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Information on EC 1.2.1.13 - glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) and Organism(s) Spinacia oleracea and UniProt Accession P19866
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1.2.1.13 glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating)Specify your search results
Word Map
- 1.2.1.13
- chloroplast
- gapdhs
- phosphoribulokinase
-
nadp-linked
-
4.1.1.39
-
calvin
-
2.7.1.19
-
2.7.2.3
- 1,3-bisphosphoglycerate
-
nad-specific
-
calvin-benson
-
triose-p
- sedoheptulose
- ribulose-5-phosphate
- medicine
The taxonomic range for the selected organisms is: Spinacia oleracea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
glyceraldehyde-3-p dehydrogenase, nadp-glyceraldehyde-3-phosphate dehydrogenase, gapa1, nadp-gapdh, gapa-1, nadp-gpd, glyceraldehyde-3-dehydrogenase, photosynthetic gapdh, ov-gapdh, nadp-dependent gapdh, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide phosphate phosphorylating)
-
-
-
-
GAPDH
glyceraldehyde 3-phosphate dehydrogenase (NADP)
-
-
-
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glyceraldehyde phosphate dehydrogenase (nicotinamide adenine dinucleotide phosphate phosphorylating)
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-
-
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glyceraldehyde-P dehydrogenase
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-
-
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NAD(P)-GAPDH
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-
-
-
NADP+-dependent G-3-P dehydrogenase
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-
-
-
NADP-dependent glyceraldehyde phosphate dehydrogenase
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-
-
-
NADP-dependent glyceraldehydephosphate dehydrogenase
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-
-
-
NADP-glyceraldehyde phosphate dehydrogenase
-
-
-
-
NADP-glyceraldehyde-3-phosphate dehydrogenase
-
-
-
-
NADP-GPD
-
-
-
-
NADP-triose phosphate dehydrogenase
-
-
-
-
NADPH-D-GA3P
-
-
-
-
triosephosphate dehydrogenase (NADP+)
-
-
-
-
GAPDH
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate:NADP+ oxidoreductase (phosphorylating)
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CAS REGISTRY NUMBER
COMMENTARY
37250-87-6
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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 + NADH
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
-
-
?
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
-
?
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
-
-
-
?
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
the enzyme retains the deuterium at the C4 HA position, removing the hydrogen atom and is therefore a B(pro-S) specific dehydrogenase
-
?
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
only reaction of the reductive pentose phosphate cycle in chloroplasts that uses as a substrate reducing power, NADPH, that is generated photochemically
-
-
?
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
enzyme of Benson-Calvin cycle
-
?
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
regulatory enzyme of the reductive pentose phosphate cycle
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NAD+
3-phospho-D-glyceroyl phosphate + NADH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH
-
-
-
?
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH
-
-
-
r
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH
-
-
-
r
NATURAL SUBSTRATE
NATURAL 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
D-glyceraldehyde 3-phosphate + phosphate + NADP+
3-phospho-D-glyceroyl phosphate + NADPH + H+
-
-
-
?
3-phospho-D-glyceroyl phosphate + NADPH + H+
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
-
-
-
?
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
only reaction of the reductive pentose phosphate cycle in chloroplasts that uses as a substrate reducing power, NADPH, that is generated photochemically
-
-
?
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
enzyme of Benson-Calvin cycle
-
?
3-phospho-D-glyceroyl phosphate + NADPH
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
regulatory enzyme of the reductive pentose phosphate cycle
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
the residues Thr33 and Ser188 are involved in NADPH over NADH selectivity
NADPH
the residues Thr33 and Ser188 are involved in NADPH over NADH selectivity
NAD+
-
reaction stoichiometry of 8:1 for both coenzymes and substrates, formation of the characteristic Racker band upon binding of either NADP+ or NAD+ to the apoenzyme
NADP+
-
cofactor
287990, 287991, 287992, 287996, 288000, 288001, 288002, 288004, 288006, 288007, 288015, 288021, 288022, 288025, 288027, 288030, 288031, 288032, 288034
NADP+
-
reaction stoichiometry of 8:1 for both coenzymes and substrates, formation of the characteristic Racker band upon binding of either NADP+ or NAD+ to the apoenzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
iodoacetate
-
preincubation with glyceraldehyde-phosphate, 10fold molar excess over iodoacetate, prevents inactivation
sulfite
-
non-competitive inhibitor with respect to both NADPH and 3-phosphoglycerate
thioredoxin
-
a regulatory disulfide between Cys359 and Cys358 of the C-terminal extension of GapB does form in presence of oxidized thioredoxin. This covalent modification is required for the NAD+-dependent association into higher oligomers and inhibition of the NADPH-dependent activity
NAD+
-
promotes association of the enzyme protomer of 160000 Da into a regulatory conformer of 600000 Da with low NADPH activity during dark deactivation
NAD+
-
a regulatory disulfide between Cys359 and Cys358 of the C-terminal extension of GapB does form in presence of oxidized thioredoxin. This covalent modification is required for the NAD+-dependent association into higher oligomers and inhibition of the NADPH-dependent activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glycerate 1,3-bisphosphate
-
most effective on a molar basis in stimulating NADPH-activity of dark chloroplast extracts and purified enzyme
thioredoxin
-
enzyme is activated by thioredoxin that is reduced either photochemically with ferredoxin and ferredoxin-thioredoxin reductase or chemically with dithiothreitol
1,3-diphosphoglycerate
-
the role of the reduction of the enzyme in vivo is to increase its sensitivity towards the activator 1,3-bisphosphoglycerate. The actual activation and aggregation state of the enzyme in chloroplasts in light is regulated by the concentration of 1,3-diphosphoglycerate as activator in the stroma and its actual activity by the availability of 1,3-diphosphoglycerate as substrate
dithiothreitol
-
the role of the reduction of the enzyme in vivo is to increase its sensitivity towards the activator 1,3-bisphosphoglycerate
additional information
-
effect of an activator on the enzyme is selectively enhanced by either dithiothreitol-reduced thioredoxin-f or a cosolvent, and is inhibited by spermine
-
additional information
-
complete light activation at 25 W*m-2 photosynthetically active radiation
-
additional information
-
addition of organic solvents miscible in water to the activation process enhance the specific activity, cosolvents added during catalysis lower the rate of substrate conversion
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.29
NADH
-
with NADH as coenzyme, activation by 20 mM dithiothreitol and 0.021 mM 1,3-bisphosphoglycerate
0.01
3-phospho-D-glyceroyl phosphate
mutant enzyme T33A/S188A, reaction with NADH
0.012
3-phospho-D-glyceroyl phosphate
mutant enzyme S188A, reaction with NADH
0.012
3-phospho-D-glyceroyl phosphate
mutant enzyme T33A, reaction with NADH
0.012
3-phospho-D-glyceroyl phosphate
mutant enzyme T33A/S188A, reaction with NADPH
0.012
3-phospho-D-glyceroyl phosphate
native enzyme A3-GAPDH, reaction with NADH
0.013
3-phospho-D-glyceroyl phosphate
mutant enzyme S188A, reaction with NADPH
0.015
3-phospho-D-glyceroyl phosphate
native enzyme A3-GAPDH, reaction with NADPH
0.018
3-phospho-D-glyceroyl phosphate
mutant enzyme T33A, reaction with NADPH
0.015
3-phospho-D-glyceroyl phosphate
-
GapB, analyzed under reducing conditions
0.016
3-phospho-D-glyceroyl phosphate
-
with NADH as cofactor, activation by 20 mM dithiothreitol and 0.021 mM 1,3-bisphosphoglycerate
0.019
3-phospho-D-glyceroyl phosphate
-
A(plusCTE) mutant, analyzed under oxidizing conditions
0.02
3-phospho-D-glyceroyl phosphate
-
with NADPH as coenzyme, activation by 20 mM dithiothreitol and 0.021 mM 1,3-bisphosphoglycerate
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
0.024
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
0.06
NADPH
-
activation by 20 mM dithiothreitol and 0.021 mM 1,3-bisphosphoglycerate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). G3PA_SPIOL
401
0
43023
Swiss-Prot
Chloroplast (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
189000
-
tetrameric conformation of GAPDH-A2B2 stabilized by NADPH, estimated by gel filtration
232000
-
GapB mutant B(E326Q) in the presence of NADPH, estimated by 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
36225
-
x * 39355, subunit A, + x * 36225, subunit B, calculation from amino acid sequence
37000
38000
39355
-
x * 39355, subunit A, + x * 36225, subunit B, calculation from amino acid sequence
43000
491000
-
wild-type GapB in the presence of NADH, compatible with octameric structure, estimated by gel filtration
520000
553000
-
GapB mutant B(S188A) in the presence of NADH, compatible with octameric structure, estimated by gel filtration
600000
760000
-
oligomer of GAPDH in the presence of NADH, suggesting A8B8 stoichiometry, estimated by gel filtration
37000
-
x * 43000 + x * 37000, molar ratio of the subunits is 1:1, GAPDH I, SDS-PAGE
37000
-
x * 43000 + x * 37000, excess of the lighter subunit, GAPDH II, SDS-PAGE
43000
-
x * 43000 + x * 37000, molar ratio of the subunits is 1:1, GAPDH I, SDS-PAGE
43000
-
x * 43000 + x * 37000, excess of the lighter subunit, GAPDH II, SDS-PAGE
520000
-
GapB mutant B(E326Q) in the presence of NADH, compatible with octameric structure, estimated by gel filtration
520000
-
GapB mutant B(R77A) in the presence of NADH, compatible with octameric structure, estimated by gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
?
-
x * 43000 + x * 37000, molar ratio of the subunits is 1:1, GAPDH I, SDS-PAGE
?
-
x * 43000 + x * 37000, excess of the lighter subunit, GAPDH II, SDS-PAGE
?
-
x * 39355, subunit A, + x * 36225, subunit B, calculation from amino acid sequence
additional information
-
structural characterization of the subunits, the subunits have a very similar amino acid composition
additional information
-
enzyme is freely interconvertible between protomers of the 160000 Da form or the 300000 Da intermediate form with high NADPH-activity, produced in the light by the action of thioredoxin and activating metabolites, and a regulatory 600000 Da conformer with lower NADPH-activity produced in darkness or when photosynthesis is inhibited
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method is used to grow crystals of recombinant A4-GAPDH, T33A and S188A A4-GAPDH mutants complexed with NADP+
molecular docking of ferredoxin-NADP-reductase EC 1.18.1.2 and GAPD. enzymes are able to form at least two different complexes, one involving a single GAPD monomer and an ferredoxin-NADP-reductase monomer or dimer. The amino acid residues located at the putative interface are highly conserved on the chloroplastic forms of both enzymes. The other potential complex involves the GAPD A2B2 tetramer and an FNR monomer or dimer. Ferredoxin is able to interact with FNR in either complex
sitting drop vapour diffusion method with 2.0-2.5 M or 1.5-1.2 M ammonium sulfate and 0.1 M potassium phosphate (pH 7.0-8.0)
two crystal forms of the A4-GAPDH isoform are used to solve the structure of the apo form to a resolution of 3.0 A
crystal structure of the non-regulatory A(4) isoform of glyceraldehyde-3-phosphate dehydrogenase complexed with NADP+
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E356Q/E357Q
complete redox insensitivity is achieved in the double mutant
S188A
affinity for NADPH is significantly decreased, decrease in the ratio of turnover number to Km-value in the NADPH-dependent reaction, significant expansion of the A4-tetramer
T33A
affinity for NADPH is significantly decreased, turnover-number for NADPH is lowered
T33A/S188A
affinity for NADPH is significantly decreased, turnover-number for NADPH is lowered
C349S
-
mutant of GapB subunit is less redox-sensitive than GapB. Active tetramer, unable to aggregate to higher oligomers in presence of NAD+
C349S/C358S
-
mutant of GapB subunit is less redox-sensitive than GapB. Active tetramer, unable to aggregate to higher oligomers in presence of NAD+
c358S
-
mutant of GapB subunit is less redox-sensitive than GapB. Active tetramer, unable to aggregate to higher oligomers in presence of NAD+
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxidation typically leads to about 50% inhibition of the NADPH-dependent activity
689747
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, GAPDH I is stable for several months, GAPDH II and GAPDH III spontaneously lose activity
-
4°C, pH 8.5, protein concentration 2.5 mg/ml, apoprotein, complete loss of activity after 48 h
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wolosiuk, R.A.; Stein, M.
Modulation of spinach chloroplast NADP-glyceraldehyde-3-phosphate dehydrogenase by chaotropic anions
Arch. Biochem. Biophys.
279
70-77
1990
Spinacia oleracea
Ferri, G.; Stoppini, M.; Meloni, M.L.; Zapponi, M.C.; Iadarola, P.
Chloroplast glyceraldehyde-3-phosphate dehydrogenase (NADP): amino acid sequence of the subunits from isoenzyme I and structural relationship with isoenzyme II
Biochim. Biophys. Acta
1041
36-42
1990
Spinacia oleracea
Levy, L.M.; Betts, G.F
Stereospecificity of C4 nicotinamide hydrogen transfer of the NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
Biochim. Biophys. Acta
997
331-333
1989
Spinacia oleracea
Ferri, G.; Stoppini, M.; Iadarola, P.; Zapponi, M.C.; Galliano, M.; Minchiotti, L.
Structural characterization of the subunit of spinach chloroplast glyceraldehyde-3-phosphate dehydrogenase (NADP)
Biochim. Biophys. Acta
915
149-156
1987
Spinacia oleracea
-
Iadarola, P.; Bonferoni, C.; Ferri, G.; Stoppini, M.; Zapponi, M.C.
Reversed-phase high-performance liquid chromatographic separation and partial structural characterization of chloroplast glyceraldehyde-3-phosphate dehydrogenase
J. Chromatogr.
359
423-432
1986
Spinacia oleracea
-
Wolosiuk, R.A.; Hertig, C.M.; Busconi, L.
Activation of spinach chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by concerted hysteresis
Arch. Biochem. Biophys.
246
1-8
1986
Spinacia oleracea
Ripamonti, F.S.; Sabatino, P.; Zanotti, G.; Scagliarini, S.; Sparla, F.; Trost, P.
Crystal structure of the non-regulatory A(4) isoform of spinach chloroplast glyceraldehyde-3-phosphate dehydrogenase complexed with NADP+
J. Mol. Biol.
314
527-542
2001
Spinacia oleracea
Wolosiuk, R.A.; Corley, E.; Crawford, N.A.; Buchanan, B.B.
Dual effects of organic solvents on chloroplast phosphoribulokinase
FEBS Lett.
189
212-216
1985
Spinacia oleracea
-
Iadarola, P.; Zapponi, M.C.; Ferri, G.
Molecular forms of chloroplast glyceraldehyde-3-P-dehydrogenase
Experientia
39
50-52
1983
Spinacia oleracea
-
Zapponi, M.C.; Berni, R.; Iadarola, P.; Ferri, G.
Spinach chloroplast glyceraldehyde-3-phosphate dehydrogenase (NADP). Formation of complexes with coenzymes and substrates
Biochim. Biophys. Acta
744
260-264
1983
Spinacia oleracea
-
Cerff, R.
Quaternary structure of higher plant glyceraldehyde-3-phosphate dehydrogenases
Eur. J. Biochem.
94
243-247
1979
Hordeum vulgare, Pisum sativum, Spinacia oleracea
Wolosiuk, R.A.; Buchanan, B.B.
Activation of chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by ferredoxin/thioredoxin system
Plant Physiol.
61
669-671
1978
Spinacia oleracea
Ferri, G.; Comerio, G.; Iadarola, P.; Zapponi, M.C.; Speranza, M.L.
Subunit structure and activity of glyceraldehyde-3-phosphate dehydrogenase from spinach chloroplasts
Biochim. Biophys. Acta
522
19-31
1978
Spinacia oleracea
Ziegler, I.; Marewa, A.; Schoepe, E.
Action of sulphite on the substrate kinetics of chloroplastic NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
Phytochemistry
15
1627-1632
1976
Spinacia oleracea
-
Yonuschot, G.R.; Ortwerth, B.J.; Koeppe, O.J.
Purification and properties of a nicotinamide adenine dinucleotide phosphate-requiring glyceraldehyde 3-phosphate dehydrogenase from spinach leaves
J. Biol. Chem.
245
4193-4198
1970
Spinacia oleracea
Trost, P.; Scagliarini, S.; Valenti, V.; Pupillo, P.
Activation of spinach chloroplast glyceraldehyde 3-phosphate dehydrogenase: effect of glycerate 1,3-bisphosphate
Planta
190
320-326
1993
Spinacia oleracea
-
Scagliarini, S.; Trost, P.; Pupillo, P.; Valenti, V.
Light activation and molecular-mass changes of NAD(P)-glyceraldehyde 3-phosphate dehydrogenase of spinach and maize leaves
Planta
190
313-319
1993
Spinacia oleracea, Zea mays
-
Baalmann, E.; Backhausen, J.E.; Rak, C.; Vetter, S.; Scheibe, R.
Reductive modification and nonreductive activation of purified spinach chloroplast NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
Arch. Biochem. Biophys.
324
201-208
1995
Spinacia oleracea
Wolosiuk, R.A.; Buchanan, B.B.
Studies on the regulation of chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase
J. Biol. Chem.
251
6456-6461
1976
Spinacia oleracea
Sparla, F.; Pupillo, P.; Trost, P.
The C-terminal extension of glyceraldehyde-3-phosphate dehydrogenase subunit B acts as an autoinhibitory domain regulated by thioredoxins and nicotinamide adenine dinucleotide
J. Biol. Chem.
277
44946-44952
2002
Spinacia oleracea
Sparla, F.; Fermani, S.; Falini, G.; Zaffagnini, M.; Ripamonti, A.; Sabatino, P.; Pupillo, P.; Trost, P.
Coenzyme site-directed mutants of photosynthetic A4-GAPDH show selectively reduced NADPH-dependent catalysis, similar to regulatory AB-GAPDH inhibited by oxidized thioredoxin
J. Mol. Biol.
340
1025-1037
2004
Spinacia oleracea (P19866)
Camara-Artigas, A.; Hirasawa, M.; Knaff, D.B.; Wang, M.; Allen, J.P.
Crystallization and structural analysis of GADPH from Spinacia oleracea in a new form
Acta Crystallogr. Sect. F
62
1087-1092
2006
Spinacia oleracea (P19866)
Sparla, F.; Zaffagnini, M.; Wedel, N.; Scheibe, R.; Pupillo, P.; Trost, P.
Regulation of photosynthetic GAPDH dissected by mutants
Plant Physiol.
138
2210-2219
2005
Spinacia oleracea
Negi, S.S.; Carol, A.A.; Pandya, S.; Braun, W.; Anderson, L.E.
Co-localization of glyceraldehyde-3-phosphate dehydrogenase with ferredoxin-NADP reductase in pea leaf chloroplasts
J. Struct. Biol.
161
18-30
2008
Pisum sativum, Spinacia oleracea (P19866), Spinacia oleracea
Fermani, S.; Sparla, F.; Falini, G.; Martelli, P.L.; Casadio, R.; Pupillo, P.; Ripamonti, A.; Trost, P.
Molecular mechanism of thioredoxin regulation in photosynthetic A2B2-glyceraldehyde-3-phosphate dehydrogenase
Proc. Natl. Acad. Sci. USA
104
11109-11114
2007
Spinacia oleracea (P19866), Spinacia oleracea
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