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apo-glyceraldehyde-3-phosphate dehydrogenase
-
-
dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide phosphate)
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-
-
-
glyceraldehyde 3-phosphate dehydrogenase
-
glyceraldehyde 3-phosphate dehydrogenase (NADP)
-
-
-
-
glyceraldehyde 3-phosphate:NADP+ reductase, non-phosphorylating
glyceraldehyde phosphate dehydrogenase (NADP)
-
-
-
-
glyceraldehyde-3-phosphate dehydrogenase
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
Glyceraldehyde-3-phosphate dehydrogenase [NADP+]
-
-
-
-
glyceraldehyde-3-phosphate:NADP reductase
-
-
-
-
NADP+-dependent glyceraldehyde 3-phosphate dehydrogenase
-
NADP-dependent ALDH11A3
-
NADP-dependent glyceraldehyde 3-phosphate dehydrogenase
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
NADP-dependent nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
-
NADP-glyceraldehyde phosphate dehydrogenase
-
-
-
-
NADP-glyceraldehyde-3-phosphate dehydrogenase
-
-
-
-
NADPH-glyceraldehyde-3-phosphate dehydrogenase
-
-
non phosphorylating glyceraldehyde-3-phosphate dehydrogenase
non-phosphorylating GAP dehydrogenase
Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase
-
-
-
-
non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase
non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase GAPN
-
-
non-phosphorylating glyceraldehyde-phosphate dehydrogenase
-
-
non-phosphorylating NADP+-dependent Ga3PDHase
-
-
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
-
-
triose phosphate dehydrogenase
-
-
-
-
Triosephosphate dehydrogenase
-
-
-
-
CagapC
-
-
CbgapC
-
-
CsgapC
-
-
GAP dehydrogenase
-
GAPC
-
-
GAPDH
-
-
GAPDHN
-
GAPN
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-
glyceraldehyde 3-phosphate:NADP+ reductase, non-phosphorylating
-
-
glyceraldehyde 3-phosphate:NADP+ reductase, non-phosphorylating
-
-
glyceraldehyde 3-phosphate:NADP+ reductase, non-phosphorylating
-
-
glyceraldehyde-3-phosphate dehydrogenase
-
-
glyceraldehyde-3-phosphate dehydrogenase
-
-
glyceraldehyde-3-phosphate dehydrogenase
-
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
-
-
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
-
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
-
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
-
-
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
-
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
-
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
-
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
-
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
-
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
-
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
no activity in Penicillium chrysogenum
-
-
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
-
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
-
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
-
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
-
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
-
-
NADP-dependent glyceraldehyde 3-phosphate dehydrogenase
-
-
NADP-dependent glyceraldehyde 3-phosphate dehydrogenase
-
-
-
NADP-dependent glyceraldehyde 3-phosphate dehydrogenase
-
-
NADP-dependent glyceraldehyde 3-phosphate dehydrogenase
-
-
-
NADP-dependent glyceraldehyde 3-phosphate dehydrogenase
-
-
NADP-dependent glyceraldehyde 3-phosphate dehydrogenase
-
-
-
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
-
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
-
NADPH-dependent GAPDH
-
-
NADPH-dependent GAPDH
-
-
NADPH-dependent GAPDH
-
-
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
-
non phosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
non phosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
non phosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
non-phosphorylating GAP dehydrogenase
-
-
non-phosphorylating GAP 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
-
-
non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
-
non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
-
nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
-
-
-
nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
-
NP-Ga3PDHase
-
-
NP-GAPDH
-
-
SSO3194
locus name
St-GAPN
-
STK_24770
locus name
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + H2O + NADP+
(2R)-3-phosphoglycerate + NADPH + 2 H+
-
-
-
?
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + 2 H+
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + H+
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
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 + NAD+
D-3-phosphoglycerate + NADH + H+
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH + H+
D-glyceraldehyde-3-phosphate + nicotinamide-hypoxanthine dinucleotide phosphate
D-3-phosphoglycerate + ?
-
-
-
-
?
DL-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-DL-glycerate + NADH + H+
DL-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
r
DL-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-DL-glycerate + NADPH + H+
additional information
?
-
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+
-
-
-
-
?
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+
-
-
-
-
?
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 EntnerDoudoroff 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+
-
-
-
?, 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+
-
-
-
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
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
-
-
-
-
ir
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
?
-
-
recombinant CbgapC shows no catalytic activity
-
-
-
additional information
?
-
-
recombinant CbgapC shows no catalytic activity
-
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
D-glyceraldehyde 3-phosphate + H2O + NADP+
(2R)-3-phosphoglycerate + NADPH + 2 H+
-
-
-
?
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 + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
r
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
DL-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-DL-glycerate + NADPH + H+
-
-
-
-
?
additional information
?
-
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+
-
-
-
-
?
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+
-
-
-
-
?
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 EntnerDoudoroff 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+
-
-
-
?, 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+
-
-
-
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
-
-
-
-
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
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
-
-
?
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0.04
1,N6-ethenoadenine-nicotinamide dinucleotide phosphate
-
-
0.016
3-acetylpyridine-adenine dinucleotide phosphate
-
-
0.012 - 0.031
3-phospho-D-glyceroyl phosphate
0.08
beta-nicotinamide adenine dinucleotide 2',3'-cyclic monophosphate
-
-
0.017 - 0.051
D-glyceraldehyde 3-phosphate
0.046 - 9.2
D-Glyceraldehyde-3-phosphate
0.501 - 0.51
DL-glyceraldehyde 3-phosphate
0.42
NADH
-
3-phosphoglycerate
0.033
nicotinamide-hypoxanthine dinucleotide phosphate
-
-
0.012
3-phospho-D-glyceroyl phosphate
-
mutant B(E362Q)
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
-
mutant B(R77A)
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
0.022
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
0.017 - 0.022
D-glyceraldehyde 3-phosphate
-
-
0.019
D-glyceraldehyde 3-phosphate
-
-
0.025
D-glyceraldehyde 3-phosphate
-
-
0.031
D-glyceraldehyde 3-phosphate
-
-
0.051
D-glyceraldehyde 3-phosphate
-
-
0.046
D-Glyceraldehyde-3-phosphate
-
pH 8.5, 25°C, wild-type enzyme
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
0.18
D-Glyceraldehyde-3-phosphate
-
pH 8.5, 25°C, mutant enzyme Y170F
0.51
D-Glyceraldehyde-3-phosphate
in 90 mM HEPES/KOH, 160 mM KCl, pH 7.0, at 70°C
0.545
D-Glyceraldehyde-3-phosphate
-
pH 8.5, 25°C
0.666
D-Glyceraldehyde-3-phosphate
-
pH 8.5, 25°C
9.2
D-Glyceraldehyde-3-phosphate
-
pH 8.5, 25°C, mutant enzyme R459I
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
1.2
NAD+
-
glyceraldehyde 3-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
17.2
NAD+
pH 8.0, 60°C, mutant enzyme A198S/S199I
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
25.8
NAD+
pH 8.0, 60°C, mutant enzyme S199I
26.4
NAD+
pH 8.0, 60°C, wild-type enzyme
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
0.0035
NADP+
-
-
0.01
NADP+
-
coupled assay with aldolase
0.022
NADP+
pH 8.0, 60°C, mutant enzyme A198S/S199I
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
0.023
NADP+
pH 8.0, 60°C, wild-type enzyme
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
0.026
NADP+
pH 8.0, 60°C, mutant enzyme S199I
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
0.385
NADP+
-
pH 8.5, 25°C
0.019
NADPH
-
mutant B(minCTE)
0.024
NADPH
-
mutant B(188)A, analyzed under oxidizing conditions
0.024
NADPH
-
mutant B(E362Q)
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
0.03
NADPH
-
GapB, analyzed under reducing conditions
0.038
NADPH
-
GapB, analyzed under oxidizing conditions
0.043
NADPH
-
A(plusCTE) mutant, analyzed under oxidizing conditions
0.046
NADPH
-
mutant B(188)A, analyzed under reducing conditions
0.05
NADPH
-
AB-GAPDH, analyzed under oxidizing conditions
0.05
NADPH
-
AB-GAPDH, analyzed under reducing conditions
0.062
NADPH
-
3-phosphoglycerate
0.065
NADPH
-
A(plusCTE) mutant, analyzed under reducing conditions
0.078
NADPH
-
mutant B(R77A)
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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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
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
C302A
-
compared to wild-type enzyme the amount of the thermolabile species is higher
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
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
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
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%
-
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
E268A
mutant shows reduced deacylation rate
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
-
CRISPR-Cpf1-assisted engineering of Corynebacterium glutamicum SNK118 for enhanced L-ornithine production by NADP-dependent glyceraldehyde-3-phosphate dehydrogenase and NADH-dependent glutamate dehydrogenase. Insufficient intracellular NADPH content has been recognized as a limiting factor in L-ornithine biosynthesis. Overexpression of NADP-dependent glyceraldehyde 3-phosphate dehydrogenase gene CsgapC from Clostridium saccharobutylicum strain DSM 13864 and NADH-dependent glutamate dehydrogenase gene BsrocG from Bacillus subtilis strain HB-1 results in markedly increased ornithine biosynthesis. The engineered Corynebacterium glutamicum strain KBJ11 (SNK118DELTAargRDELTAargFDELTAncgl2228/pXMJ19-CsgapC-BsrocG) is constructed for L-ornithine overproduction. In fed-batch fermentation, L-ornithine of 88.26 g/l with productivity of 1.23 g/l/h (over 72 h) and yield of 0.414 g/g glucose is achieved by strain KBJ11 in a 10-l bioreactor. High titer and yield of L-ornithine production by microbial fermentation proves that heterologous expression of CsgapC and BsrocG can promote L-ornithine production by Corynebacterium glutamicum strains
additional information
-
CRISPR-Cpf1-assisted engineering of Corynebacterium glutamicum SNK118 for enhanced L-ornithine production by NADP-dependent glyceraldehyde-3-phosphate dehydrogenase and NADH-dependent glutamate dehydrogenase. Insufficient intracellular NADPH content has been recognized as a limiting factor in L-ornithine biosynthesis. Overexpression of NADP-dependent glyceraldehyde 3-phosphate dehydrogenase gene CsgapC from Clostridium saccharobutylicum strain DSM 13864 and NADH-dependent glutamate dehydrogenase gene BsrocG from Bacillus subtilis strain HB-1 results in markedly increased ornithine biosynthesis. The engineered Corynebacterium glutamicum strain KBJ11 (SNK118DELTAargRDELTAargFDELTAncgl2228/pXMJ19-CsgapC-BsrocG) is constructed for L-ornithine overproduction. In fed-batch fermentation, L-ornithine of 88.26 g/l with productivity of 1.23 g/l/h (over 72 h) and yield of 0.414 g/g glucose is achieved by strain KBJ11 in a 10-l bioreactor. High titer and yield of L-ornithine production by microbial fermentation proves that heterologous expression of CsgapC and BsrocG can promote L-ornithine production by Corynebacterium glutamicum 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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Rumpho, M.E.; Edwards, G.E.; Loescher, W.H.
A pathway for photosynthetic carbon flow to mannitol in celery leaves
Plant Physiol.
73
869-873
1983
Apium graveolens
brenda
Iglesias, A.A.; Losada, M.
Purification and kinetic and structural properties of spinach leaf NADP-dependent nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase
Arch. Biochem. Biophys.
260
830-840
1988
Spinacia oleracea
brenda
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
1-10
1987
Chlamydomonas reinhardtii
-
brenda
Pupillo, P.; Faggiani, R.
Subunit structure of three glyceraldehyde 3-phosphate dehydrogenases of some flowering plants
Arch. Biochem. Biophys.
194
581-592
1979
Arum italicum, Beta vulgaris, Ficaria verna, Spinacia oleracea
brenda
Kelly, G.J.; Gibbs, M.
Nonreversible D-glyceraldehyde 3-phosphate dehydrogenase of plant tissue
Plant Physiol.
52
111-118
1973
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