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1.2.1.12: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)

This is an abbreviated version!
For detailed information about glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), go to the full flat file.

Word Map on EC 1.2.1.12

Reaction

D-glyceraldehyde 3-phosphate
+
phosphate
+
NAD+
=
3-phospho-D-glyceroyl phosphate
+
NADH
+
H+

Synonyms

3-phosphoglyceraldehyde dehydrogenase, A4-GAPDH, A4-glyceraldehyde-3-phosphate dehydrogenase, AB-GAPDH, AnBn-GAPDH, AsGAPDH, At3g04120, BARS-38, CbbG, CgGAP, Clo1313_2095, complement-C3-binding protein, CP 17/CP 18, Ctherm_Gapdh, cytosolic NAD-dependent glyceraldehyde 3-P dehydrogenase, cytosolic phosphorylating glyceraldehyde-3-phosphate dehydrogenase, D-glyceraldehyde-3-phosphate dehydrogenase, D-glyceraldehyde-3-phosphate: NAD+ oxidoreductase (phosphorylating), dehydrogenase, glyceraldehyde phosphate, dihydrogenase, glyceraldehyde phosphate, EcGAPDH, EcGAPDH1, FgGAPDH, FhGAPDH, G3PD, G3PDH, Ga3P dehydrogenase, Ga3PDHase, GADPH, GAP, GAP1, gap2, GapA, GapB, GAPC, GapC-1, GapC1, GapC2, GAPCp, GAPCp1, GAPCp2, GAPD, GAPDH, GAPDH type 1, GAPDH1, GAPDH2, GAPDH3, GAPDHS, GAPDS, GAPN, GBS GAPDH, glyceraldehyde 3-phosphate dehydrogenase, glyceraldehyde 3-phosphate dehydrogenase-S, glyceraldehyde phosphate dehydrogenase (NAD), glyceraldehyde-3 phosphate dehydrogenase, glyceraldehyde-3-P-dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase (NAD), glyceraldehyde-3-phosphate dehydrogenase 1, glyceraldehyde-3-phosphate dehydrogenase, type I, glyceraldehyde-3-phosphate dehydrogenase-spermatogenic protein, glyceraldehyde-3-phosphate dehydrogenase-spermatogenic protein GAPDHS, glyceraldehyde-3-phosphate dehydrogenases, GPD, GPD2, Gra3PDH, GraP-DH, H.c-C3BP, hGAPDH, HsGAPDH, kmGAPDH1p, Larval antigen OVB95, Major larval surface antigen, Mtb-GAPDH, NAD+-dependent GAPDH, NAD+-dependent glyceraldehyde 3-phosphate dehydrogenase, NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase, NAD+-G-3-P dehydrogenase, NAD+-GAPDH, NAD-dependent Ga3PDHase, NAD-dependent glyceraldehyde 3-phosphate dehydrogenase, NAD-dependent glyceraldehyde phosphate dehydrogenase, NAD-dependent glyceraldehyde-3-phosphate dehydrogenase, NAD-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase, NAD-dependent phosphorylating glyceraldehyde-3-phosphate dehydrogenase, NAD-G3PDH, NAD-GAPDH, NADH-glyceraldehyde phosphate dehydrogenase, P-37, p-GAPDH, PfGAPDH, phosphoglyceraldehyde dehydrogenase, phosphorylating NAD+-dependent GAPDH, Plasmin receptor, Plasminogen-binding protein, plastidial glyceraldehyde-3-phosphate dehydrogenase, pmGAPDH, PyGapdh, rmGAPDH, Rv1436, somatic GAPD, somatic glyceraldehyde 3-phosphate dehydrogenase, sperm-specific GAPDS, sperm-specific glyceraldehyde 3-phosphate dehydrogenase, sperm-specific glyceraldehyde-3-phosphate dehydrogenase, TaeNAD-GAPDH, TagapC, TDH1, TDH2, TDH3, TLAb, triose phosphate dehydrogenase, UDG, uracil-DNA glycosylase, vGPD

ECTree

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.1 With NAD+ or NADP+ as acceptor
                1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)

Engineering

Engineering on EC 1.2.1.12 - glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C149S
C153S
C155S
nuclear relocalization of GAPC1 under cadmium-induced oxidative stress is stimulated, rather than inhibited, by mutation of the catalytic cysteine C155
C159S
the mutant C159S of the isozyme GapC2 shows decreased specific activity
D32A
-
activity of mutant enzyme D32A with NAD+ is equal to that of the wild-type enzyme, mutant enzyme also shows activity with NADP+, about 3% of the activity with NAD+
D32A/L187N
-
wild-type enzyme has no activity with NADP+, the mutant enzyme D32A/L187N shows catalytic efficiency with NADP+ higher than that with NAD+
L187N
-
activity of mutant L187N with NAD+ is higher than that of the wild-type enzyme, mutant enzyme also shows activity with NADP+, about 7% of the activity with NAD+
D35G/L36R/P192S
D35G/L36T/T37K
D35G/L36T/T37K/P192S
D35G
-
mutation enables GAPDH to accept both NAD and NADP
-
D35G/L36R/P192S
-
mutant accepts both Nad AND nadp WITH SIMILAR EFFICINCY
-
D35G/L36T/T37K
-
catalytic efficiency with NADP is about 10fold hihger than with NAD
-
D35G/L36T/T37K/P192S
-
Mutant shows the highest catalytic efficiency with NADP while the catalytic efficiency with NAD also increases
-
L36T
-
mutation enables GAPDH to accept both NAD and NADP
-
C153S
C149A
C153A
-
site-directed mutagenesis
N313T/Y317G
dissociation constant for NAD+ is 300times higher than that of the wild-type enzyme. Conformational equilibrium between the syn and the anti forms with a preference for the anti conformer
Y317A
dissociation constant for NAD+ is 5times higher than that of the wild-type enzyme. Wild-type syn orientation of bound nicotinamide remains unchanged
Y317G
dissociation constant for NAD+ is 13times higher than that of the wild-type enzyme. Wild-type syn orientation of bound nicotinamide remains unchanged
C149A
mutant enzyme displays no significant dehydrogenase activity
C149S
low but significant phosphorylating dehydrogenase activity
C149selenocysteine
-
mutant enzyme has selenoperoxidase activity
D186G
behavior in NAD+ binding is similar to that of the wild type enzyme
D186G/E276G
positive cooperativity in binding the coenzyme NAD+
D282G
-
enzyme exists as dimer and tetramer, the tetramer is inactive, the dimer is slightly active, 650fold decrease in turnover number for NAD+, 5.8fold increase in Km-value for NAD+ compared to wild-type enzyme
E276G
behavior in NAD+ binding is similar to that of the wild type enzyme
L187A/P188S
-
the mutant is catalytically active not only with NAD+, as the wild-type enzyme, but also with NADP+
N313T
-
mutant enzyme with a drastic decrease in thermostability, weakening of cooperative interactions between the catalytic and the cofactor domains and an inefficient binding of NAD+, mutant enzyme exists only as tetramer, 65fold decrease in turnover number for NAD+, 50fold increase in Km-value for NAD+ compared to wild-type enzyme
T34Q/T39S/L43Q
-
drastic decrease in thermostability, inefficient NAD+ binding, enzyme exists as dimer and tetramer, the tetramer is inactive, the dimer is slightly active, 650fold decrease in turnover number for NAD+, 4fold increase in Km-value for NAD+ compared to wild-type enzyme
W310F
-
mutant enzyme with a drastic decrease in thermostability, mutant enzyme exists only as tetramer, 2fold increase of Km-value for NAD+, 1.3fold decrease in turnover number compared to wild-type enzyme
W84F
-
slightly lower Km-values for NAD+ and glyceraldehyde 3-phosphate, slightly higher Km-value for phosphate. The construction of the mutant permitts the identification of the individual fluorescence and phosphorescence characteristics of the two Trp residues W84 and W310 in the native enzyme
Y283V
-
mutant enzyme with a drastic decrease in thermostability, dimeric form is inactive, KM-value and turnover-number of tetramer are nearly identical to that of the wild-type
Y46G
behavior in NAD+ binding is similar to that of the wild type enzyme
Y46G/R52G
-
inactive mutant enzyme, only exists as dimer
Y46G/S48G
C149A
-
mutant has almost completely lost the ability to bind telomere. Upon expression in A-549 cells, mutant localizes to the nucleus but is unable to confer any significant protection of telomeres against chemotherapy-induced degradation or growth inhibition
C152G
mutant retains the ability to interact with but is unable to reactivate DNA repair enzyme APE1
C156G
mutant retains the ability to interact with but is unable to reactivate DNA repair enzyme APE1
D234A
-
site-directed mutagenesis
D256R/K260E
site-directed mutagenesis, the double mutation of GAPDH results in loss of detectable binding activity to wild-type capsid N-terminal domain
D256R/K260E/K263E/E267R
site-directed mutagenesis, multiple-substituted GAPDH mutant D256R/K260E/K263E/E267R retains the oligomeric formation with wild-type GAPDH in HIV-1 producing cells, but the incorporation level of the hetero-oligomer is decreased in viral particles. The viruses produced from cells expressing the D256R/K260E/K263E/E267R mutant restores tRNALys3 packaging efficiency because the mutant exerts a dominant negative effect by preventing wild-type GAPDH from binding to matrix region and capsid N-terminal domain and improves the reverse transcription
D256R/K260E/Q264A
site-directed mutagenesis, the mutant lacks the ability to bind to the wild-type capsid N-terminal domain
D256R/K260E/Q264A/E267R
site-directed mutagenesis, the mutant lacks the binding ability to the wild-type capsid N-terminal domain
D311N
D32A
-
mutant is unable to bind NAD+, is enzymatically inactive and has almost completely lost the ability to bind telomere. Upon expression in A-549 cells, mutant localizes to the nucleus but is unable to confer any significant protection of telomeres against chemotherapy-induced degradation or growth inhibition
D356R
site-directed mutagenesis, the mutation leads to loss of the ability to bind to wild-type matrix region
E244Q
E267R
site-directed mutagenesis, the mutation leads to loss of the ability to bind to wild-type matrix region
H179A
-
site-directed mutagenesis, the KD value of cADPR to GAPDHHis179Ala mutant protein is markedly increased compared to wild-type GAPDH enzyme
K263E
site-directed mutagenesis, the mutation leads to loss of the ability to bind to wild-type matrix region
P111A
site-directed mutagenesis, mutation at first position of alpha-helix
P157A
site-directed mutagenesis, mutation at first position of alpha-helix
P164A
site-directed mutagenesis, mutation at beta-turn, the mutant shows reduced thermostability and reduced resistance against guanidine hydrochloride. The Tm value of the heat-absorption curve decreases by 3.3°C compared to the wild-type protein
P197A
site-directed mutagenesis, mutation at beta-turn
P213A
site-directed mutagenesis, mutation at beta-turn
P326A
site-directed mutagenesis, mutation at first position of alpha-helix, the mutant shows reduced thermostability and reduced resistance against guanidine hydrochloride. The Tm value of the heat-absorption curve decreases by 6.0°C compared to the wild-type protein
A229V
-
exhibits 50-55% residual activity in blood compared to the wild type enzyme
C281W
-
exhibits 50-55% residual activity in blood compared to the wild type enzyme
G166D
-
exhibits 50-55% residual activity in blood compared to the wild type enzyme
I308S
-
exhibits 50-55% residual activity in blood compared to the wild type enzyme
V239I
-
exhibits 50-55% residual activity in blood compared to the wild type enzyme
Y327N
-
exhibits 50-55% residual activity in blood compared to the wild type enzyme
C158A
site-directed mutagenesis, inactive mutant
C162A
site-directed mutagenesis, the mutant exhibits a comparable Vmax to the wild-type enzyme and only a 2fold increased Km value for D-glyceraldehyde 3-phosphate
H185A
site-directed mutagenesis, inactive mutant
N142S
naturally occuring mutation, resulting in a non-significant structural change, since Ser at position 142 also shows a similar characteristic to the wild-type residues N142, experimentally the mutation results in a loss of enzyme activity
P295L
naturally occuring mutation
N142S
-
naturally occuring mutation, resulting in a non-significant structural change, since Ser at position 142 also shows a similar characteristic to the wild-type residues N142, experimentally the mutation results in a loss of enzyme activity
-
P295L
-
naturally occuring mutation
-
C158A
-
site-directed mutagenesis, inactive mutant
-
C162A
-
site-directed mutagenesis, the mutant exhibits a comparable Vmax to the wild-type enzyme and only a 2fold increased Km value for D-glyceraldehyde 3-phosphate
-
H185A
-
site-directed mutagenesis, inactive mutant
-
N142S
-
naturally occuring mutation, resulting in a non-significant structural change, since Ser at position 142 also shows a similar characteristic to the wild-type residues N142, experimentally the mutation results in a loss of enzyme activity
-
P295L
-
naturally occuring mutation
-
C149S
-
treatment of with (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide at 0.1 mM leads to low levels of aggregation (5% of wild type)
C149S/C281S
-
mutant shows a complete absence of aggregation in the presence of (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide
C153S
-
aggregation can be detected at low concentrations of (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide (0.001 mM) and is enhanced at higher concentrations
C244A
-
aggregation can be detected at low concentrations of (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide (0.001 mM) and is enhanced at higher concentrations
C281S
-
the levels of aggregation in C281S are reduced to 45% of wild type at 0.1 mM (E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide
F37G
the mutant shows strongly reduced kcat values compared to the wild type enzyme
F37L
the mutant shows strongly reduced kcat values compared to the wild type enzyme
F37T
the mutant shows strongly reduced kcat values compared to the wild type enzyme
F37G
substitution of residue F37 with Gly, Thr or Leu leads to 6- to 9fold increase in Km value for cofactor NAD+ or NADG, with only slight increase for substrates D- glyceraldehyde 3-phosphate or 3-phospho-D-glyceroyl phosphate
F37L
substitution of residue F37 with Gly, Thr or Leu leads to 6- to 9fold increase in Km value for cofactor NAD+ or NADG, with only slight increase for substrates D-glyceraldehyde 3-phosphate or 3-phospho-D-glyceroyl phosphate
F37T
substitution of residue F37 with Gly, Thr or Leu leads to 6- to 9fold increase in Km value for cofactor NAD+ or NADG, with only slight increase for substrates D-glyceraldehyde 3-phosphate or 3-phospho-D-glyceroyl phosphate
T227A
mutation at site of O-GlcNAcylation. Mutation induces the cytoplasmic accumulation of glyceraldehyde 3-phosphate dehydrogenase
C150G
C151/H178N
the rate of the forward reaction is decreased by 47000 times compared to the wild type enzyme with similar affinity for the substrate and the coenzyme
C151G
the mutant is completely inactive
C151S
the mutant shows drastically reduced kcat values compared to the wild type enzyme
H178N
the mutant shows no significant difference in the Km values of D-glyceraldehyde 3-phosphate, phosphate, and NAD+ compared to the wild type enzyme, however, the mutation results in the reduction of kcat of oxidative phosphorylation by 1400times
C151/H178N
-
the rate of the forward reaction is decreased by 47000 times compared to the wild type enzyme with similar affinity for the substrate and the coenzyme
-
C151G
-
the mutant is completely inactive
-
C151S
-
the mutant shows drastically reduced kcat values compared to the wild type enzyme
-
H178N
-
the mutant shows no significant difference in the Km values of D-glyceraldehyde 3-phosphate, phosphate, and NAD+ compared to the wild type enzyme, however, the mutation results in the reduction of kcat of oxidative phosphorylation by 1400times
-
C152S
site-directed mutagenesis, mutation of the catalytic residue inactivates the enzyme
S124A
site-directed mutagenesis, the mutant is phosphorylated in a similar way like the wild-type enzyme, but shows highly reduced activity
S205A
site-directed mutagenesis, the mutant is poorly or not phosphorylated, the mutant shows similar affinity for both substrates but near half of the Vmax compared to wild-type
S205D
site-directed mutagenesis, the mutant enzyme (mimicking the phosphorylated form) exhibits a sstrong decrease in activity but similar affinity toward substrates compared to wild-type. The catalytic efficiency is 330 and 410fold lower with NAD+ and Ga3P, respectively
S66A
site-directed mutagenesis, the mutant is phosphorylated in a similar way like the wild-type enzyme, the mutant shows similar affinity for both substrates but near half of the Vmax compared to wild-type
additional information