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apo-glyceraldehyde-3-phosphate dehydrogenase
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-
dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide phosphate)
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-
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glyceraldehyde 3-phosphate dehydrogenase
-
glyceraldehyde 3-phosphate dehydrogenase (NADP)
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-
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glyceraldehyde 3-phosphate:NADP+ reductase, non-phosphorylating
glyceraldehyde phosphate dehydrogenase (NADP)
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-
-
-
glyceraldehyde-3-phosphate dehydrogenase
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
Glyceraldehyde-3-phosphate dehydrogenase [NADP+]
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-
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glyceraldehyde-3-phosphate:NADP reductase
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NADP+-dependent glyceraldehyde 3-phosphate dehydrogenase
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NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
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NADP-dependent nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase
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-
NADP-glyceraldehyde phosphate dehydrogenase
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-
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NADP-glyceraldehyde-3-phosphate dehydrogenase
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-
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NADPH-glyceraldehyde-3-phosphate dehydrogenase
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non phosphorylating glyceraldehyde-3-phosphate dehydrogenase
non-phosphorylating GAP dehydrogenase
Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase
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non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase
non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase GAPN
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non-phosphorylating glyceraldehyde-phosphate dehydrogenase
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non-phosphorylating NADP+-dependent Ga3PDHase
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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
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-
triose phosphate dehydrogenase
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-
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Triosephosphate dehydrogenase
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GAP dehydrogenase

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GAPDH

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GAPDHN

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GAPN

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glyceraldehyde 3-phosphate:NADP+ reductase, non-phosphorylating

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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
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-
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+)
-
-
NADPH-dependent GAPDH

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-
NADPH-dependent GAPDH
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-
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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3-phospho-D-glycerate + NADH + H+
D-glyceraldehyde 3-phosphate + NAD+ + H2O
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-
-
-
r
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+
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
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-
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
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-
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 EntnerĆ¢ĀĀDoudoroff 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

?
-
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 + 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+
the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase is a key-enzyme of the semi-phosphorylative branch of the EntnerĆ¢ĀĀDoudoroff 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, 25ưC, 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, 25ưC, mutant enzyme Y170F
0.51
D-Glyceraldehyde-3-phosphate
in 90 mM HEPES/KOH, 160 mM KCl, pH 7.0, at 70ưC
0.545
D-Glyceraldehyde-3-phosphate
-
pH 8.5, 25ưC
0.666
D-Glyceraldehyde-3-phosphate
-
pH 8.5, 25ưC
9.2
D-Glyceraldehyde-3-phosphate
-
pH 8.5, 25ưC, mutant enzyme R459I
0.501
DL-glyceraldehyde 3-phosphate

in the presence of D-glucose 1-phosphate
0.51
DL-glyceraldehyde 3-phosphate
70ưC, 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 60ưC
17.2
NAD+
pH 8.0, 60ưC, mutant enzyme A198S/S199I
17.4
NAD+
in 90 mM HEPES/KOH, 160 mM KCl, pH 7.0, at 70ưC
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 60ưC
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 60ưC
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 60ưC
25.8
NAD+
pH 8.0, 60ưC, mutant enzyme S199I
26.4
NAD+
pH 8.0, 60ưC, 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 60ưC
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 60ưC
0.0035
NADP+

-
-
0.01
NADP+
-
coupled assay with aldolase
0.022
NADP+
pH 8.0, 60ưC, 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 60ưC
0.023
NADP+
pH 8.0, 60ưC, 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 60ưC
0.026
NADP+
pH 8.0, 60ưC, 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 60ưC
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 70ưC
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 60ưC
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 60ưC
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 60ưC
0.2
NADP+
-
pH 8.5, 25ưC
0.385
NADP+
-
pH 8.5, 25ưC
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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1.13 - 341
D-glyceraldehyde 3-phosphate
0.06 - 103
D-Glyceraldehyde-3-phosphate
additional information
additional information
-
1.13
D-glyceraldehyde 3-phosphate

pH 8.0, 60ưC, mutant enzyme Y139R
15
D-glyceraldehyde 3-phosphate
pH 8.0, 60ưC
117
D-glyceraldehyde 3-phosphate
pH 8.0, 60ưC, mutant enzyme R136K
161
D-glyceraldehyde 3-phosphate
pH 8.0, 60ưC, mutant enzyme E141D
257
D-glyceraldehyde 3-phosphate
pH 8.0, 60ưC, mutant enzyme L138T
297
D-glyceraldehyde 3-phosphate
pH 8.0, 60ưC, mutant enzyme K137E
341
D-glyceraldehyde 3-phosphate
pH 8.0, 60ưC, wild-type enzyme
0.06
D-Glyceraldehyde-3-phosphate

-
pH 8.5, 25ưC, mutant enzyme R301L
0.28
D-Glyceraldehyde-3-phosphate
-
pH 8.5, 25ưC, mutant enzyme R459I
2.8
D-Glyceraldehyde-3-phosphate
-
pH 8.5, 25ưC, mutant enzyme R124L
60
D-Glyceraldehyde-3-phosphate
-
pH 8.5, 25ưC, wild-type enzyme
103
D-Glyceraldehyde-3-phosphate
-
pH 8.5, 25ưC, mutant enzyme Y170F
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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0.378
NAD+

pH 8.0, 60ưC, wild-type enzyme
0.378
NAD+
wild type enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60ưC
0.434
NAD+
mutant enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60ưC
0.434
NAD+
pH 8.0, 60ưC, mutant enzyme S199I
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 60ưC
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 60ưC
1
NAD+
mutant enzyme A198S/S199I, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60ưC
1
NAD+
pH 8.0, 60ưC, mutant enzyme A198S/S199I
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 60ưC
48.1
NADP+

mutant enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60ưC
48.1
NADP+
pH 8.0, 60ưC, mutant enzyme S199I
61.5
NADP+
mutant enzyme A198S/S199I, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60ưC
61.5
NADP+
pH 8.0, 60ưC, mutant enzyme A198S/S199I
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 60ưC
96.6
NADP+
pH 8.0, 60ưC, wild-type enzyme
96.6
NADP+
wild type enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60ưC
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 60ưC
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 60ưC
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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
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.
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