Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH + H+
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
-
r
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+
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 + 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 + 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
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
additional information
?
-
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+
-
-
-
-
?
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
-
-
?
additional information
?
-
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+
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
additional information
?
-
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+
-
-
-
?
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+
-
-
-
-
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
-
-
?
additional information
?
-
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-mercaptoethanol
-
activation
Br-
-
0.6 M, maximal stimulation
Cl-
-
1.0 M, maximal stimulation
Cl3CCOO-
-
0.24 M, maximal stimulation
ClO4-
-
0.08 M, maximal stimulation
cysteine
-
required for maximal activity
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
-
glutathione
-
required for maximal activity
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
I-
-
0.35 M, maximal stimulation
SCN-
-
0.05 M, maximal stimulation
1,3-diphosphoglycerate

-
stimulates
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

-
activation
ATP
-
activation in absence of NAD+, no activation in presence of NAD+
ATP
-
high concentrations required for stimulation, activation by ATP is unlikely of physiological significance
dithiothreitol

full activation with 50 mM dithiothreitol
dithiothreitol
-
activation
dithiothreitol
-
the role of the reduction of the enzyme in vivo is to increase its sensitivity towards the activator 1,3-bisphosphoglycerate
dithiothreitol
-
activation by dithiothreitol + NADPH
dithiothreitol
-
activation
dithiothreitol
-
activation
dithiothreitol
-
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
NADP+

-
activates
NADP+
-
activation in absence of NAD+, no activation in presence of NAD+
NADPH

-
activation
NADPH
-
activation in absence of NAD+, no activation in presence of NAD+
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
-
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
-
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
-
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
-
complete light activation at 25 W*m-2 photosynthetically active radiation
-
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
-
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
-
additional information
-
complete light activation at 100 W*m-2 photosynthetically active radiation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00041 - 5.8
3-phospho-D-glyceroyl phosphate
0.75 - 0.838
D-glyceraldehyde 3-phosphate
0.21 - 0.77
DL-glyceraldehyde 3-phosphate
additional information
additional information
-
0.00041
3-phospho-D-glyceroyl phosphate

pH 6.5, 70°C
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
0.012
3-phospho-D-glyceroyl phosphate
mutant enzyme T33A, reaction with NADH
0.012
3-phospho-D-glyceroyl phosphate
mutant enzyme T33A/S188A, reaction with NADPH
0.012
3-phospho-D-glyceroyl phosphate
native enzyme A3-GAPDH, reaction with NADH
0.012
3-phospho-D-glyceroyl phosphate
-
mutant B(E362Q)
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
0.015
3-phospho-D-glyceroyl phosphate
-
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
0.016
3-phospho-D-glyceroyl phosphate
-
mutant B(R77A)
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
0.02
3-phospho-D-glyceroyl phosphate
-
GapB, analyzed under oxidizing conditions
0.021
3-phospho-D-glyceroyl phosphate
-
A(plusCTE) mutant, analyzed under reducing conditions
0.022
3-phospho-D-glyceroyl phosphate
-
B(minCTE) mutant
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
30
arsenate

-
-
0.75
D-glyceraldehyde 3-phosphate

pH 9.2, 30°C, reaction with NAD+ or NADP+
0.838
D-glyceraldehyde 3-phosphate
pH 6.5, 70°C
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
0.2
NAD+

-
-
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
0.099
NADH
-
mutant enzyme R197A
0.102
NADH
-
mutant enzyme R82D, pH and temperature not specified in the publication
0.11
NADH
-
mutant enzyme R197E
0.12
NADH
-
wild-type enzyme
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
0.14
NADH
native enzyme A3-GAPDH
0.157
NADH
-
mutant enzyme R82A, pH and temperature not specified in the publication
0.168
NADH
mutant enzyme S188A
0.174
NADH
mutant enzyme T33A
0.184
NADH
mutant enzyme T33A/S188A
0.25
NADH
-
mutant enzyme K128A
0.272
NADH
-
mutant enzyme K128E
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
0.003
NADP+

-
-
0.067
NADP+
pH 7.5, 50°C
0.271
NADP+
pH 6.5, 70°C
0.28
NADP+
-
wild type enzyme, in 50 mM EPPS/NaOH (pH 8.0), 20 mM potassium phosphate, at 60°C
0.002
NADPH

-
-
0.018
NADPH
-
pH 7.7, 30°C, native A4 glyceraldehyde 3-phosphate dehydrogenase
0.019
NADPH
-
B(minCTE) mutant
0.023
NADPH
-
mutant enzyme K128E
0.024
NADPH
-
mutant B(188)A, analyzed under oxidizing conditions
0.024
NADPH
-
mutant B(E362Q)
0.027
NADPH
-
mutant enzyme K128A
0.028
NADPH
-
wild-type enzyme
0.028
NADPH
-
mutant enzyme R197A
0.028
NADPH
-
pH 7.7, 30°C, recombinant A4 glyceraldehyde 3-phosphate dehydrogenase
0.028
NADPH
-
wild type enzyme, pH and temperature not specified in the publication
0.028
NADPH
-
mutant enzyme S195A, pH and temperature not specified in the publication
0.029
NADPH
native enzyme A3-GAPDH
0.03
NADPH
-
GapB, analyzed under reducing conditions
0.035
NADPH
-
mutant enzyme R197E
0.038
NADPH
-
GapB, analyzed under oxidizing conditions
0.043
NADPH
-
A(plusCTE) mutant, analyzed under oxidizing conditions
0.044
NADPH
mutant enzyme T33A
0.046
NADPH
-
mutant B(188)A, analyzed under reducing conditions
0.05
NADPH
mutant enzyme S188A
0.05
NADPH
mutant enzyme T33A/S188A
0.05
NADPH
-
AB-GAPDH, analyzed under oxidizing conditions
0.05
NADPH
-
AB-GAPDH, analyzed under reducing conditions
0.06
NADPH
-
activation by 20 mM dithiothreitol and 0.021 mM 1,3-bisphosphoglycerate
0.065
NADPH
-
A(plusCTE) mutant, analyzed under reducing conditions
0.074
NADPH
pH 6.5, 70°C
0.078
NADPH
-
mutant B(R77A)
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
409
phosphate
pH 6.5, 70°C
additional information
additional information

-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
no Michaelis-Menten kinetics with 1,3-bisphosphoglycerate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
40 - 419
3-phospho-D-glyceroyl phosphate
additional information
additional information
-
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
32
NADH
mutant enzyme S188A
37
NADH
mutant enzyme T33A
40
NADH
-
mutant enzyme K128A
41
NADH
native enzyme A3-GAPDH
41
NADH
-
pH 7.7, 30°C, native A4 glyceraldehyde 3-phosphate dehydrogenase
48
NADH
mutant enzyme T33A/S188A
56
NADH
-
mutant enzyme K128E
71
NADH
-
mutant enzyme R82A, pH and temperature not specified in the publication
104
NADH
-
wild-type enzyme
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
108
NADH
-
mutant enzyme R197A
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
137
NADH
-
mutant enzyme R197E
32
NADPH

mutant enzyme S188A
42
NADPH
mutant enzyme T33A/S188A
52
NADPH
mutant enzyme T33A
61
NADPH
native enzyme A3-GAPDH
161
NADPH
-
mutant enzyme K128E
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
220
NADPH
-
mutant enzyme K128A
220
NADPH
-
mutant enzyme R197E
251
NADPH
-
pH 7.7, 30°C, native A4 glyceraldehyde 3-phosphate dehydrogenase
392
NADPH
-
mutant enzyme R197A
430
NADPH
-
wild-type enzyme
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
additional information
additional information

-
catalytic rate constant 238 s-1, control
-
additional information
additional information
-
catalytic rate constant 289 s-1, 3 microM 3-phospho-D-glyceroyl phosphate, NADPH-dependent activity of GAPDH in the GAPDH/CP12 complex
-
additional information
additional information
-
catalytic rate constant 316 s-1, 160 microM 3-phospho-D-glyceroyl phosphate, NADPH-dependent activity of GAPDH in the GAPDH/CP12 complex
-
additional information
additional information
-
catalytic rate constant 330 s-1, 10 microM thioredoxin, NADPH-dependent activity of GAPDH in the GAPDH/CP12 complex
-
additional information
additional information
-
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
-
additional information
additional information
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
1.11
-
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
13.92
-
NAD+-dependent activity
15.4
-
NADP+-dependent activity
740
-
NADH-enzyme activity
1.101

-
effect of water stress on the activity, rehydration, control, 89.9% of control value, Mironovskaya 808, leaves
1.101
-
effect of water stress on the activity, stress, 1 day, BAP, 89.9% of control value, Mironovskaya 808, leaves
additional information

-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
132000
-
GapA, estimated by gel filtration
148300
sedimentation analysis
15000
-
GAPDH III, gel filtration
150000
-
GAPDH, gel filtration
151000
-
B(minCTE) mutant, estimated by gel filtration
152000
-
native A4 glyceraldehyde 3-phosphate dehydrogenase in complex with the small protein CP12, gel filtration
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
299000
-
GAPDHâCP12âFNR complex, gel filtration
300000
-
GAPDH II, gel filtration
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
37072
-
4 * 37072, recombinant A4 glyceraldehyde 3-phosphate dehydrogenase, MALDI-TOF
37500
-
4 * 37500, calculated from amino acid sequence
37581
4 * 37581, calculated from sequence
37596
x * 37596, calculated from sequence
37611
4 * 37611, laser desorption mass spectrophotometry
39355
-
x * 39355, subunit A, + x * 36225, subunit B, calculation from amino acid sequence
41000
-
4 * 41000, SDS-PAGE
45000
-
4 * 45000, SDS-PAGE
491000
-
wild-type GapB 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
760000
-
oligomer of GAPDH in the presence of NADH, suggesting A8B8 stoichiometry, estimated by gel filtration
155000

-
gel filtration
155000
-
recombinant A4 glyceraldehyde 3-phosphate dehydrogenase, gel filtration
36000

-
4 * 36000, isoenzyme 2, SDS-PAGE
36000
-
A2B2, 2 * 36000 + 2 * 39000, isoenzyme 1, SDS-PAGE
37000

-
x * 43000 + x * 37000, molar ratio of the subunits is 1:1, GAPDH I, SDS-PAGE
37000
-
x * 43000 + x * 37000, SDS-PAGE
37000
-
x * 43000 + x * 37000, excess of the lighter subunit, GAPDH II, SDS-PAGE
37000
-
4 * 37000, GAPDH III, SDS-PAGE
38000

SDS-PAGE
38000
-
SDS-PAGE and immunoblot
38000
-
4 * 38000, SDS-PAGE
38000
-
A2B2, 2 * 38000 + 2 * 42000, isoenzyme 1, SDS-PAGE
38000
-
A2B2, 2 * 38000 + 2 * 39000, isoenzyme 1, SDS-PAGE
38000
-
A2B2, 2 * 38000 + 2 * 40000, isoenzyme I, SDS-PAGE
38000
-
4 * 38000, isoenzyme 2, SDS-PAGE
38000
-
4 * 38000, isoenzyme 2, SDS-PAGE
38000
-
4 * 38000, isoenzyme 2, SDS-PAGE
39000

-
x * 39000, SDS-PAGE
39000
-
4 * 39000, SDS-PAGE
39000
-
A2B2, 2 * 38000 + 2 * 39000, isoenzyme 1, SDS-PAGE
39000
-
A2B2, 2 * 36000 + 2 * 39000, isoenzyme 1, SDS-PAGE
39500

x * 39500, SDS-PAGE
39500
4 * 39500, SDS-PAGE
40000

x * 40000, SDS-PAGE
40000
-
A2B2, 2 * 38000 + 2 * 40000, isoenzyme I, SDS-PAGE
42000

-
1 * 42000, SDS-PAGE
42000
-
A2B2, 2 * 38000 + 2 * 42000, isoenzyme 1, SDS-PAGE
43000

-
x * 43000 + x * 37000, molar ratio of the subunits is 1:1, GAPDH I, SDS-PAGE
43000
-
x * 43000 + x * 37000, SDS-PAGE
43000
-
x * 43000 + x * 37000, excess of the lighter subunit, GAPDH II, SDS-PAGE
520000

-
GapB mutant B(E326Q) in the presence of NADH, compatible with octameric structure, estimated by gel filtration
520000
-
GapB mutant B(R77A) in the presence of NADH, compatible with octameric structure, estimated by gel filtration
600000

-
equilibrium sedimentation
600000
-
GAPDH I, gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
heterotetramer
fully active enzyme
monomer
-
1 * 42000, SDS-PAGE
?

x * 40000, SDS-PAGE
?
x * 37596, calculated from sequence
?
-
x * 38000, SDS-PAGE
-
?
-
x * 43000 + x * 37000, molar ratio of the subunits is 1:1, GAPDH I, SDS-PAGE
?
-
x * 43000 + x * 37000, SDS-PAGE
?
-
x * 43000 + x * 37000, excess of the lighter subunit, GAPDH II, SDS-PAGE
?
-
x * 39355, subunit A, + x * 36225, subunit B, calculation from amino acid sequence
homotetramer

-
4 * 36700, about, mass spectrometry, 4 * 47000, SDS-PAGE
homotetramer
-
4 * 38000, SDS-PAGE
homotetramer
-
4 * 37500, calculated from amino acid sequence
tetramer

-
-
tetramer
-
4 * 36854, native A4 glyceraldehyde 3-phosphate dehydrogenase, MALDI-TOF
tetramer
-
4 * 37072, recombinant A4 glyceraldehyde 3-phosphate dehydrogenase, MALDI-TOF
tetramer
-
4 * 36000, isoenzyme 2, SDS-PAGE
tetramer
-
A2B2, 2 * 36000 + 2 * 39000, isoenzyme 1, SDS-PAGE
tetramer
-
4 * 45000, SDS-PAGE
tetramer
-
A2B2, 2 * 38000 + 2 * 42000, isoenzyme 1, SDS-PAGE
tetramer
-
4 * 38000, isoenzyme 2, 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 * 41000, SDS-PAGE
tetramer
4 * 39500, SDS-PAGE
tetramer
4 * 37581, calculated from sequence
tetramer
4 * 37611, laser desorption mass spectrophotometry
tetramer
-
A2B2, 2 * 38000 + 2 * 39000, isoenzyme 1, SDS-PAGE
tetramer
-
4 * 38000, isoenzyme 2, SDS-PAGE
tetramer
-
4 * 37000, GAPDH III, SDS-PAGE
tetramer
-
A2B2, 2 * 38000 + 2 * 40000, isoenzyme I, SDS-PAGE
tetramer
-
4 * 38000, isoenzyme 2, SDS-PAGE
tetramer
-
4 * 39000, 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
-
subunit A and B are very similar in primary sequence
additional information
-
-
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
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
A(plusCTE)
-
chimeric mutant for testing the regulatory function of CTE
B(E326Q)
-
site specific mutant of the GAPDH B-subunit
B(minCTE)
-
deletion mutant for testing the regulatory function of CTE
B(R77A)
-
site specific mutant of the GAPDH B-subunit
B(S188A)
-
site specific mutant of the GAPDH B-subunit
C18S
-
mutant of GapB subunit still shows stron redox regulation
C274S
-
mutant of GapB subunit still shows stron redox regulation
C285S
-
mutant of GapB subunit still shows stron redox regulation
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+
D351N
the mutation only marginally affects the redox sensitivity
E356Q
the mutation only marginally affects the redox sensitivity
E356Q/E357Q
complete redox insensitivity is achieved in the double mutant
E357Q
the mutation only marginally affects the redox sensitivity
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.