electron flow from the photosystem I reaction center
-
additional information
-
effect of an activator on the enzyme is selectively enhanced by either dithiothreitol-reduced thioredoxin-f or a cosolvent, and is inhibited by spermine
-
additional information
-
addition of organic solvents miscible in water to the activation process enhance the specific activity, cosolvents added during catalysis lower the rate of substrate conversion
-
additional information
-
complete light activation at 25 W*m-2 photosynthetically active radiation
-
additional information
-
no influence on activity is observed on assaying of the enzyme with 5 mM substrate and 0.5 mM co-substrate with 1 mM ATP, ADP, AMP, D-glucose 6-phosphate, D-fructose 6-phosphate, galactose 1-phosphate, D-glucose 1-phosphate or coenzyme A in either the glycolytic or gluconeogenic reaction
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Albinism
Correlations between photosynthetic enzymes, CO2-fixation and plastid structure in an albino mutant of Zea mays L.
Cataract
Human lens enzyme alterations with age and cataract: glyceraldehyde-3-P dehydrogenase and triose phosphate isomerase.
Coronary Artery Disease
AGXT2 and DDAH-1 genetic variants are highly correlated with serum ADMA and SDMA levels and with incidence of coronary artery disease in Egyptians.
Dehydration
Antioxidative defense system, pigment composition, and photosynthetic efficiency in two wheat cultivars subjected to drought
Filariasis
DNA vaccine encoding the moonlighting protein Onchocerca volvulus glyceraldehyde-3-phosphate dehydrogenase (Ov-GAPDH) leads to partial protection in a mouse model of human filariasis.
Heart Arrest
Effects of fructose-1,6-diphosphate, glucose, and saline on cardiac resuscitation.
Infection
DNA vaccine encoding the moonlighting protein Onchocerca volvulus glyceraldehyde-3-phosphate dehydrogenase (Ov-GAPDH) leads to partial protection in a mouse model of human filariasis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
3-phospho-D-glyceroyl phosphate
-
mutant enzyme T33A/S188A, reaction with NADH
0.012
3-phospho-D-glyceroyl phosphate
-
mutant enzyme S188A, reaction with NADH; mutant enzyme T33A, reaction with NADH; mutant enzyme T33A/S188A, reaction with NADPH; native enzyme A3-GAPDH, reaction with NADH
0.013
3-phospho-D-glyceroyl phosphate
-
mutant enzyme S188A, reaction with NADPH
0.015
3-phospho-D-glyceroyl phosphate
-
native enzyme A3-GAPDH, reaction with NADPH
0.015
3-phospho-D-glyceroyl phosphate
-
GapA; GapB, analyzed under reducing conditions
0.016
3-phospho-D-glyceroyl phosphate
-
with NADH as cofactor, activation by 20 mM dithiothreitol and 0.021 mM 1,3-bisphosphoglycerate
0.018
3-phospho-D-glyceroyl phosphate
-
mutant enzyme T33A, reaction with NADPH
0.019
3-phospho-D-glyceroyl phosphate
-
A(plusCTE) mutant, analyzed under oxidizing conditions
0.02
3-phospho-D-glyceroyl phosphate
-
with NADPH as coenzyme, activation by 20 mM dithiothreitol and 0.021 mM 1,3-bisphosphoglycerate
0.02
3-phospho-D-glyceroyl phosphate
-
AB-GAPDH, analyzed under reducing conditions; GapB, analyzed under oxidizing conditions
0.021
3-phospho-D-glyceroyl phosphate
-
A(plusCTE) mutant, analyzed under reducing conditions
0.024
3-phospho-D-glyceroyl phosphate
-
AB-GAPDH, analyzed under oxidizing conditions
0.027
3-phospho-D-glyceroyl phosphate
-
mutant B(188)A, analyzed under oxidizing conditions
0.031
3-phospho-D-glyceroyl phosphate
-
mutant B(188)A, analyzed under reducing conditions
5.8
3-phospho-D-glyceroyl phosphate
-
wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 50°C
0.75
D-glyceraldehyde 3-phosphate
pH 9.2, 30°C, reaction with NAD+ or NADP+
0.21
DL-glyceraldehyde 3-phosphate
-
wild type enzyme, with NADP+ as cosubstrate, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C
0.77
DL-glyceraldehyde 3-phosphate
-
wild type enzyme, with NAD+ as cosubstrate, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C
16.8
NAD+
-
wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C
0.01
NADH
-
mutant enzyme R190A, pH and temperature not specified in the publication
0.102
NADH
-
mutant enzyme R82D, pH and temperature not specified in the publication
0.12
NADH
-
pH 7.7, 30°C, recombinant A4 glyceraldehyde 3-phosphate dehydrogenase
0.12
NADH
-
wild type enzyme, pH and temperature not specified in the publication
0.136
NADH
-
pH 7.7, 30°C, native A4 glyceraldehyde 3-phosphate dehydrogenase
0.157
NADH
-
mutant enzyme R82A, pH and temperature not specified in the publication
0.29
NADH
-
with NADH as coenzyme, activation by 20 mM dithiothreitol and 0.021 mM 1,3-bisphosphoglycerate
0.61
NADH
-
wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 50°C
0.872
NADH
-
mutant enzyme S195A, pH and temperature not specified in the publication
0.28
NADP+
-
wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C
0.018
NADPH
-
pH 7.7, 30°C, native A4 glyceraldehyde 3-phosphate dehydrogenase
0.024
NADPH
-
mutant B(188)A, analyzed under oxidizing conditions; mutant B(E362Q)
0.028
NADPH
-
pH 7.7, 30°C, recombinant A4 glyceraldehyde 3-phosphate dehydrogenase
0.028
NADPH
-
mutant enzyme S195A, pH and temperature not specified in the publication; wild type enzyme, pH and temperature not specified in the publication
0.05
NADPH
-
AB-GAPDH, analyzed under oxidizing conditions; AB-GAPDH, analyzed under reducing conditions
0.06
NADPH
-
activation by 20 mM dithiothreitol and 0.021 mM 1,3-bisphosphoglycerate
0.18
NADPH
-
wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 50°C
0.202
NADPH
-
mutant enzyme R82D, pH and temperature not specified in the publication
0.3
NADPH
-
mutant enzyme R82A, pH and temperature not specified in the publication
10.7
phosphate
-
wild type enzyme, with NADP+ as cosubstrate, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C
additional information
additional information
-
no Michaelis-Menten kinetics with 1,3-bisphosphoglycerate
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
catalytic rate constant 238 s-1, control; catalytic rate constant 289 s-1, 3 microM 3-phospho-D-glyceroyl phosphate, NADPH-dependent activity of GAPDH in the GAPDH/CP12 complex; catalytic rate constant 316 s-1, 160 microM 3-phospho-D-glyceroyl phosphate, NADPH-dependent activity of GAPDH in the GAPDH/CP12 complex; catalytic rate constant 330 s-1, 10 microM thioredoxin, NADPH-dependent activity of GAPDH in the GAPDH/CP12 complex; catalytic rate constant 390 s-1, 10 microM thioredoxin, 3 microM 3-phospho-D-glyceroyl phosphate, NADPH-dependent activity of GAPDH in the GAPDH/CP12 complex; catalytic rate constant 462 s-1, 10 microM thioredoxin, 160 microM 3-phospho-D-glyceroyl phosphate, NADPH-dependent activity of GAPDH in the GAPDH/CP12 complex
-
40
3-phospho-D-glyceroyl phosphate
-
pH 7.7, 30°C, native A4 glyceraldehyde 3-phosphate dehydrogenase, reaction with NADH
88
3-phospho-D-glyceroyl phosphate
-
pH 7.7, 30°C, recombinant A4 glyceraldehyde 3-phosphate dehydrogenase, reaction with NADH
223
3-phospho-D-glyceroyl phosphate
-
pH 7.7, 30°C, native A4 glyceraldehyde 3-phosphate dehydrogenase, reaction with NADPH
419
3-phospho-D-glyceroyl phosphate
-
pH 7.7, 30°C, recombinant A4 glyceraldehyde 3-phosphate dehydrogenase, reaction with NADPH
8.4
NADH
-
mutant enzyme R190A, pH and temperature not specified in the publication
41
NADH
-
pH 7.7, 30°C, native A4 glyceraldehyde 3-phosphate dehydrogenase
71
NADH
-
mutant enzyme R82A, pH and temperature not specified in the publication
104
NADH
-
pH 7.7, 30°C, recombinant A4 glyceraldehyde 3-phosphate dehydrogenase
104
NADH
-
wild type enzyme, pH and temperature not specified in the publication
119
NADH
-
mutant enzyme S195A, pH and temperature not specified in the publication
135
NADH
-
mutant enzyme R82D, pH and temperature not specified in the publication
196
NADPH
-
mutant enzyme R82A, pH and temperature not specified in the publication
203
NADPH
-
mutant enzyme R82D, pH and temperature not specified in the publication
210
NADPH
-
mutant enzyme S195A, pH and temperature not specified in the publication
251
NADPH
-
pH 7.7, 30°C, native A4 glyceraldehyde 3-phosphate dehydrogenase
430
NADPH
-
pH 7.7, 30°C, recombinant A4 glyceraldehyde 3-phosphate dehydrogenase
430
NADPH
-
wild type enzyme, pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
49.1
3-phospho-D-glyceroyl phosphate
-
wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 50°C
10.7
NAD+
-
wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C
0.081
NADH
-
wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 50°C
0.75
NADP+
-
wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C
0.035
NADPH
-
wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 50°C
2.8
DL-glyceraldehyde 3-phosphate
-
wild type enzyme, with NAD+ as cosubstrate, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C
13.1
DL-glyceraldehyde 3-phosphate
-
wild type enzyme, with NADP+ as cosubstrate, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.015
GAPDH segregator
Oryctolagus cuniculus
-
GAPDS inhibts the glycolytic enzymatic function of GAPDH
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.026
-
pH not specified in the publication, 37°C, activity in undialyzed cell extracts
0.0602
-
effect of water stress on the activity, stress, 1 day, control, 39.6% of control value, Lutescens 758, seedlings
0.0759
-
effect of water stress on the activity, stress, 1 day, Kartolin-4, 50.5% of control value, Lutescens 758, seedlings
0.076
-
effect of water stress on the activity, rehydration, control, 50.1% of control value, Lutescens 758, seedlings
0.0843
-
effect of water stress on the activity, stress, 1 day, control, 25.4% of control value, Mironovskaya 808, seedlings
0.0916
-
effect of water stress on the activity, rehydration, Kartolin-4, 61.0% of control value, Lutescens 758, seedlings
0.1103
-
effect of water stress on the activity, stress, 1 day, BAP, 33.2% of control value, Mironovskaya 808, seedlings
0.1169
-
effect of water stress on the activity, stress, 1 day, TDZ, 35.2% of control value, Mironovskaya 808, seedlings
0.123
-
effect of water stress on the activity, stress, 2 weeks, control, 51.0% of control value, Lutescens 758, leaves
0.1265
-
effect of water stress on the activity, stress, 1 day, Kartolin-2, 38.1% of control value, Mironovskaya 808, seedlings
0.1457
-
effect of water stress on the activity, rehydration, control, 60.4% of control value, Lutescens 758, leaves
0.1502
-
effect of water stress on the activity, original Kartolin-4, 100% of control value, Lutescens 758, seedlings
0.152
-
effect of water stress on the activity, original control, 100% of control value, Lutescens 758, seedlings
0.2002
-
effect of water stress on the activity, stress, 2 weeks, Kartolin-4, 79.9% of control value, Lutescens 758, leaves
0.2153
-
effect of water stress on the activity, rehydration, Kartolin-4, 86.0% of control value, Lutescens 758, leaves
0.2412
-
effect of water stress on the activity, original, control, 100% of control value, Lutescens 758, leaves
0.2503
-
effect of water stress on the activity, original, Kartolin-4, 100% of control value, Lutescens 758, leaves
0.3321
-
effect of water stress on the activity, original, control, 100% of control value, Mironovskaya 808, seedlings
0.7602
-
effect of water stress on the activity, stress, 2 weeks, control, 62.2% of control value, Mironovskaya 808, leaves
0.8568
-
effect of water stress on the activity, stress, 2 weeks, TDZ, 69.9% of control value, Mironovskaya 808, leaves
0.86
-
effect of water stress on the activity, stress, 2 weeks, BAP, 70.1% of control value, Mironovskaya 808, leaves
0.9806
-
effect of water stress on the activity, stress, 1 day, control, 80.1% of control value, Mironovskaya 808, leaves
0.9878
-
effect of water stress on the activity, stress, 2 weeks, Kartolin-2, 80.7% of control value, Mironovskaya 808, leaves
0.9989
-
effect of water stress on the activity, stress, 1 day, TDZ, 80.8% of control value, Mironovskaya 808, leaves
1.101
-
effect of water stress on the activity, rehydration, control, 89.9% of control value, Mironovskaya 808, leaves; effect of water stress on the activity, stress, 1 day, BAP, 89.9% of control value, Mironovskaya 808, leaves
1.11
-
effect of water stress on the activity, stress, 1 day, Kartolin-2, 90.1% of control value, Mironovskaya 808, leaves
1.138
-
effect of water stress on the activity, rehydration, TDZ, 94.0% of control value, Mironovskaya 808, leaves
1.145
-
effect of water stress on the activity, rehydration, BAP, 94.5% of control value, Mironovskaya 808, leaves
1.187
-
effect of water stress on the activity, rehydration, Kartolin-2, 97.8% of control value, Mironovskaya 808, leaves
1.224
-
effect of water stress on the activity, original, control, 100% of control value, Mironovskaya 808, leaves
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9.1
-
pH 7.0: about 40% of maximal activity, pH 9.1: about 90% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
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; tissue with highest activity
brenda
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; tissue with highest activity. Expression is terminated during prolonged darkness or following sucrose treatments
brenda
-
minimal activity in leaf primordia, which are enclosed in the bud, a gradient of increasing activity along the leaf blade as leaves expand out of the bud and are exposed to light, further modest increase to a maximum level of activity as leaves attain full expansion, decrease in activity as mature, fully expanded leaves become senescent
brenda
-
-
brenda
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
brenda
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
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
ferredoxin-NADP-reductase EC 1.18.1.2 and GAPD are co-localized, suggesting that ferredoxin-NADP-reductase might carry FADH2 or NADPH from the thylakoid membrane to GAPD, or that ferredoxin might carry electrons to ferredoxin-NADP-reductase; GAPD is colocalized with ferredoxin-NAPD reductase in chloroplasts
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
a deletion mutant strain does not exhibit any growth under gluconeogenic conditions
metabolism
physiological function
metabolism
-
Diatom plastids lack of the oxidative pentose phosphate pathway, and so cannot produce NADPH in the dark. The observed downregulation of GAPDH in the dark may allow NADPH to be rerouted towards other reductive processes contributing to their ecological success
physiological function
-
with the aid of the gapC gene, NADPH-dependent production of lycopene and epsilon-caprolactone is enhanced by 150 and 95%, respectively. Especially, overexpression of gapC significantly reduces the carbon flux to the pentose phosphate pathway (80% decrease)
physiological function
-
the enzyme is involved in glycogen catabolism
physiological function
-
GAPDH has a strategic position within cell metabolism because GAP is an intermediate in many metabolic pathways, and therefore GAPDH needs to be highly regulated. In cyanobacteria, green and red algae and higher plants, GAPDH and phosphoribulokinase (PRK, EC 2.7.1.19) are downregulated by forming a ternary complex with CP12. Regulation of the key Calvin cycle enzymes of diatom algae differs from that of the Plantae. Enzyme GAPDH interacts with ferredoxin-nicotinamide adenine dinucleotide phosphate (NADP) reductase (FNR) from the primary phase of photosynthesis, and the small chloroplast protein, CP12
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
A0A0J9E1Q7_9RHOB
333
0
35950
TrEMBL
A0A3G7RL70_9PSED
521
0
57134
TrEMBL
A0A3G7LWB2_9PSED
487
0
53279
TrEMBL
A0A3G7F4S7_9PSED
487
0
53232
TrEMBL
Q8VXQ5_BIGNA
Bigelowiella natans (Pedinomonas minutissima) (Chlorarachnion sp. (strain CCMP621))
444
0
47523
TrEMBL
A0A3G7ICI2_9PSED
521
0
57134
TrEMBL
A0A3G7JCX9_9PSED
487
0
53248
TrEMBL
A0A3G7KX24_9PSED
487
0
53218
TrEMBL
G3P_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
340
0
37596
Swiss-Prot
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
-
4 * 36000, isoenzyme 2, SDS-PAGE; A2B2, 2 * 36000 + 2 * 39000, isoenzyme 1, SDS-PAGE
36225
-
x * 39355, subunit A, + x * 36225, subunit B, calculation from amino acid sequence
36854
-
4 * 36854, native A4 glyceraldehyde 3-phosphate dehydrogenase, MALDI-TOF
37000
37072
-
4 * 37072, recombinant A4 glyceraldehyde 3-phosphate dehydrogenase, MALDI-TOF
38000
39000
39355
-
x * 39355, subunit A, + x * 36225, subunit B, calculation from amino acid sequence
39500
40000
42000
43000
152000
-
native A4 glyceraldehyde 3-phosphate dehydrogenase in complex with the small protein CP12, gel filtration
155000
189000
-
tetrameric conformation of GAPDH-A2B2 stabilized by NADPH, estimated by gel filtration
232000
-
GapB mutant B(E326Q) in the presence of NADPH, estimated by gel filtration
243000
-
wild-type GapB, tetramer in the presence of NADPH, estimated by gel filtration
247000
-
GapB mutant B(S188A) in the presence of NADPH, estimated by gel filtration
270000
-
A(plusCTE) mutant, tetramer in the presence of NADPH, estimated by gel filtration
278000
-
GapB mutant B(R77A) in the presence of NADPH, estimated by gel filtration
491000
-
wild-type GapB in the presence of NADH, compatible with octameric structure, estimated by gel filtration
520000
-
GapB mutant B(E326Q) in the presence of NADH, compatible with octameric structure, estimated by gel filtration; GapB mutant B(R77A) in the presence of NADH, compatible with octameric structure, estimated by gel filtration
553000
-
GapB mutant B(S188A) in the presence of NADH, compatible with octameric structure, estimated by gel filtration
600000
760000
-
oligomer of GAPDH in the presence of NADH, suggesting A8B8 stoichiometry, estimated by gel filtration
37000
-
4 * 37000, GAPDH III, SDS-PAGE; x * 43000 + x * 37000, excess of the lighter subunit, GAPDH II, SDS-PAGE; x * 43000 + x * 37000, molar ratio of the subunits is 1:1, GAPDH I, SDS-PAGE
38000
-
4 * 38000, isoenzyme 2, SDS-PAGE; A2B2, 2 * 38000 + 2 * 42000, isoenzyme 1, SDS-PAGE
38000
-
4 * 38000, isoenzyme 2, SDS-PAGE; A2B2, 2 * 38000 + 2 * 40000, isoenzyme I, SDS-PAGE
38000
-
4 * 38000, isoenzyme 2, SDS-PAGE; A2B2, 2 * 38000 + 2 * 39000, isoenzyme 1, SDS-PAGE
43000
-
x * 43000 + x * 37000, excess of the lighter subunit, GAPDH II, SDS-PAGE; x * 43000 + x * 37000, molar ratio of the subunits is 1:1, GAPDH I, SDS-PAGE
155000
-
recombinant A4 glyceraldehyde 3-phosphate dehydrogenase, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
tetramer
additional information
?
-
x * 39355, subunit A, + x * 36225, subunit B, calculation from amino acid sequence
?
-
x * 43000 + x * 37000, excess of the lighter subunit, GAPDH II, SDS-PAGE; x * 43000 + x * 37000, molar ratio of the subunits is 1:1, GAPDH I, SDS-PAGE
homotetramer
-
4 * 37500, calculated from amino acid sequence; 4 * 38000, SDS-PAGE
tetramer
-
4 * 36854, native A4 glyceraldehyde 3-phosphate dehydrogenase, MALDI-TOF; 4 * 37072, recombinant A4 glyceraldehyde 3-phosphate dehydrogenase, MALDI-TOF
tetramer
-
4 * 36000, isoenzyme 2, SDS-PAGE; A2B2, 2 * 36000 + 2 * 39000, isoenzyme 1, SDS-PAGE
tetramer
-
4 * 38000, isoenzyme 2, SDS-PAGE; A2B2, 2 * 38000 + 2 * 42000, isoenzyme 1, SDS-PAGE
tetramer
-
composed of very similar A and B subunits, appear to hybridize most likely forming a family of five tetramers, A4, A3B, A2B2, AB3 and B4
tetramer
-
4 * 37581, calculated from sequence; 4 * 37611, laser desorption mass spectrophotometry; 4 * 39500, SDS-PAGE
tetramer
-
4 * 38000, isoenzyme 2, SDS-PAGE; A2B2, 2 * 38000 + 2 * 39000, isoenzyme 1, SDS-PAGE
tetramer
-
4 * 38000, isoenzyme 2, SDS-PAGE; A2B2, 2 * 38000 + 2 * 40000, isoenzyme I, SDS-PAGE
additional information
-
subunit A and B are very similar in primary sequence
additional information
-
NAD(P)-controlled aggregation of glyceraldehyde-3-phosphate dehydrogenase (NADP) is due primarily to enzyme association with a separate binding fraction rather than to enzyme polymerization
additional information
-
structural characterization of the subunits, the subunits have a very similar amino acid composition
additional information
-
enzyme is freely interconvertible between protomers of the 160000 Da form or the 300000 Da intermediate form with high NADPH-activity, produced in the light by the action of thioredoxin and activating metabolites, and a regulatory 600000 Da conformer with lower NADPH-activity produced in darkness or when photosynthesis is inhibited
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
in presence and absence of NADP+, to 2.6 A and 1.74 A resolution, respectively
-
crystallized from ammonium sulfate to produce crystals that diffract to 2.4 A with a space group of P4(3)2(1)2 or P4(1)2(1)2
-
determination of the crystal structure of the apoenzyme by multiple isomorphous replacement at 2.05 A resolution, hanging drop technique. The crystals belong to space group P4(1)2(1)2 or its enantiomorph with cell dimensions a = b = 102.3 A, c = 181.6 A, which contract upon cryocooling at 100 K to a = b = 101.6 A, c = 179.9 A. The asymmetric unit contains two subunits with a molecular mass of 37611 Da
-
crystal structure of the non-regulatory A(4) isoform of glyceraldehyde-3-phosphate dehydrogenase complexed with NADP+
-
hanging-drop vapour-diffusion method is used to grow crystals of recombinant A4-GAPDH, T33A and S188A A4-GAPDH mutants complexed with NADP+
-
molecular docking of ferredoxin-NADP-reductase EC 1.18.1.2 and GAPD. enzymes are able to form at least two different complexes, one involving a single GAPD monomer and an ferredoxin-NADP-reductase monomer or dimer. The amino acid residues located at the putative interface are highly conserved on the chloroplastic forms of both enzymes. The other potential complex involves the GAPD A2B2 tetramer and an FNR monomer or dimer. Ferredoxin is able to interact with FNR in either complex
-
sitting drop vapour diffusion method with 2.0-2.5 M or 1.5-1.2 M ammonium sulfate and 0.1 M potassium phosphate (pH 7.0-8.0)
-
two crystal forms of the A4-GAPDH isoform are used to solve the structure of the apo form to a resolution of 3.0 A
-
the structure of NADP-dependent GAPDH in complex with NADP is solved by molecular replacement and refined to an R factor of 19.1% and a free R factor of 24% at 2.5 A resolution
-
the crystal structure of apo-glyceraldehyde-3-phosphate dehydrogenase is solved by molecular replacement and refined to an R of 21.7% and Rfree of 27.5% at 2.9 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K128A
-
Km-value for NADPH is nearly identical to wild-type value, turnover-number for NADPH is decreased about 2fold. Km-value for NADH is increased 2.1fold compared to wild-type enzyme, turnover-number for NADH is decreased 2.6fold
K128E
-
Km-value for NADPH is about 80% of the wild-type value, turnover-number for NADPH is decreased 2.7fold. Km-value for NADH is increased 2.3fold compared to wild-type enzyme, turnover-number for NADH is decreased 1.9fold
R190A
-
the catalytic constant, kcat, of the mutant in the presence of NADH decreases 10fold while the Km for NADH decreases 12fold. The mutant shows no activity with NADPH
R197A
-
Km-value for NADPH is identical to wild-type value, turnover-number for NADPH is about 90% of the wild-type value. Km-value for NADH is about 80% of the wild-type value, turnover-number for NADH is nearly identical to wild-type value
R197E
-
Km-value for NADPH is increased 1.3fold compared to wild-type enzyme, turnover-number for NADPH is decreased 2fold. Km-value for NADH is about 90% of the wild-type value, turnover-number for NADH is increased 1.3fold
R82A
-
the mutation leads to a 10fold increase in the Km for NADPH but does not affect the kinetics of NADH
R82D
-
the mutation leads to a 10fold increase in the Km for NADPH but does not affect the kinetics of NADH
S195A
-
the mutation has no effect on the affinity of the enzyme for NADPH and its affinity for NADH and for BPGA in the presence of NADH is reduced
C151S
K225A
-
K225 is critical for binding of GAPDH to Siah1, an ubiquitin-E3-ligase, eliciting the translocation of GAPDH to the nucleus
Y123W
-
increase of temperature of irreversible inactivation by 1.3°C
Y323S
-
decrease of temperature of irreversible inactivation by 4.5°C
C151S
C349S
-
mutant of GapB subunit is less redox-sensitive than GapB. Active tetramer, unable to aggregate to higher oligomers in presence of NAD+
C349S/C358S
-
mutant of GapB subunit is less redox-sensitive than GapB. Active tetramer, unable to aggregate to higher oligomers in presence of NAD+
c358S
-
mutant of GapB subunit is less redox-sensitive than GapB. Active tetramer, unable to aggregate to higher oligomers in presence of NAD+
E356Q/E357Q
-
complete redox insensitivity is achieved in the double mutant
S188A
-
affinity for NADPH is significantly decreased, decrease in the ratio of turnover number to Km-value in the NADPH-dependent reaction, significant expansion of the A4-tetramer
T33A
-
affinity for NADPH is significantly decreased, turnover-number for NADPH is lowered
T33A/S188A
-
affinity for NADPH is significantly decreased, turnover-number for NADPH is lowered
additional information
C151S
-
mutant, substituting Ser for Cys at position 151 of GAPDH results in no binding to the cells, no decreased cell-spreading efficiency and no cell morphological changes
C151S
-
mutant, substituting Ser for Cys at position 151 of GAPDH results in no binding to the cells, no decreased cell-spreading efficiency and no cell morphological changes
C151S
-
mutant, substituting Ser for Cys at position 151 of GAPDH results in no binding to the cells, no decreased cell-spreading efficiency and no cell morphological changes
C151S
-
mutant, substituting Ser for Cys at position 151 of GAPDH results in no binding to the cells, no decreased cell-spreading efficiency and no cell morphological changes
additional information
to increase NADPH bioavailability, the native NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase (GAPDH) gapA gene, EC 1.2.1.12, in Escherichia coli is replaced with the NADP+-dependent gapB gene, EC 1.2.1.13, from Bacillus subtilis. To overcome the limitation of NADP+ availability, Escherichia coli NAD kinase, gene nadK is also coexpressed with gapB in Escherichia coli. replacing NAD+-dependent GapA activity with NADP+-dependent GapB activity increases the synthesis of NADPH-dependent compounds
additional information
-
to increase NADPH bioavailability, the native NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase (GAPDH) gapA gene, EC 1.2.1.12, in Escherichia coli is replaced with the NADP+-dependent gapB gene, EC 1.2.1.13, from Bacillus subtilis. To overcome the limitation of NADP+ availability, Escherichia coli NAD kinase, gene nadK is also coexpressed with gapB in Escherichia coli. replacing NAD+-dependent GapA activity with NADP+-dependent GapB activity increases the synthesis of NADPH-dependent compounds
-
additional information
-
construction of hybrid enzymes between the glyceraldehyde-3-phosphate dehydrogenases from the mesophilic Methanobacterium bryantii and the thermophilic Methanothermus fervidus
additional information
-
construction of hybrid enzymes between the glyceraldehyde-3-phosphate dehydrogenases from the mesophilic Methanobacterium bryantii and the thermophilic Methanothermus fervidus
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
100
104
-
half-life: 9 min without stabilizer, stable for 30 min in presence of 250 mM potassium citrate
additional information
80
-
activity half-life: 17 h. The thermostability of the enzyme can be attributed to a combination of an ion pair cluster and an intrasubunit disulfide bond
additional information
-
the efficiency of salts stabilizing against thermal inactivation at a specific ionic strength decrease in the order: potassium phosphate, sodium phosphate, potassium sulfate, sodium sulfate, sodium citrate, potassium chloride, sodium chloride
additional information
-
sodium chloride, potassium chloride, sodium sulfate, potassium sulfate, sodium phosphate, potassium phosphate, sodium citrate and potassium citrate stabilize against thermal inactivation at 104°C. K+ is more effective than Na+ with respect to anion
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is stabilized by glycerol, several salts, especially sodium or potassium phosphate
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxidation typically leads to about 50% inhibition of the NADPH-dependent activity
-
689747
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, GAPDH I is stable for several months, GAPDH II and GAPDH III spontaneously lose activity
-
4°C, pH 8.5, protein concentration 2.5 mg/ml, apoprotein, complete loss of activity after 48 h
-
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
2 isoenzymes: 1 and 2
by Ni2+ chelate chromatography and pH-shift under denaturating conditions
-
heat treatment at 80°C is an effective first step in the purification of these recombinant enzymes from extracts of the Escherichia coli host
-
recombinant and native GAPDH are purified to apparent homogeneity from Escherichia coli cells and Chlamydomonas reinhardtii, respectively
-
the GAPDH–CP12–FNR complex is purified using ion exchange chromatography and gel filtration, followed by complex dissociation with 20 mM DTT for 20 min at 30°C, and gel filtration to about 86% purity, all steps in presence of NADPH
-
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Saccharomyces cerevisiae mutant AG2 with deletion of NAD+-dependent glycerol-3-phosphate dehydrogenase gene GPD2
-
expression in Escherichia coli
expression in Escherichia coli. The phosphoglycerate kinase and glyceraldehyde-3-phosphate dehydrogenase genes from Sulfolobus solfataricus overlap by 8-bp
-
gene gapB, recombinant overexpression in and complementation of Escherichia coli gapA-deficient strain MG1655 gapA::Tn10, gene gapB is expressed from plasmid pDHC29 under the Plac promoter control, coexpression with Escherichia coli gene nadK encoding the NAD kinase, genes gapB and nadk are grouped as a single operon
into the pJC45Flag vector for expression in the Escherichia coli strain PAPlaclQ DE3, into the vaccination vector pcDNA3.1+ for transformation of DH5alpha cells
-
overexpression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a slight increase in enzyme activity is observed in the presence of D-fructose 6-phosphate and coenzyme A (1.1fold)
-
ATP, ADP, AMP, D-glucose 6-phosphate and galactose 1-phosphate exhibit no effect on enzyme activity
-
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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
Onchocerca volvulus antigens possibly involved in protection against human onchocerciasis, GAPDH as a therapeutic target in helminth infections
medicine
-
the results suggest that GAPDH is an active regulator in the phosphoinositide-mediated signaling pathway and a potential new target for insulin resistance treatment, diabetes, obesity and aging research
medicine
-
the results suggest that GAPDH is an active regulator in the phosphoinositide-mediated signaling pathway and a potential new target for insulin resistance treatment, diabetes, obesity and aging research
medicine
-
results suggest that GAPDH may have a common role in modulating the pathophysiology of polyQ diseases like the Huntington desease
medicine
-
results suggest that GAPDH may have a common role in modulating the pathophysiology of polyQ diseases like the Huntington desease
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zwickl, P.; Fabry, S.; Bogedain, C.; Haas, A.; Hensel, R.
Glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaebacterium Pyrococcus woesei: characterization of the enzyme, cloning and sequencing of the gene, and expression in Escherichia coli
J. Bacteriol.
172
4329-4338
1990
Pyrococcus woesei
brenda
Fabry, S.; Hensel, R.
Purification and characterization of D-glyceraldehyde-3-phosphate dehydrogenase from the thermophilic archaebacterium Methanothermus fervidus
Eur. J. Biochem.
165
147-155
1987
Methanothermus fervidus
brenda
Martin, W.; Cerff, R.
Prokaryotic features of a nucleus-encoded enzyme. cDNA sequences for chloroplast and cytosolic glyceraldehyde-3-phosphate dehydrogenase from mustard (Sinapis alba)
Eur. J. Biochem.
159
323-331
1986
Sinapis alba
brenda
Grissom, F.E.; Kahn, J.S.
Glyceraldehyde-3-phosphate dehydrogenases from Euglena gracilis. Purification and physical and chemical characterization
Arch. Biochem. Biophys.
171
444-458
1975
Euglena gracilis
brenda
Biro, J.; Fabry, S.; Dietmaier, W.; Bogedain, C.; Hensel, R.
Engineering thermostability in archaebacterial glyceraldehyde-3-phosphate dehydrogenase. Hints for the important role of interdomain contacts in stabilizing protein conformation
FEBS Lett.
275
130-134
1990
Methanobacterium bryantii, Methanothermus fervidus
brenda
Wolosiuk, R.A.; Stein, M.
Modulation of spinach chloroplast NADP-glyceraldehyde-3-phosphate dehydrogenase by chaotropic anions
Arch. Biochem. Biophys.
279
70-77
1990
Spinacia oleracea
brenda
Ferri, G.; Stoppini, M.; Meloni, M.L.; Zapponi, M.C.; Iadarola, P.
Chloroplast glyceraldehyde-3-phosphate dehydrogenase (NADP): amino acid sequence of the subunits from isoenzyme I and structural relationship with isoenzyme II
Biochim. Biophys. Acta
1041
36-42
1990
Spinacia oleracea
brenda
Levy, L.M.; Betts, G.F
Stereospecificity of C4 nicotinamide hydrogen transfer of the NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
Biochim. Biophys. Acta
997
331-333
1989
Spinacia oleracea
brenda
Fabry, S.; Lehmacher, A.; Bode, W.; Hensel, R.
Expression of the glyceraldehyde-3-phosphate dehydrogenase gene from the extremely thermophilic archaebacterium Methanothermus fervidus in E. coli. Enzyme purification, crystallization, and preliminary crystal data
FEBS Lett.
237
213-217
1988
Methanothermus fervidus
brenda
Gowri, G.; Campbell, W.H.
cDNA clones for corn leaf NADH:nitrate reductase and chloroplast NAD(P)+:glyceraldehyde-3-phosphate dehydrogenase
Plant Physiol.
90
792-798
1989
Zea mays
brenda
Hensel, R.; Laumann, S.; Lang, J.; Heumann, H.; Lottspeich, F.
Characterization of two D-glyceraldehyde-3-phosphate dehydrogenases from the extremely thermophilic archaebacterium Thermoproteus tenax
Eur. J. Biochem.
170
325-333
1987
Thermoproteus tenax
brenda
Ferri, G.; Stoppini, M.; Iadarola, P.; Zapponi, M.C.; Galliano, M.; Minchiotti, L.
Structural characterization of the subunit of spinach chloroplast glyceraldehyde-3-phosphate dehydrogenase (NADP)
Biochim. Biophys. Acta
915
149-156
1987
Spinacia oleracea
-
brenda
Croxdale, J.G.; Pappas, T.
Activity of glyceraldehyde-3-phosphate dehydrogenase-NADP in developing leaves of light-grown Dianthus chinensis
Plant Physiol.
84
1427-1430
1987
Dianthus chinensis
brenda
Russo, A.D.; Rullo, R.; Masullo, M.; Ianniciello, G.; Arcari, P.; Bocchini, V.
Glyceraldehyde 3-phosphate dehydrogenase in the hyperthermophilic archaeon Sulfolobus solfataricus: characterization and significance in glucose metabolism
Biochem. Mol. Biol. Int.
36
123-135
1995
Saccharolobus solfataricus
brenda
Iadarola, P.; Bonferoni, C.; Ferri, G.; Stoppini, M.; Zapponi, M.C.
Reversed-phase high-performance liquid chromatographic separation and partial structural characterization of chloroplast glyceraldehyde-3-phosphate dehydrogenase
J. Chromatogr.
359
423-432
1986
Spinacia oleracea
-
brenda
Wolosiuk, R.A.; Hertig, C.M.; Busconi, L.
Activation of spinach chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by concerted hysteresis
Arch. Biochem. Biophys.
246
1-8
1986
Spinacia oleracea
brenda
Ripamonti, F.S.; Sabatino, P.; Zanotti, G.; Scagliarini, S.; Sparla, F.; Trost, P.
Crystal structure of the non-regulatory A(4) isoform of spinach chloroplast glyceraldehyde-3-phosphate dehydrogenase complexed with NADP+
J. Mol. Biol.
314
527-542
2001
Spinacia oleracea
brenda
Maciozek, J.; Anderson, L.E.
Changing kinetic properties of the two-enzyme phosphoglycerate kinase/NADP-linked glyceraldehyde-3-phosphate dehydrogenase couple from pea chloroplast during photosynthetic induction
Biochim. Biophys. Acta
892
185-190
1987
Pisum sativum
-
brenda
Wolosiuk, R.A.; Corley, E.; Crawford, N.A.; Buchanan, B.B.
Dual effects of organic solvents on chloroplast phosphoribulokinase
FEBS Lett.
189
212-216
1985
Spinacia oleracea
-
brenda
Ravid, K.; Lavie, L.; Gershon, D.
The presence of NADPH-glyceraldehyde 3-phosphate oxidoreductase in macrophages
FEBS Lett.
162
107-111
1983
Mus musculus
brenda
Iadarola, P.; Zapponi, M.C.; Ferri, G.
Molecular forms of chloroplast glyceraldehyde-3-P-dehydrogenase
Experientia
39
50-52
1983
Spinacia oleracea
-
brenda
Zapponi, M.C.; Berni, R.; Iadarola, P.; Ferri, G.
Spinach chloroplast glyceraldehyde-3-phosphate dehydrogenase (NADP). Formation of complexes with coenzymes and substrates
Biochim. Biophys. Acta
744
260-264
1983
Spinacia oleracea
-
brenda
Udvardy, J.; Balogh, A.; Farkas, G.L.
Modulation of glyceraldehyde-3-phosphate dehydrogenase in Anacystis nidulans
Arch. Microbiol.
133
2-5
1982
Synechococcus elongatus PCC 7942
-
brenda
Mve Akamba, L.; Anderson, L.E.
Light modulation of glyceraldehyde-3-phosphate dehydrogenase and glucose-6-phosphate dehydrogenase by photosynthetic electron flow in pea chloroplasts
Plant Physiol.
67
197-200
1981
Pisum sativum
brenda
Wara-Aswapati, O.; Kemble, R.J.; Bradbeer, J.W.
Activation of glyceraldehyde-phosphate dehydrogenase (NADP) and phosphoribulokinase in Phaseolus vulgaris leaf extracts involves the dissociation of oligomers
Plant Physiol.
66
34-39
1980
Phaseolus vulgaris
brenda
Horrum, M.A.; Schwartzbach, S.D.
Nutritional regulation of organelle biogenesis in Euglena. Repression of chlorophyl and NADP-glyceraldehyde-3-phosphate dehydrogenase
Plant Physiol.
65
382-386
1980
Euglena gracilis
brenda
Woodrow, S.; Powls, R.
Glyceraldehyde 3-phosphate dehydrogenase of Scenedesmus obliquus. The effect of ATP on the dithiothreitol-promoted induction of NADPH-dependent activity
Arch. Microbiol.
120
177-180
1979
Tetradesmus obliquus
-
brenda
O'Brien, M.J.; Easterby, J.S.; Powls, R.
Algal glyceraldehyde-3-phosphate dehydrogenases. Conversion of the NADH-linked enzyme of Scenedesmus obliquus into a form which preferentially uses NADPH as coenzyme
Biochim. Biophys. Acta
449
209-223
1976
Auxenochlorella pyrenoidosa, Chlamydomonas reinhardtii, Euglena gracilis, no activity in Rhodopseudomonas capsulata, Porphyridium purpureum, Synechococcus elongatus PCC 7942, Tetradesmus obliquus
brenda
O'Brien, M.J.; Easterby, J.S.; Powls, R.
Glyceraldehyde-3-phosphate dehydrogenase of Scenedesmus obliquus. Effects of dithiothreitol and nucleotide on coenzyme specificity
Biochim. Biophys. Acta
481
348-358
1977
Tetradesmus obliquus
brenda
Cerff, R.
Quaternary structure of higher plant glyceraldehyde-3-phosphate dehydrogenases
Eur. J. Biochem.
94
243-247
1979
Hordeum vulgare, Pisum sativum, Spinacia oleracea
brenda
Woodrow, S.; O'Brien, M.J.; Easterby, J.S.; Powls, R.
Glyceraldehyde-3-phosphate dehydrogenase of Scenedesmus obliquus. A kinetic analysis of the effects of nucleotide and dithiothreitol on the production of NADPH-dependent activity
Eur. J. Biochem.
98
425-430
1979
Tetradesmus obliquus
brenda
Lonergan, T.A.; Sargent, M.L.
Regulation of the photosynthesis rhythm in Euglena gracilis. I. Carbonic anhydrase and glyceraldehyde-3-phosphate dehydrogenase do not regulate the photosynthesis rhythm
Plant Physiol.
61
150-153
1978
Euglena gracilis
brenda
Cerff, R.; Chambers, S.E.
Subunit structure of higher plant glyceraldehyde-3-phosphate dehydrogenases (EC 1.2.1.12 and EC 1.2.1.13)
J. Biol. Chem.
254
6094-6098
1979
Hordeum vulgare, Sinapis alba
brenda
Cerff, R.; Chambers, S.E.
Glyceraldehyde-3-phosphate dehydrogenase (NADP) from Sinapis alba L. Isolation and electrophoretic characterization of isoenzymes
Hoppe-Seyler's Z. Physiol. Chem.
359
769-772
1978
Sinapis alba
brenda
Huber, S.C.
Substrates and inorganic phosphate control: the light activation of NADP-glyceraldehyde-3-phosphate dehydrogenase and phosphoribulokinase in barley (Hordeum vulgare) chloroplasts
FEBS Lett.
92
12-16
1978
Hordeum vulgare
-
brenda
Wolosiuk, R.A.; Buchanan, B.B.
Activation of chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by ferredoxin/thioredoxin system
Plant Physiol.
61
669-671
1978
Spinacia oleracea
brenda
Ferri, G.; Comerio, G.; Iadarola, P.; Zapponi, M.C.; Speranza, M.L.
Subunit structure and activity of glyceraldehyde-3-phosphate dehydrogenase from spinach chloroplasts
Biochim. Biophys. Acta
522
19-31
1978
Spinacia oleracea
brenda
Cerff, R.
Glyceraldehyde-3-phosphate dehydrogenase (NADP) from Sinapis alba: steady state kinetics
Phytochemistry
17
2061-2067
1978
Sinapis alba
-
brenda
Zeikus, J.G.; Fuchs, G.; Kenealy, W.; Thauer, R.K.
Oxidoreductases involved in cell carbon synthesis of Methanobacterium thermoautotrophicum
J. Bacteriol.
132
604-613
1977
Methanothermobacter thermautotrophicus
brenda
Ziegler, I.; Marewa, A.; Schoepe, E.
Action of sulphite on the substrate kinetics of chloroplastic NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
Phytochemistry
15
1627-1632
1976
Spinacia oleracea
-
brenda
Yonuschot, G.R.; Ortwerth, B.J.; Koeppe, O.J.
Purification and properties of a nicotinamide adenine dinucleotide phosphate-requiring glyceraldehyde 3-phosphate dehydrogenase from spinach leaves
J. Biol. Chem.
245
4193-4198
1970
Spinacia oleracea
brenda
Cerff, R.
Glyceraldehyde-3-phosphate dehydrogenase (NADP) from Sinapis alba L.
Plant Physiol.
61
369-372
1978
Sinapis alba
brenda
Buchanan, B.B.; Crawford, N.A.; Wolosiuk, R.A.
Ferredoxin/thioredoxin system functions with effectors in activation of NADP-glyceraldehyde 3-phosphate dehydrogenase of barley seedlings
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Hordeum vulgare
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Trost, P.; Scagliarini, S.; Valenti, V.; Pupillo, P.
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Spinacia oleracea
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Scagliarini, S.; Trost, P.; Pupillo, P.; Valenti, V.
Light activation and molecular-mass changes of NAD(P)-glyceraldehyde 3-phosphate dehydrogenase of spinach and maize leaves
Planta
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Spinacia oleracea, Zea mays
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brenda
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Spinacia oleracea