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

EC NUMBER
COMMENTARY hide
1.2.1.9
-
RECOMMENDED NAME
GeneOntology No.
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glyceraldehyde 3-phosphate + NADP+ + H2O = 3-phospho-D-glycerate + NADPH + 2 H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glycolysis IV (plant cytosol)
-
-
Entner Doudoroff pathway
-
-
glycolysis
-
-
Glycolysis / Gluconeogenesis
-
-
Pentose phosphate pathway
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate:NADP+ oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9028-92-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
peanut
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
sugar beet
-
-
Manually annotated by BRENDA team
lesser celandine
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
hyperthermophilic archaeon
-
-
Manually annotated by BRENDA team
no activity in Penicillium chrysogenum
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
Peptoclostridium difficile
-
Uniprot
Manually annotated by BRENDA team
light-inducible
-
-
Manually annotated by BRENDA team
castor bean
-
-
Manually annotated by BRENDA team
; Streptococcus bovis gapN, sequence of gapN gene of S. mutans and S. pyogenes used for PCR primer design, Q59931, Q99Z67
SwissProt
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
DELTAgapN cells do not grow under glycolytic conditions
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
show the reaction diagram
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + 2 H+
show the reaction diagram
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + H+
show the reaction diagram
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADP+ + H+
show the reaction diagram
-
-
-
ir
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
show the reaction diagram
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
show the reaction diagram
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
r
D-glyceraldehyde-3-phosphate + 1,N6-ethenoadenine-nicotinamide dinucleotide phosphate
D-3-phosphoglycerate + ?
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde-3-phosphate + 3-acetylpyridine-adenine dinucleotide phosphate
D-3-phosphoglycerate + ?
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde-3-phosphate + beta-nicotinamide adenine dinucleotide 2',3'-cyclic monophosphate
D-3-phosphoglycerate + ?
show the reaction diagram
-
-
-
-
?
D-glyceraldehyde-3-phosphate + NAD+
D-3-phosphoglycerate + NADH + H+
show the reaction diagram
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
show the reaction diagram
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH + H+
show the reaction diagram
D-glyceraldehyde-3-phosphate + nicotinamide-hypoxanthine dinucleotide phosphate
D-3-phosphoglycerate + ?
show the reaction diagram
-
-
-
-
?
DL-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-DL-glycerate + NADH + H+
show the reaction diagram
DL-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-DL-glycerate + NADPH + H+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
show the reaction diagram
D-glyceraldehyde 3-phosphate + NAD+ + H2O
3-phospho-D-glycerate + NADH + H+
show the reaction diagram
-
NAD+ is a poor co-substrate
-
-
-
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADP+ + H+
show the reaction diagram
Q3C1A6
-
-
-
ir
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + 2 H+
show the reaction diagram
D-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-D-glycerate + NADPH + H+
show the reaction diagram
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
r
D-glyceraldehyde-3-phosphate + NADP+
D-3-phosphoglycerate + NADPH
show the reaction diagram
DL-glyceraldehyde 3-phosphate + NADP+ + H2O
3-phospho-DL-glycerate + NADPH + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,N6-ethenoadenine-nicotinamide dinucleotide phosphate
-
-
3-acetylpyridine-adenine dinucleotide phosphate
-
-
beta-nicotinamide adenine dinucleotide 2',3'-cyclic monophosphate
-
-
nicotinamide-hypoxanthine dinucleotide phosphate
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
-
stimulation
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
Na+
-
stimulation
NH4+
-
stimulation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-aminopyridine
-
competitive
3-phosphohydroxypyruvate
beta-Glycerophosphate
-
competitive
chloroplast protein CP12
-
the chloroplast protein CP12 behaves as a negative regulator of GAPDH activity
-
CP-12 protein
-
-
-
D-3-phosphoglycerate
D-erythrose 4-phosphate
D-glyceraldehyde 3-phosphate
-
substrate inhibition
D-Glyceraldehyde-3-phosphate
-
-
D-ribose 5-phosphate
-
-
Diamide
diphosphate
-
after interaction with the 14-3-3 regulatory protein the phosphorylated enzyme exhibits higher sensitivity to inhibition
DL-alpha-glycerophosphate
-
competitive
DL-glyceraldehyde
-
competitive
galactonate
slight inhibition; slight inhibition (1.2 to 1.3fold); slight inhibition (1.2 to 1.3fold)
gluconate
slight inhibition
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
iodoacetamide
L-alpha-glycerophosphate
-
competitive
L-Glyceraldehyde 3-phosphate
NADPH
phosphate
-
-
Phosphoglycolate
sedoheptulose 7-phosphate
-
-
sodium nitroprusside
-
-
Thionicotinamide
-
competitive
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-O-phosphono-D-fructofuranose
minor stimulatory effect
ADP
-
3 mM, in coupled assay with aldolase
ATP
-
3 mM, in coupled assay with aldolase
D-fructose
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
methyl viologen
NADP+
pyruvate
minor stimulatory effect
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
1.2 - 29.3
NAD+
0.42
NADH
-
3-phosphoglycerate
0.0035 - 0.385
NADP+
0.019 - 0.3
NADPH
0.033
nicotinamide-hypoxanthine dinucleotide phosphate
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.13 - 341
D-glyceraldehyde 3-phosphate
0.06 - 103
D-Glyceraldehyde-3-phosphate
additional information
additional information
Chlamydomonas reinhardtii
-
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
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.378 - 1.63
NAD+
7
48.1 - 203
NADP+
10
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00045
3-aminopyridine
-
-
0.339
beta-Glycerophosphate
-
-
0.525
D-3-phosphoglycerate
-
-
36.5
D-glyceraldehyde 3-phosphate
-
in 100 mM MES/KOH (pH 7.0), at 70C
0.54 - 1.9
D-Glyceraldehyde-3-phosphate
0.45
DL-alpha-glycerophosphate
-
-
1.05
DL-glyceraldehyde
-
-
2.5
GSSG
-
pH and temperature not specified in the publication
6.3 - 254
hydrazin
4.7 - 95
hydroxylamine
0.94
L-alpha-glycerophosphate
-
-
0.0055 - 0.037
L-Glyceraldehyde 3-phosphate
0.6
sodium nitroprusside
-
pH and temperature not specified in the publication
0.00034
Thionicotinamide
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
0.014
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
0.016
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
0.038
-
-
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
0.065
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
26.9
-
purified enzyme, NADH
32.4
-
purified enzyme
150.5
-
purified native and recombinat enzyme, NADPH
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
at 60C; at 60C
8.3
activity assay
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6 - 8.8
-
-
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
activity assay at room temperature
23
activity assay at room temperature
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
-
chromatofocusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
aqueous phase of latex after centrifugation at 38000 x g
-
Manually annotated by BRENDA team
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)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46000
determined by SDS-PAGE and immunodetection
47000
determined by SDS-PAGE and immunodetection
48000
determined by SDS-PAGE and immunodetection
49000
determined by SDS-PAGE and immunodetection
56930
subunit, calculated from amino acid sequence; subunit, calculated from amino acid sequence; subunit, calculated from amino acid sequence
132000
-
GapA, estimated by gel filtration
151000
-
B(minCTE) mutant, estimated by gel filtration
160000
-
gel filtration
189000
190000 - 200000
204000
-
non-denaturing PAGE
223000
-
gel filtration
224000
-
non-denaturing PAGE
227000
-
gel filtration; gel filtration
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
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
tetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
6 min, 89% inactivation
70
-
10 min, inactivation above
75
-
10 min, complete inactivation
95
-
10 min, complete inactivation
additional information
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
native and recombinant enzyme resistent to 1 mM H2O2
-
288345
no inactivation by 1 mM H2O2 after 35 min, NADP+ has no effect
-
654427
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 0.01 M potassium phosphate buffer, pH 6.4, 2 mM dithiothreitol, 50% v/v glycerol, 3 months
-
0-4C, 50 mM Tris-HCl buffer, pH 7.5, 1 mM EDTA, 10 mM mercaptoethanol, at least 6 months, or precipitated in 60% ammonium sulfate
-
4C, 25 mM Tris-HCl buffer, pH 7.5, 0.1 mM EDTA, 10 mM mercaptoethanol, at least 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; HisTrap column chromatography and Superdex 200 gel filtration
-
cell-free extract preparation
DEAE Trisacryl column chromatography
-
heat precipitation and Superdex 200 gel filtration; Superdex 200 gel filtration; Superdex 200 gel filtration
heat treatment (85C, 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
using a Q-Sepharose HP and a MonoQ anion-exchange column
-
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 BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) CodonPlus RIL cells
-
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
expression in Escherichia coli BL-21
-
into the pET29 vector for expression in Escherichia coli BL21DE3 cells
-
into the pGEM-T easy vector for sequencing
overexpression in Escherichia coli BL21(DE3)-pLysS
-
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
the enzyme is not down-regulated in the dark
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
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
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%; the mutant shows reduced catalytic efficiency with NADP+ and increased catalytic efficiency with NAD+ as compared to the 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
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%; the mutant shows reduced catalytic efficiency with NADP+ and increased catalytic efficiency with NAD+ as compared to the wild type enzyme
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
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kcat for D-glyceraldehyde 3-phosphate is 2.8fold lower than wild-type value
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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%
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additional information
Show AA Sequence (508 entries)
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