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Enzyme Nomenclature
Information on EC 1.2.1.9 - glyceraldehyde-3-phosphate dehydrogenase (NADP+)
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
1.2.1.9
-
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RECOMMENDED NAME
GeneOntology No.
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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+
two-step mechanism and kinetics
-
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
redox reaction
-
-
-
-
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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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
PCC 7942, enzyme not clearly distinctable from chloroplastidic from, EC 1.2.1.12
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-
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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
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-phospho-D-glyceroyl phosphate + 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 + ?
-
-
-
-
?
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+
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+
-
-
-
-
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+
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+
-
-
-
?
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+
-
-
-
?
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 + 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
-
-
-
-
?
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 SUBSTRATES
NATURAL PRODUCTS
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+
Q3C1A6
-
-
-
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+
-
-
-
-
r
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
Q97U30, Q97XA5, Q97XS9
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+
-
-
-
-
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+
Q2HQS1
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
Q2HQS0
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
Q2HQR5
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
Q2HQR4
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
Q2HQR9
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
Q2HQR7
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
Q2HQR8
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
Q2HQR6
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
Q2HQS4
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
Q3C1A6
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
Q59931
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
Q2HQR3
-
-
-
?
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
Q2HQS3
-
-
-
?
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
?
-
Q6Z9G0
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; negligible activity with NAD+; negligible activity with NAD+
NAD+
-
enzyme activity is observed with both NAD+ and NADP+, but NADP+ is the preferred cofactor
NADP+
; prefers NADP+ more than NAD+ as cofactor; prefers NADP+ more than NAD+ as cofactor; the enzyme shows only negligible activity with NAD+ compared to the physiological cosubstrate NADP+
NADP+
-
preferred cofactor; the enzyme prefers NADP+ to NAD+. NAD+ is a poor co-substrate
NADP+
-
enzyme activity is observed with both NAD+ and NADP+, but NADP+ is the preferred cofactor
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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INHIBITORS
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
-
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 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
-
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
-
GapA; 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; 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; 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; 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; pH 8.0, 60°C, mutant enzyme A198S/S199I
17.4
NAD+
70°C, pH 7; in 90 mM HEPES/KOH, 160 mM KCl, pH 7.0, at 70°C; in 90 mM HEPES/KOH, 160 mM KCl, pH 7.0, at 70°C; 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
25.8
NAD+
-
mutant enzyme, in the absence of D-glucose 1-phosphate, in 50 mM EPPS/NaOH (pH 8.0), at 60°C; pH 8.0, 60°C, mutant enzyme S199I
26.4
NAD+
-
pH 8.0, 60°C, wild-type enzyme; 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; enzyme from leaf after treatment with alkaline phosphatase
0.06
NADP+
enzyme from endosperm after treatment with alkaline phosphatase
0.09
NADP+
70°C, pH 7; in 90 mM HEPES/KOH, 160 mM KCl, pH 7.0, at 70°C; in 90 mM HEPES/KOH, 160 mM KCl, pH 7.0, at 70°C; 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
0.024
NADPH
-
mutant B(188)A, analyzed under oxidizing conditions; mutant B(E362Q)
0.028
NADPH
-
mutant enzyme S195A, pH and temperature not specified in the publication; wild type enzyme, pH and temperature not specified in the publication
0.05
NADPH
-
AB-GAPDH, analyzed under oxidizing conditions; AB-GAPDH, analyzed under reducing conditions
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
additional information
additional information
-
catalytic rate constant 238 s-1, control; catalytic rate constant 289 s-1, 3 microM 3-phospho-D-glyceroyl phosphate, NADPH-dependent activity of GAPDH in the GAPDH/CP12 complex; catalytic rate constant 316 s-1, 160 microM 3-phospho-D-glyceroyl phosphate, NADPH-dependent activity of GAPDH in the GAPDH/CP12 complex; catalytic rate constant 330 s-1, 10 microM thioredoxin, NADPH-dependent activity of GAPDH in the GAPDH/CP12 complex; 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; 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+
-
pH 8.0, 60°C, wild-type enzyme; 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; pH 8.0, 60°C, 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 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; pH 8.0, 60°C, 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 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; pH 8.0, 60°C, 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 60°C; pH 8.0, 60°C, 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 60°C
96.6
NADP+
-
pH 8.0, 60°C, wild-type enzyme; 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
strain 12U1-ccpA-, energy substrate glucose, microM NADP+ reduced min-1 (mg of cell-N)-1; strain 12U1-ccpA-, energy substrate glucose, microM NADP+ reduced min-1 (mg of cellular nitrogen)-1
0.015
0.016
strain 12U1, energy substrate lactose, microM NADP+ reduced min-1 (mg of cell-N)-1; 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; strain 12U1p, microM NADP+ reduced min-1 (mg of cell-N)-1
0.032
growth stage: middle log growth, microM NADP+ reduced min-1 (mg of cell-N)-1
0.033
strain 12U1, energy substrate glucose, microM NADP+ reduced min-1 (mg of cell-N)-1; 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; strain 12U1gapN-1, microM NADP+ reduced min-1 (mg of cell-N)-1
0.04
0.065
recombinant GAPN overexpression strain 12U1gapN-2, energy substrate glucose, microM NADP+ reduced min-1 (mg of cellular nitrogen)-1; strain 12U1gapN-2, microM NADP+ reduced min-1 (mg of cell-N)-1
additional information
0.011
growth stage: later log growth, 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 cell-N)-1; strain 12U1-ccpA-, energy substrate lactose, microM NADP+ reduced min-1 (mg of cellular nitrogen)-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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.9
8 - 9
8.2
8.5
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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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
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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
52000
53000
55000
56400
-
4 * 56400, calculated from amino acid sequence; 4 * 56400, calculated from sequence
56930
subunit, calculated from amino acid sequence; subunit, calculated from amino acid sequence; subunit, calculated from amino acid sequence
57000
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
520000
-
GapB mutant B(E326Q) in the presence of NADH, compatible with octameric structure, estimated by gel filtration; GapB mutant B(R77A) in the presence of NADH, compatible with octameric structure, estimated by gel filtration
553000
-
GapB mutant B(S188A) in the presence of NADH, compatible with octameric structure, estimated by gel filtration
760000
-
oligomer of GAPDH in the presence of NADH, suggesting A8B8 stoichiometry, estimated by gel filtration
57000
4 * 57000, SDS-PAGE; 4 * 57000, SDS-PAGE; subunit, SDS-PAGE; x * 57000, SDS-PAGE
189000
-
tetrameric conformation of GAPDH-A2B2 stabilized by NADPH, estimated by gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
tetramer
homotetramer
-
4 * 57000, SDS-PAGE; 4 * 57000, SDS-PAGE; 4 * 57000, SDS-PAGE
-
homotetramer
-
4 * 56000, SDS-PAGE; 4 * 56400, calculated from amino acid sequence
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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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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; Superdex 200 gel filtration; 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; expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) CodonPlus cells
EcoRI-digested genomic DNA into plasmid pUC18 for sequencing of gapN, into an expression vector for recombinant production of the enzyme in Escherichia coli; for expression in Escherichia coli
expressed in Escherichia coli C43 (DE3) cells; expression in Escherichia coli
-
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
-
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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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ENGINEERING
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
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compared to wild-type enzyme the amount of the thermolabile species is significantly lower
R124L
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turnover number is 21fold lower than turnover-number of wild-type enzym
R301L
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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
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compared to wild-type enzyme the amount of the thermolabile species is similar
Y170F
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turnover number is 1.7fold higher than turnover-number of wild-type enzyme
A198S/S199I
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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%; the mutant shows reduced catalytic efficiency with NADP+ and increased catalytic efficiency with NAD+ as compared to the wild type enzyme
E141D
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kcat for D-glyceraldehyde 3-phosphate is 2.1fold lower than wild-type value
K137E
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kcat for D-glyceraldehyde 3-phosphate is 1.1fold lower than wild-type value
L138T
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kcat for D-glyceraldehyde 3-phosphate is 1.3fold lower than wild-type value
R136K
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kcat for D-glyceraldehyde 3-phosphate is 2.8fold lower than wild-type value
S199I
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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%; the mutant shows reduced catalytic efficiency with NADP+ and increased catalytic efficiency with NAD+ as compared to the wild type enzyme
Y139R
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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
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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%
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E141D
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kcat for D-glyceraldehyde 3-phosphate is 2.1fold lower than wild-type value
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K137E
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kcat for D-glyceraldehyde 3-phosphate is 1.1fold lower than wild-type value
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L138T
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kcat for D-glyceraldehyde 3-phosphate is 1.3fold lower than wild-type value
-
R136K
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kcat for D-glyceraldehyde 3-phosphate is 2.8fold lower than wild-type value
-
S199I
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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
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attacking water molecule in the hydrolysis process is poorly activated, can be overcome by the nulceophiles hydrazin and hydroxylamine
E268A
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compared to wild-type enzyme the amount of the thermolabile species is significantly lower
R459I
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turnover number is 214fold lower than turnover-number of wild-type enzyme. Rate limiting step is acylation, compared to deacylation in wild-type enzyme
R459I
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compared to wild-type enzyme the amount of the thermolabile species is significantly lower
additional information
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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
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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
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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
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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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additional information
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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
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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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