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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
-
4.1.1.39
-
calvin
-
2.7.1.19
-
2.7.2.3
- 1,3-bisphosphoglycerate
-
nad-specific
-
calvin-benson
-
triose-p
- sedoheptulose
- ribulose-5-phosphate
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
glyceraldehyde-3-p dehydrogenase, nadp-glyceraldehyde-3-phosphate dehydrogenase, gapa1, nadp-gapdh, gapa-1, nadp-gpd, glyceraldehyde-3-dehydrogenase, photosynthetic gapdh, ov-gapdh, nadp-dependent gapdh, 
more
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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 GAPDH
NADP-dependent glyceraldehyde phosphate dehydrogenase
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-
-
-
NADP-dependent glyceraldehydephosphate dehydrogenase
-
-
-
-
NADP-G3PDH
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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-
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
-
-
NADP-glyceraldehyde-3-phosphate dehydrogenase
-
-
-
-
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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
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-
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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
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-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NADP+
3-phospho-D-glyceroyl arsenate + NADPH
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-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NADP+
3-phospho-D-glyceroyl arsenate + NADPH
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-
-
-
?
D-glyceraldehyde 3-phosphate + arsenate + NADP+
3-phospho-D-glyceroyl arsenate + NADPH
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-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
?
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
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+
-
-
-
-
?
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
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
?
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
-
-
?
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+
-
optimum stimulation of NADPH-dependent dehydrogenase activity is achieved on incubation of the NADH-specific enzyme with dithiothreitol and NADPH, or dithiothreitol and a 1,3-diphosphoglycerate generating system
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+
-
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+
-
activity with NADP+ is about 50fold higher than that determined for NAD+
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