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Information on EC 1.2.1.9 - glyceraldehyde-3-phosphate dehydrogenase (NADP+)
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EC Tree
1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP+)Specify your search results
Word Map
- 1.2.1.9
-
groes
- chaperonins
-
refolding
- atpase
-
heat-shock
-
co-chaperonins
- rhodanese
- groel-groes
- chloroplast
-
heptameric
-
tubulins
-
double-ring
-
encapsulate
-
misfolded
-
machine
- malate
-
anti-hsp60
-
equatorial
-
t-complex
- rubisco
-
cage
-
toroid
- mg-atp
-
co-chaperone
-
cryo-electron
-
endosymbiotic
-
chlamydial
- amp-pnp
-
atp-induced
-
aphid
-
endosymbionts
-
molten
-
hetero-oligomeric
-
coarse-grained
-
protein-folding
-
back-to-back
-
nonnative
-
trachomatis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
triosephosphate dehydrogenase, non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase, apo-gapdh, gap dehydrogenase, np-ga3pdhase, apo-glyceraldehyde-3-phosphate dehydrogenase, nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase, np-gapdh, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, gapdhn, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
apo-glyceraldehyde-3-phosphate dehydrogenase
-
-
GAP dehydrogenase
GAPDH
GAPDHN
GAPN
glyceraldehyde 3-phosphate:NADP+ reductase, non-phosphorylating
glyceraldehyde-3-phosphate dehydrogenase
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
NADP-dependent nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
-
NADPH-dependent GAPDH
non phosphorylating glyceraldehyde-3-phosphate dehydrogenase
non-phosphorylating GAP dehydrogenase
non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase
non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase GAPN
-
-
non-phosphorylating NADP+-dependent glyceraldehyde-3-phosphate dehydrogenase
-
-
non-phosphorylating NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
-
-
nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase
nonphosphorylating NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
-
-
NP-Ga3PDHase
SSO3194
St-GAPN
STK_24770
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
-
-
non phosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
non phosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
non phosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
non phosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
non phosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-glyceraldehyde 3-phosphate + NADP+ + H2O = 3-phospho-D-glycerate + NADPH + 2 H+
two-step mechanism and kinetics
-
D-glyceraldehyde 3-phosphate + NADP+ + H2O = 3-phospho-D-glycerate + NADPH + 2 H+
proposed mechanism
-
D-glyceraldehyde 3-phosphate + NADP+ + H2O = 3-phospho-D-glycerate + NADPH + 2 H+
probably identical with EC 1.2.1.13
-
D-glyceraldehyde 3-phosphate + NADP+ + H2O = 3-phospho-D-glycerate + NADPH + 2 H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate:NADP+ oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
9028-92-6
-
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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-glycerate + NADH + H+
D-glyceraldehyde 3-phosphate + NAD+ + H2O
-
-
-
r
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADP+ + H+
-
-
ir
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
r
D-glyceraldehyde-3-phosphate + 1,N6-ethenoadenine-nicotinamide dinucleotide phosphate
D-3-phosphoglycerate + ?
-
-
-
?
D-glyceraldehyde-3-phosphate + 3-acetylpyridine-adenine dinucleotide phosphate
D-3-phosphoglycerate + ?
-
-
-
?
D-glyceraldehyde-3-phosphate + beta-nicotinamide adenine dinucleotide 2',3'-cyclic monophosphate
D-3-phosphoglycerate + ?
-
-
-
?
D-glyceraldehyde-3-phosphate + nicotinamide-hypoxanthine dinucleotide phosphate
D-3-phosphoglycerate + ?
-
-
-
?
DL-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
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+
-
-
-
?
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + 2 H+
the enzyme prefers NADP+ to NAD+. NAD+ is a poor cosubstrate. The NAD+-dependent reaction of St-GAPN shows no saturation up to 20 mM
-
ir
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + 2 H+
the enzyme prefers NADP+ to NAD+. NAD+ is a poor cosubstrate. The NAD+-dependent reaction of St-GAPN shows no saturation up to 20 mM
-
ir
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + H+
-
-
-
r
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + H+
enzyme shows negligible activity with NAD+. The NAD+-dependent reaction shows no saturation at NAD+ concentrations up to 50 mM. The highest enzyme activity is observed at 50 mM NAD+ which is 7fold to 8fold lower than the Vmax observed using NADP+ as cofactor
-
ir
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + H+
NAD+ is a poor co-substrate
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase is a key-enzyme of the semi-phosphorylative branch of the Entner–Doudoroff pathway
-
ir
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
-
-
r
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
-
-
ir
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
the enzyme prefers NADP+ to NAD+. NAD+ is a poor cosubstrate. The NAD+-dependent reaction of St-GAPN shows no saturation up to 20 mM. K-type allosterism in which the positive cooperativity is abolished with concomitant activation by D-glucose 1-phosphate
-
ir
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
-
-
ir
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
the enzyme prefers NADP+ to NAD+. NAD+ is a poor cosubstrate. The NAD+-dependent reaction of St-GAPN shows no saturation up to 20 mM. K-type allosterism in which the positive cooperativity is abolished with concomitant activation by D-glucose 1-phosphate
-
ir
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
ir
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
ir
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
ir
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
ir
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
ir
D-glyceraldehyde-3-phosphate + NAD+
D-3-phosphoglycerate + NADH + H+
weak reaction
-
ir
D-glyceraldehyde-3-phosphate + NAD+
D-3-phosphoglycerate + NADH + H+
weak reaction
-
ir
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
-
-
ir
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
-
-
?
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
-
-
?
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
-
-
ir
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
-
-
ir
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
-
-
ir
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
absolutely specific for D-isomer
-
ir
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
may be part of a system that is responsible for the export of photosynthetically generated NADPH from chloroplast to cytoplasm
-
ir
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
-
-
?
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
-
-
ir
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
-
-
ir
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
two-step mechanism
-
ir
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
rate-limiting step in wild-type enzyme and in mutant enzymes R124L, and Y170F is deacylation. Rate limiting step in mutant enzymes R301L and R459I is acylation
-
?
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
-
-
?
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
-
-
r
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
-
-
r
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
-
-
?
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
-
-
?
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
-
?
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH + H+
-
-
ir
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH + H+
-
-
ir
DL-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-DL-glycerate + NADH + H+
NADP+ is much more efficient than NAD+
-
ir
DL-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-DL-glycerate + NADH + H+
NADP+ is much more efficient than NAD+
-
ir
DL-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-DL-glycerate + NADPH + H+
-
-
ir
DL-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-DL-glycerate + NADPH + H+
-
-
ir
DL-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-DL-glycerate + NADPH + H+
-
-
-
?
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
?
additional information
?
-
-
the enzyme shows only negligible activity with NAD+
-
?
additional information
?
-
the enzyme shows only negligible activity with NAD+
-
?
additional information
?
-
the enzyme shows only negligible activity with NAD+
-
?
additional information
?
-
the enzyme shows only negligible activity with NAD+
-
?
additional information
?
-
the enzyme shows only negligible activity with NAD+
-
?
additional information
?
-
the enzyme shows only negligible activity with NAD+
-
?
additional information
?
-
the enzyme shows only negligible activity with NAD+
-
?
additional information
?
-
-
the enzyme does not react with formaldehyde, acetaldehyde, propionaldehyde, butylaldehyde, valeraldehyde, caproaldehyde, betaine aldehyde, glycolaldehyde, succinic semialdehyde or glyceraldehyde
-
?
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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+
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + H+
NAD+ is a poor co-substrate
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADP+ + H+
-
-
-
ir
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
r
DL-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-DL-glycerate + NADPH + H+
-
-
-
-
?
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+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase is a key-enzyme of the semi-phosphorylative branch of the Entner–Doudoroff pathway
-
-
ir
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
-
-
-
r
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
-
-
-
ir
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
-
-
-
ir
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
ir
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
-
-
-
ir
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
-
-
-
?
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
-
-
-
ir
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
-
-
-
ir
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
may be part of a system that is responsible for the export of photosynthetically generated NADPH from chloroplast to cytoplasm
-
-
ir
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
-
-
-
-
ir
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
?
additional information
?
-
-
the enzyme does not react with formaldehyde, acetaldehyde, propionaldehyde, butylaldehyde, valeraldehyde, caproaldehyde, betaine aldehyde, glycolaldehyde, succinic semialdehyde or glyceraldehyde
-
-
?
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+
enzyme shows negligible activity with NAD+. The NAD+-dependent reaction of Sso-GAPN shows no saturation at NAD+ concentrations up to 50 mM. The highest enzyme activity is observed at 50 mM NAD+ which is 7fold to 8fold lower than the Vmax observed using NADP+ as cofactor
NAD+
-
enzyme activity is observed with both NAD+ and NADP+, but NADP+ is the preferred cofactor
NADP+
prefers NADP+ more than NAD+ as cofactor
NADP+
the enzyme shows only negligible activity with NAD+ compared to the physiological cosubstrate NADP+
NADP+
-
enzyme activity is observed with both NAD+ and NADP+, but NADP+ is the preferred cofactor
NADP+
the enzyme prefers NADP+ to NAD+. NAD+ is a poor co-substrate
NADP+
-
effect of NADP+ on the thermostability and the irreversible thermal denaturation of the nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans. The enzyme-NADP+ binary complex shows a strongly decreased thermal stability, with a difference of about 20°C between the temperatures of the thermal transition peak maxima of the complex and the free protein. Single amino acid substitution, known to abolish the NADP+ binding, cancelled the calorimetric effect of the coenzyme
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
MgCl2
-
phosphorylated enzyme present in heterotrophic cells is activated up to 3fold, no effect with the non-phosphorylated enzyme from leaves. MgCl2 disrupts the interaction between the enzyme and a 14-3-3 regulatory protein
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
chloroplast protein CP12
-
the chloroplast protein CP12 behaves as a negative regulator of GAPDH activity
-
diphosphate
-
after interaction with the 14-3-3 regulatory protein the phosphorylated enzyme exhibits higher sensitivity to inhibition
galactonate
slight inhibition; slight inhibition (1.2 to 1.3fold); slight inhibition (1.2 to 1.3fold)
hydrazin
-
protonated and neutral form, compete with the attacking water molecule for the binding site E268, inhibition mechanism
hydroxylamine
-
protonated and neutral form, compete with the attacking water molecule for the binding site E268, inhibition mechanism
ATP
-
after interaction with the 14-3-3 regulatory protein the phosphorylated enzyme exhibits higher sensitivity to inhibition
Diamide
-
the inhibition with diamide is reversed by addition of dithiothreitol
Diamide
-
sensitive to inactivation by diamide, inactivation is protected by D-glyceraldehyde 3-phosphate (with no effect by NADP+) and it is completely reversed by 2-mercaptoethanol
L-Glyceraldehyde 3-phosphate
-
competitive below 0.04 mM, non-competitive above 0.075 mM
Mg2+
-
near 75% of the activity is lost when 5 mM Mg2+ is included in the incubation medium
Mg2+
-
near 75% of the activity is lost when 5 mM Mg2+ is included in the incubation medium
NADPH
-
NADPH causes a large inhibition in enzyme activity even at very low concentrations (0.01-0.02?mM)
NADPH
-
under oxidized conditions, NADPH causes a large inhibition in enzyme activity even at very low concentrations (0.01-0.02 mM)
additional information
-
glyceraldehyde and ADP have no effect on GAPN activity; not inhibited by glyceraldehyde and ADP; not inhibited by glyceraldehyde and ADP
-
additional information
glyceraldehyde and ADP have no effect on GAPN activity; not inhibited by glyceraldehyde and ADP; not inhibited by glyceraldehyde and ADP
-
additional information
glyceraldehyde and ADP have no effect on GAPN activity; not inhibited by glyceraldehyde and ADP; not inhibited by glyceraldehyde and ADP
-
additional information
glyceraldehyde and ADP have no effect on GAPN activity; not inhibited by glyceraldehyde and ADP; not inhibited by glyceraldehyde and ADP
-
additional information
-
no effect: ADP, AMP, D-glucose 6-phosphate and D-galactose 1-phosphate
-
additional information
no effect: ADP, AMP, D-glucose 6-phosphate and D-galactose 1-phosphate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6-O-phosphono-D-fructofuranose
minor stimulatory effect
D-fructose 6-phosphate
a slight increase in enzyme activity is observed in the presence of D-fructose 6-phosphate and coenzyme A (1.1fold)
D-glucose 1-phosphate
14fold activation at 0.1 mM D-glucose 1-phosphate
D-glucose 1-phosphate
activates. Activation follows an increase in maximum velocity rather than in affinity glyceraldehyde-3-phosphate
D-glucose 1-phosphate
activates. Activation follows an increase in affinity for glyceraldehyde-3-phosphate rather than an increase in maximum velocity
D-glucose 1-phosphate
activity increases by 1.4fold with increasing D-glucose 1-phosphate concentration from 0 to 0.1 mM. The enzyme shows K-type allosterism in which the positive cooperativity is abolished with concomitant activation by glucose 1-phosphate
D-glucose 1-phosphate
D-glucose 1-phosphate does not influence the affinity for DL-glyceraldehyde-3-phosphate; but increases the turnover severalfold
methyl viologen
-
the specific activity of the enzyme increases up to 2fold after oxidative conditions imposed by methylviologen, expression of NP-Ga3PDHase in plants is induced by high treatments with methyl viologen
methyl viologen
-
the specific activity of the enzyme increases up to 2fold after oxidative conditions imposed by methylviologen, expression of NP-Ga3PDHase in plants is induced by high treatments with methyl viologen
NADP+
-
there is a 1.5fold increase of enzyme activity with NADP+ at concentrations higher than 0.5 mM
NADP+
-
there is a small increase of enzyme activity with NADP+ at concentrations higher than 0.5 mM
NADP+
-
there is a small increase of enzyme activity with NADP+ at concentrations higher than 0.5 mM
additional information
gapN transcription is enhanced by the catabolite control protein A, CcpA
-
additional information
-
ATP, ADP, AMP, D-glucose 6-phosphate and galactose 1-phosphate exhibit no effect on enzyme activity
-
additional information
ATP, ADP, AMP, D-glucose 6-phosphate and galactose 1-phosphate exhibit no effect on enzyme activity
-
additional information
-
only slightly activated by light, dithiothreitol and ATP
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.015
3-phospho-D-glyceroyl phosphate
-
GapB, analyzed under reducing conditions
0.019
3-phospho-D-glyceroyl phosphate
-
A(plusCTE) mutant, analyzed under oxidizing conditions
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
0.024
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
0.101
D-Glyceraldehyde-3-phosphate
enzyme from leaf before or after treatment with alkaline phosphatase
0.118
D-Glyceraldehyde-3-phosphate
enzyme from endosperm before or after treatment with alkaline phosphatase
0.51
D-Glyceraldehyde-3-phosphate
in 90 mM HEPES/KOH, 160 mM KCl, pH 7.0, at 70°C
0.501
DL-glyceraldehyde 3-phosphate
in the presence of D-glucose 1-phosphate
0.51
DL-glyceraldehyde 3-phosphate
70°C, pH 7
0.51
DL-glyceraldehyde 3-phosphate
in the absence of D-glucose 1-phosphate
17.2
NAD+
mutant enzyme A198S/S199I, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
17.4
NAD+
in 90 mM HEPES/KOH, 160 mM KCl, pH 7.0, at 70°C
17.4
NAD+
in the absence of D-glucose 1-phosphate
18.9
NAD+
wild type enzyme, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
19.4
NAD+
mutant enzyme, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
21.1
NAD+
in the presence of D-glucose 1-phosphate
25.8
NAD+
mutant enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
26.4
NAD+
wild type enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
29.3
NAD+
mutant enzyme A198S/S199I, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
0.0222
NADP+
mutant enzyme A198S/S199I, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
0.0231
NADP+
wild type enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
0.0263
NADP+
mutant enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
0.034
NADP+
enzyme from leaf before treatment with alkaline phosphatase
0.04
NADP+
enzyme from endosperm before treatment with alkaline phosphatase
0.04
NADP+
enzyme from leaf after treatment with alkaline phosphatase
0.06
NADP+
enzyme from endosperm after treatment with alkaline phosphatase
0.09
NADP+
in 90 mM HEPES/KOH, 160 mM KCl, pH 7.0, at 70°C
0.09
NADP+
in the absence or presence of D-glucose 1-phosphate
0.0901
NADP+
wild type enzyme, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
0.0979
NADP+
mutant enzyme A198S/S199I, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
0.187
NADP+
mutant enzyme, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
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
0.202
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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.13
D-glyceraldehyde 3-phosphate
pH 8.0, 60°C, mutant enzyme Y139R
117
D-glyceraldehyde 3-phosphate
pH 8.0, 60°C, mutant enzyme R136K
161
D-glyceraldehyde 3-phosphate
pH 8.0, 60°C, mutant enzyme E141D
257
D-glyceraldehyde 3-phosphate
pH 8.0, 60°C, mutant enzyme L138T
297
D-glyceraldehyde 3-phosphate
pH 8.0, 60°C, mutant enzyme K137E
341
D-glyceraldehyde 3-phosphate
pH 8.0, 60°C, wild-type enzyme
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
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.378
NAD+
wild type enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
0.434
NAD+
mutant enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
0.637
NAD+
wild type enzyme, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
0.639
NAD+
mutant enzyme, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
1
NAD+
mutant enzyme A198S/S199I, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
1.63
NAD+
mutant enzyme A198S/S199I, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
48.1
NADP+
mutant enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
61.5
NADP+
mutant enzyme A198S/S199I, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
71.4
NADP+
mutant enzyme, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
96.6
NADP+
wild type enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
188
NADP+
mutant enzyme A198S/S199I, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
203
NADP+
wild type enzyme, in the presence of 0.01 mM D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
36.5
D-glyceraldehyde 3-phosphate
-
in 100 mM MES/KOH (pH 7.0), at 70°C
0.6
sodium nitroprusside
-
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.001
growth stage: growth cessation, microM NADP+ reduced min-1 (mg of cell-N)-1
0.008
growth stage: just before the cessation of growth, microM NADP+ reduced min-1 (mg of cell-N)-1
0.011
0.014
0.015
0.016
0.028
0.032
growth stage: middle log growth, microM NADP+ reduced min-1 (mg of cell-N)-1
0.033
0.039
0.04
0.065
additional information
0.011
growth stage: later log growth, microM NADP+ reduced min-1 (mg of cell-N)-1
0.014
strain 12U1-ccpA-, energy substrate glucose, microM NADP+ reduced min-1 (mg of cell-N)-1
0.014
strain 12U1-ccpA-, energy substrate glucose, microM NADP+ reduced min-1 (mg of cellular nitrogen)-1
0.015
strain 12U1-ccpA-, energy substrate lactose, microM NADP+ reduced min-1 (mg of cell-N)-1
0.015
strain 12U1-ccpA-, energy substrate lactose, microM NADP+ reduced min-1 (mg of cellular nitrogen)-1
0.016
strain 12U1, energy substrate lactose, microM NADP+ reduced min-1 (mg of cell-N)-1
0.016
strain 12U1, energy substrate lactose, microM NADP+ reduced min-1 (mg of cellular nitrogen)-1
0.028
strain 12IU1p, energy substrate glucose, microM NADP+ reduced min-1 (mg of cellular nitrogen)-1
0.033
strain 12U1, energy substrate glucose, microM NADP+ reduced min-1 (mg of cell-N)-1
0.033
strain 12U1, energy substrate glucose, microM NADP+ reduced min-1 (mg of cellular nitrogen)-1
0.039
recombinant GAPN overexpression strain 12U1gapN-1, energy substrate glucose, microM NADP+ reduced min-1 (mg of cellular nitrogen)-1
0.039
strain 12U1gapN-1, microM NADP+ reduced min-1 (mg of cell-N)-1
0.065
recombinant GAPN overexpression strain 12U1gapN-2, energy substrate glucose, microM NADP+ reduced min-1 (mg of cellular nitrogen)-1
0.065
strain 12U1gapN-2, microM NADP+ reduced min-1 (mg of cell-N)-1
additional information
-
0 for mutant np-gapdh, deficient in NP-GAPDH expression
additional information
-
the recombinant enzyme has a specific activity of 3.74 U/mg
additional information
the recombinant enzyme has a specific activity of 3.74 U/mg
additional information
the recombinant enzyme has a specific activity of 3.74 U/mg
additional information
the recombinant enzyme has a specific activity of 3.74 U/mg
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.9
8 - 9
8.2
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8 - 8.5
-
at pH 6.8: 19% of maximal activity, at pH 8.5: 92% of maximal activity
7.5 - 12
-
pH 7.5: about 35% of maximal activity, pH 12.0: about 60% of maximal activity
additional information
-
steady-state rate constant for mutant E268Q and E268A is pH-dependent
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
60
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Streptococcus bovis gapN, sequence of gapN gene of S. mutans and S. pyogenes used for PCR primer design, Q59931, Q99Z67
SwissProt
brenda
PCC 7942, enzyme not clearly distinctable from chloroplastidic from, EC 1.2.1.12
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
aqueous phase of latex after centrifugation at 38000 x g
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
DELTAgapN cells do not grow under glycolytic conditions
malfunction
-
single amino acid substitution, known to abolish the NADP+ binding, cancelled the calorimetric effect of the coenzyme NADP+
metabolism
-
replacement of Escherichia coli GapA glyceraldehyde 3-phosphate dehydrogenase, EC 1.2.1.12 by Clostridium acetobutylicum GapC glyceraldehyde 3-phosphate dehydrogenase, EC 1.2.1.9 results in significant reduction of flux through the pentose phosphate pathway. Recombinant strains display increased NADPH availability, and consistently higher productivity than parent strains
metabolism
-
the enzyme plays a key role in providing NADPH under glycolytic conditions
metabolism
the EMP pathway can be controlled through the glyceraldehyde 3-phosphate node by NAD+-GAPDH activity, recombinant NADP+-GAPDH heterologous activity can also exert a similar response, which modulates the glucose uptake and also the acetic acid production rate
physiological function
when endogenous phosphorylating NAD-dependent glyceraldehyde-3-phosphate dehydrogenase (GAPDH) of Corynebacterium glutamicum is replaced by nonphosphorylating NADP-dependent glyceraldehyde-3-phosphate dehydrogenase (GapN) from Clostridium acetobutylicum, this NADPH-generating glycolytic pathway does not allow for the growth of Corynebacterium glutamicum with glucose as the sole carbon source. Heterologous expression of udhA encoding soluble transhydrogenase from Escherichia coli partly restores growth
physiological function
-
the enzyme is known to be crucial for the effective supply of the reducing equivalents in Streptococcus mutans and its ability to grow under aerobic conditions
Show AA Sequence and Transmembrane Helices (888 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
189000
190000 - 200000
230000
232000
-
GapB mutant B(E326Q) in the presence of NADPH, estimated by gel filtration
240000
native enzyme independent of phosphorylation state, 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
52000
520000
53000
55000
553000
-
GapB mutant B(S188A) in the presence of NADH, compatible with octameric structure, estimated by gel filtration
56400
56930
subunit, calculated from amino acid sequence
57000
760000
-
oligomer of GAPDH in the presence of NADH, suggesting A8B8 stoichiometry, estimated by gel filtration
189000
-
tetrameric conformation of GAPDH-A2B2 stabilized by NADPH, estimated by gel filtration
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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
tetramer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
reversible phosphorylation can regulate NADPH production in the cytosol of heterotrophic plant cells, the phosphorylated enzyme form has similar affinity for substrate but significant lower maximal velocity
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method, from 2-methyl-2,4-pentanediol and magnesium acetate solution
-
the structure of the thioacylenzyme intermediate is solved at a resolution of 2.55 A
the structure of NADP-dependent 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
-
hanging-drop vapour-diffusion method, ammonium sulfate as a precipitant, comparison of crystal structure of NADP+-dependent cytosolic and chloroplastic enzymes and NAD+-dependent enzymes
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
C302A
-
compared to wild-type enzyme the amount of the thermolabile species is higher
E268A
E268Q
-
attacking water molecule in the hydrolysis process is poorly activated, can be overcome by the nulceophiles hydrazin and hydroxylamine
N169T
-
compared to wild-type enzyme the amount of the thermolabile species is significantly lower
R124L
-
turnover number is 21fold lower than turnover-number of wild-type enzym
R301L
-
turnover number is 1000fold lower than turnover-number of wild-type enzyme. Rate limiting step is acylation, compared to deacylation in wild-type enzyme
R459I
T195G
-
compared to wild-type enzyme the amount of the thermolabile species is similar
Y170F
-
turnover number is 1.7fold higher than turnover-number of wild-type enzyme
A198S/S199I
E141D
kcat for D-glyceraldehyde 3-phosphate is 2.1fold lower than wild-type value
K137E
kcat for D-glyceraldehyde 3-phosphate is 1.1fold lower than wild-type value
L138T
kcat for D-glyceraldehyde 3-phosphate is 1.3fold lower than wild-type value
R136K
kcat for D-glyceraldehyde 3-phosphate is 2.8fold lower than wild-type value
S199I
Y139R
kcat for D-glyceraldehyde 3-phosphate is 302fold lower than wild-type value. The mutant enzyme no longer displays a sigmoidal K-type-like allostery but instead has apparent V-type allostery similar to that of the Sulfolobus solfataricus enzyme, suggesting that the residue located in the center of the homotetramer critically contributes to the allosteric behavior
A198S/S199I
-
the catalytic efficiency with NADP+ decreases while that with NAD+ increases by 2.5fold. Substitutions reduces the NADP/NAD preference ratio by more than 50%
E141D
-
kcat for D-glyceraldehyde 3-phosphate is 2.1fold lower than wild-type value
K137E
-
kcat for D-glyceraldehyde 3-phosphate is 1.1fold lower than wild-type value
L138T
-
kcat for D-glyceraldehyde 3-phosphate is 1.3fold lower than wild-type value
R136K
-
kcat for D-glyceraldehyde 3-phosphate is 2.8fold lower than wild-type value
S199I
-
the catalytic efficiency (kcat/Km) with NADP+ decreases by 0.5fold while that with NAD+ remains unchanged. Substitution reduces the NADP/NAD preference ratio by more than 50%
additional information
E268A
-
attacking water molecule in the hydrolysis process is poorly activated, can be overcome by the nulceophiles hydrazin and hydroxylamine
E268A
-
compared to wild-type enzyme the amount of the thermolabile species is significantly lower
R459I
-
compared to wild-type enzyme the amount of the thermolabile species is significantly lower
R459I
-
turnover number is 214fold lower than turnover-number of wild-type enzyme. Rate limiting step is acylation, compared to deacylation in wild-type enzyme
A198S/S199I
the catalytic efficiency with NADP+ decreases while that with NAD+ increases by 2.5fold. Substitutions reduces the NADP/NAD preference ratio by more than 50%
A198S/S199I
the mutant shows reduced catalytic efficiency with NADP+ and increased catalytic efficiency with NAD+ as compared to the wild type enzyme
S199I
the catalytic efficiency (kcat/Km) with NADP+ decreases by 0.5fold while that with NAD+ remains unchanged. Substitution reduces the NADP/NAD preference ratio by more than 50%
S199I
the mutant shows reduced catalytic efficiency with NADP+ and increased catalytic efficiency with NAD+ as compared to the wild type enzyme
additional information
-
replacement of Escherichia coli GapA glyceraldehyde 3-phosphate dehydrogenase, EC 1.2.1.12 by Clostridium acetobutylicum GapC glyceraldehyde 3-phosphate dehydrogenase, EC 1.2.1.9 results in significant reduction of flux through the pentose phosphate pathway. Recombinant strains display increased NADPH availability, and consistently higher productivity than parent strains
additional information
in non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Sulfolobus tokodaii, D-glucose 1-phosphate-induced activation follows an increase in affinity for glyceraldehyde-3-phosphate rather than an increase in maximum velocity, whereas in the enzyme from Sulfolobus solfataricus, D-glucose 1-phosphate-induced activation follows an increase in maximum velocity rather than in affinity for glyceraldehyde-3-phosphate. To explore the molecular basis of this difference 14 mutants and 2 chimeras are generated. The analyses of chimeric enzymes generated from regions of the Sulfolobus tokodaii enzyme and the Sulfolobus solfataricus enzyme indicates that a 57-residue module located in the subunit interface is involved in their allosteric behavior
additional information
-
in non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Sulfolobus tokodaii, D-glucose 1-phosphate-induced activation follows an increase in affinity for glyceraldehyde-3-phosphate rather than an increase in maximum velocity, whereas in the enzyme from Sulfolobus solfataricus, D-glucose 1-phosphate-induced activation follows an increase in maximum velocity rather than in affinity for glyceraldehyde-3-phosphate. To explore the molecular basis of this difference 14 mutants and 2 chimeras are generated. The analyses of chimeric enzymes generated from regions of the Sulfolobus tokodaii enzyme and the Sulfolobus solfataricus enzyme indicates that a 57-residue module located in the subunit interface is involved in their allosteric behavior
additional information
-
in non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Sulfolobus tokodaii, D-glucose 1-phosphate-induced activation follows an increase in affinity for glyceraldehyde-3-phosphate rather than an increase in maximum velocity, whereas in the enzyme from Sulfolobus solfataricus, D-glucose 1-phosphate-induced activation follows an increase in maximum velocity rather than in affinity for glyceraldehyde-3-phosphate. To explore the molecular basis of this difference 14 mutants and 2 chimeras are generated. The analyses of chimeric enzymes generated from regions of the Sulfolobus tokodaii enzyme and the Sulfolobus solfataricus enzyme indicates that a 57-residue module located in the subunit interface is involved in their allosteric behavior
additional information
the gapA gene, UniProt ID P0A9B2, EC 1.2.1.12, from Escherichia coli strain MG1655 is replaced by the gene gapN from Streptococcus mutans. The specific NADP+-GAPDH activity of the strain MG1655DgapA::gapN is 4.6times lower relative to strain MG1655DELTAgapA::gapN/pTrcgapN and no NAD+-GAPDH activity is detected. The specific NADP+-GAPDH activity levels in the derivative strain reveal that growth rate and glucose uptake differences are attributable to gapN expression level. The NADH/NAD+ ratio in the strain MG1655DELTAgapA::gapN/pTrcgapN decreases by 25% as compared to wild-type strain. In contrast, the NADPH/NADP+ ratio increases 2times indicating that the alteration in the turnover of NAD(P)H via glyceraldehyde 3-phosphate oxidation affects the redox levels of the strain MG1655DELTAgapA::gapN/pTrcgapN, which increases 2.8times the NADPH/NADH ratio
additional information
in non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Sulfolobus tokodaii, D-glucose 1-phosphate-induced activation follows an increase in affinity for glyceraldehyde-3-phosphate rather than an increase in maximum velocity, whereas in the enzyme from Sulfolobus solfataricus, D-glucose 1-phosphate-induced activation follows an increase in maximum velocity rather than in affinity for glyceraldehyde-3-phosphate. To explore the molecular basis of this difference 14 mutants and 2 chimeras are generated. The analyses of chimeric enzymes generated from regions of the Sulfolobus tokodaii enzyme and the Sulfolobus solfataricus enzyme indicates that a 57-residue module located in the subunit interface is involved in their allosteric behavior
additional information
-
in non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Sulfolobus tokodaii, D-glucose 1-phosphate-induced activation follows an increase in affinity for glyceraldehyde-3-phosphate rather than an increase in maximum velocity, whereas in the enzyme from Sulfolobus solfataricus, D-glucose 1-phosphate-induced activation follows an increase in maximum velocity rather than in affinity for glyceraldehyde-3-phosphate. To explore the molecular basis of this difference 14 mutants and 2 chimeras are generated. The analyses of chimeric enzymes generated from regions of the Sulfolobus tokodaii enzyme and the Sulfolobus solfataricus enzyme indicates that a 57-residue module located in the subunit interface is involved in their allosteric behavior
additional information
-
in non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Sulfolobus tokodaii, D-glucose 1-phosphate-induced activation follows an increase in affinity for glyceraldehyde-3-phosphate rather than an increase in maximum velocity, whereas in the enzyme from Sulfolobus solfataricus, D-glucose 1-phosphate-induced activation follows an increase in maximum velocity rather than in affinity for glyceraldehyde-3-phosphate. To explore the molecular basis of this difference 14 mutants and 2 chimeras are generated. The analyses of chimeric enzymes generated from regions of the Sulfolobus tokodaii enzyme and the Sulfolobus solfataricus enzyme indicates that a 57-residue module located in the subunit interface is involved in their allosteric behavior
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
additional information
additional information
-
phosphate binds to the enzyme, resulting in the formation of a GAPN-phosphate binary complex characterized by a strongly decreased thermal stability, with a difference of at least 15°C between the maximum temperature of the thermal transition peaks, phosphate binds to the substrate C-3 subsite. Glycerol-3-phosphate has similar effects in thermal stability
additional information
-
effect of NADP+ on the thermostability and the irreversible thermal denaturation of the nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans. The enzyme-NADP+ binary complex shows a strongly decreased thermal stability, with a difference of about 20°C between the temperatures of the thermal transition peak maxima of the complex and the free protein. GAPN thermal inactivation is considerably decelerated in the presence of NADP+ showing that the apparent change in stability of the active centre can be the opposite to that of the whole protein molecule. NADP+ can also reactivate the inactive GAPN species, obtained by heating of the apoenzyme below the thermal denaturation transition temperature. The mechanism provides GAPN the sufficient flexibility for the earlier observed profound active site reorganizations required during the catalytic cycle. The elevated thermal stability of the apoenzyme may, in turn, be important for maintaining a constant level of active GAPN
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
a relative stability of NP-Ga3PDHase mainly accounts for the increase in specific activity observed in treatments with low and medium levels (up to 0.01 mM) of methyl viologen
the enzyme is oxidized to about 40% residual activity with 1 mM H2O2 during 1 h. The recovery of enzyme activity by thioredoxin-h takes place independently of the inactivation degree reached by oxidation
-
725162
a relative stability of NP-Ga3PDHase mainly accounts for the increase in specific activity observed in treatments with low and medium levels (up to 0.01 mM) of methyl viologen
-
688646
a relative stability of NP-Ga3PDHase mainly accounts for the increase in specific activity observed in treatments with low and medium levels (up to 0.01 mM) of methyl viologen
-
688646
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.01 M potassium phosphate buffer, pH 6.4, 2 mM dithiothreitol, 50% v/v glycerol, 3 months
-
0-4°C, 50 mM Tris-HCl buffer, pH 7.5, 1 mM EDTA, 10 mM mercaptoethanol, at least 6 months, or precipitated in 60% ammonium sulfate
-
4°C, 25 mM Tris-HCl buffer, pH 7.5, 0.1 mM EDTA, 10 mM mercaptoethanol, at least 1 month
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cell-free extract preparation
heat precipitation and Superdex 200 gel filtration
heat treatment (85°C, 30 min), anion exchange chromatography and gel filtration
-
partial
partial purification
recombinant and native GAPDH are purified to apparent homogeneity from Escherichia coli cells and Chlamydomonas reinhardtii, respectively
-
recombinant enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned and expressed in BL21 (DE3) CodonPlus using the pET expression vector system
EcoRI-digested genomic DNA into plasmid pUC18 for sequencing of gapN, into an expression vector for recombinant production of the enzyme in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) CodonPlus cells
expressed in Saccharomyces cerevisiae mutant AG2 with deletion of NAD+-dependent glycerol-3-phosphate dehydrogenase gene GPD2
-
expression by functional complementation of the Escherichia coli gap mutant W3CG
-
expression in Escherichia coli
gene gapN, construction of the mutant Escherichia coli strain MG1655DELTAgapA::gapN using the fusion of the gapN gene with a chloramphenicol resistance cassette resulting in plasmid pTrcgapN
expressed in Escherichia coli BL21(DE3) cells
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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
the enzyme is down-regulated in the dark
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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A pathway for photosynthetic carbon flow to mannitol in celery leaves
Plant Physiol.
73
869-873
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Apium graveolens
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Iglesias, A.A.; Losada, M.
Purification and kinetic and structural properties of spinach leaf NADP-dependent nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase
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260
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Iglesias, A.A.; Serrano, A.; Guerrro, M.G.; Losada, M.
Purification and properties of NADP-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the green algae Chlamydomonas reinhardtii
Biochim. Biophys. Acta
925
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1987
Chlamydomonas reinhardtii
-
brenda
Pupillo, P.; Faggiani, R.
Subunit structure of three glyceraldehyde 3-phosphate dehydrogenases of some flowering plants
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194
581-592
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Arum italicum, Beta vulgaris, Ficaria verna, Spinacia oleracea
brenda
Kelly, G.J.; Gibbs, M.
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52
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Arachis hypogaea, Ricinus communis, Pisum sativum, Zea mays
brenda
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31
255-265
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Hevea brasiliensis
brenda
Crow, V.L.; Wittenberger, C.L.
Separation and properties of NAD+- and NADP+-dependent glyceraldehyde-3-phosphate dehydrogenases from Streptococcus mutans
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254
1134-1142
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Streptococcus mutans
brenda
Mann, K.H.; Mecke, D.
Inhibition of spinach glyceraldehyde-3-phosphate dehydrogenase by pentalenolactone
Nature
282
535-536
1979
Spinacia oleracea
-
brenda
Tamoi, M.; Ishikawa, T.; Takeda, T.; Shigeoka, S.
Enzymic and molecular characterization of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from Synechoccocus PCC 7942: resistance of the enzyme to hydrogen peroxide
Biochem. J.
316
685-690
1996
Synechococcus sp.
brenda
Marchal, S.; Branlant, G.
Engineered nonphosphorylating gylceraldehyde 3-phosphate dehydrogenase at position 268 binds hydroxylamine and hydrazine as acyl acceptors
Eur. J. Biochem.
268
5764-5770
2001
Streptococcus mutans
brenda
Charron, C.; Talfournier, F.; Isupov, M.N.; Branlant, G.; Littlechild, J.A.; Vitoux, B.; Aubry, A.
Crystallization and preliminary X-ray diffraction studies of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus
Acta Crystallogr. Sect. D
55
1253-1255
1999
Methanothermus fervidus
-
brenda
Nakamura, Y.; Tada, T.; Wada, K.; Kinoshita, T.; Tamoi, M.; Shigeoka, S.; Nishimura, K.
Crystallization and preliminary X-ray diffraction analysis of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase of Synechococcus PCC 7942
Acta Crystallogr. Sect. D
57
879-881
2001
Synechococcus sp.
brenda
Arutyunov, D.Y.; Muronetz, V.I.
The activation of glycolysis performed by the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase in the model system
Biochem. Biophys. Res. Commun.
300
149-154
2003
Streptococcus mutans
brenda
Bustos, D.M.; Iglesias, A.A.
Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase is post-translationally phosphorylated in heterotrophic cells of wheat (Triticum aestivum)
FEBS Lett.
530
169-173
2002
Triticum aestivum (Q8LK61), Triticum aestivum
brenda
Marchal, S.; Branlant, G.
Characterization of the amino acids involved in substrate specificity of nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans
J. Biol. Chem.
277
39235-39242
2002
Streptococcus mutans
brenda
Rahuel-Clermont, S.; Arutyunov, D.; Marchal, S.; Orlov, V.; Muronetz, V.; Branlant, G.
Thermal destabilization of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans upon phosphate binding in the active site
J. Biol. Chem.
280
18590-18597
2005
Streptococcus mutans
brenda
Iddar, A.; Valverde, F.; Serrano, A.; Soukri, A.
Purification of recombinant non-phosphorylating NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from Streptococcus pyogenes expressed in E. coli
Mol. Cell. Biochem.
247
195-203
2003
Streptococcus pyogenes
brenda
Bustos, D.M.; Iglesias, A.A.
Phosphorylated non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from heterotrophic cells of wheat interacts with 14-3-3 proteins
Plant Physiol.
133
2081-2088
2003
Triticum aestivum
brenda
Iglesias, A.A.; Vicario, L.R.; Gomez-Casati, D.F.; Sesma, J.I.; Gomez-Casati, M.E.; Bustos, D.M.; Podesta, F.E.
On the interaction of substrate analogues with non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from celery leaves
Plant Sci.
162
689-696
2002
Apium graveolens
-
brenda
Iddar, A.; Valverde, F.; Serrano, A.; Soukri, A.
Expression, purification, and characterization of recombinant nonphosphorylating NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from Clostridium acetobutylicum
Protein Expr. Purif.
25
519-526
2002
Clostridium acetobutylicum
brenda
Kitatani, T.; Nakamura, Y.; Wada, K.; Kinoshita, T.; Tamoi, M.; Shigeoka, S.; Tada, T.
Structure of apo-glyceraldehyde-3-phosphate dehydrogenase from Synechococcus PCC7942
Acta crystallogr. Sect. F
62
727-730
2006
Synechococcus elongatus PCC 7942 = FACHB-805
brenda
DAmbrosio, K.; Pailot, A.; Talfournier, F.; Didierjean, C.; Benedetti, E.; Aubry, A.; Branlant, G.; Corbier, C.
The first crystal structure of a thioacylenzyme intermediate in the ALDH family: new coenzyme conformation and relevance to catalysis
Biochemistry
45
2978-2986
2006
Streptococcus mutans (Q59931)
brenda
Lebreton, S.; Andreescu, S.; Graciet, E.; Gontero, B.
Mapping of the interaction site of CP12 with glyceraldehyde-3-phosphate dehydrogenase from Chlamydomonas reinhardtii. Functional consequences for glyceraldehyde-3-phosphate dehydrogenase
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273
3358-3369
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Chlamydomonas reinhardtii