Information on EC 1.2.7.6 - glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.2.7.6
-
RECOMMENDED NAME
GeneOntology No.
glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glyceraldehyde-3-phosphate + H2O + 2 oxidized ferredoxin = 3-phospho-D-glycerate + 2 H+ + 2 reduced ferredoxin
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
gluconeogenesis II (Methanobacterium thermoautotrophicum)
-
-
Glycolysis / Gluconeogenesis
-
-
glycolysis V (Pyrococcus)
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
glycolysis
-
-
SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate:ferredoxin oxidoreductase
Contains tungsten-molybdopterin and iron-sulfur clusters. This enzyme is thought to function in place of glyceralde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase in the novel Embden-Meyerhof-type glycolytic pathway found in Pyrococcus furiosus [1]. It is specific for glyceraldehyde-3-phosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
162995-20-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
no activity in Aeropyrum pernix
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
-
the enzyme is involved in the modified Embden-Meyerhof pathway
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate + H2O + 2 oxidized ferredoxin
3-phospho-D-glycerate + 2 H+ + 2 reduced ferredoxin
show the reaction diagram
D-glyceraldehyde 3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
show the reaction diagram
D-glyceraldehyde-3-phosphate + H2O + oxidized benzyl viologen
3-phospho-D-glycerate + H+ + reduced benzyl viologen
show the reaction diagram
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
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
D-glyceraldehyde 3-phosphate + H2O + 2 oxidized ferredoxin
3-phospho-D-glycerate + 2 H+ + 2 reduced ferredoxin
show the reaction diagram
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
D-glyceraldehyde-3-phosphate + H2O + oxidized ferredoxin
3-phospho-D-glycerate + H+ + reduced ferredoxin
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
-
molybdopterin
content of Mo-GAPOR expressed in Escherichia coli strain BL21(DE3) is estimated to be 0.35 g-atoms per mol of protein
tungsten-molybdopterin
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
contains 1 molecule per enzyme
S2-
Mo-GAPOR expressed in Escherichia coli strain BL21(DE3) is estimated to contain 6.1 g-atoms of acid-labile sulfide per mol of protein
Tungsten
Zn2+
-
contains 2 molecules per enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
0.001-0.01 mM completely inhibits
crotonaldehyde
-
25% inhibition at 10 mM
D-Glyceraldehyde-3-phosphate
recombinant GAPOR is posttranscriptionally regulated as it exhibits pronounced and irreversible substrate inhibition. Inhibition is independent of benzyl viologen
Dithionite
formaldehyde
-
25% inhibition at 10 mM
glyceraldehyde-3-phosphate
-
substrate inhibition above 0.5 mM
O2
reversibly inactivates GAPOR purified from M9/Mo+ cultures. GAPOR activity of crude lysates is irreversibly inactivated
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-bisphosphoglycerate
-
stimulates
3-phosphoglycerate
-
stimulates
acetyl phosphate
-
stimulates
Ionic strength
-
particularly by polyanions
-
isopropyl-beta-D-thiogalactopyranoside
1 mM induces cultures at the exponential phase of growth
L-cysteine
reversibly activates GAPOR purified from M9/Mo+ cultures
maltose
stimulates about 4fold
potassium chloride
-
3.5fold activation at 200 mM
potassium phosphate
-
3.5fold activation at 200 mM
Sodium arsenate
-
3.5fold activation at 200 mM
Sodium citrate
-
3.5fold activation at 200 mM
Sodium sulfate
-
3.5fold activation at 200 mM
Tungsten
-
stimulates cell growth when added to the medium
additional information
enzyme is induced during glycolysis
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
benzyl viologen
-
0.043 - 0.28
D-glyceraldehyde 3-phosphate
0.028 - 0.043
D-Glyceraldehyde-3-phosphate
1
Oxidized benzyl viologen
pH 7.8, 50C
0.006
oxidized ferredoxin
-
pH 8.4, 70C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.07
-
substrate: D-glyceraldehyde 3-phosphate (cosubstrate: benzyl viologen), 50C, pH not specified in the publication, enzyme from starch-grown cells
0.15
cell free extract, at 50C
1.8
maximum specific activity of protein for Mo-GAPOR expressed in Escherichia coli strain BL21(DE3)
17
113fold purified, at 50C, with a yield of 0.2%; pH 7.8, 50C
30
-
purified enzyme
120
Mo-GAPOR purified from Escherichia coli strain Rosetta-gami 2(DE3)
140
-
purified enzyme
additional information
-
strictly anaerobic assay conditions
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7
60% of maximum activity
8.3
60% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
specific activity is 10fold higher in starch-grown cells than in lactate-grown cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56000
gel filtration
63000
-
1 * 63000, SDS-PAGE
64000
1 * 64000, SDS-PAGE
65000
1 * 65000, SDS-PAGE
66000
1 * 66000, SDS-PAGE
73000
-
gel filtration
74000
sequence determination
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7 - 8.3
60% activity at pH 7.7 and 8.3
692377
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
-
t1/2: 15 min
100
2 h, 70% residual activity; retains 70% of its activity upon incubation for 2 h (half-life, 500 min)
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
aerobic conditions: loss of about 50% activity in cell extract after 12 h at 23C
-
644692
O2-sensitive, t1/2 at 23C: 6 h
-
644691
sensitive against O2
-
644692
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, Tris-HCl buffer, pH 9, several weeks
23C, under argon, 12 h, no loss of activity in cell extract
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
30fold, under strictly anaerobic conditions
-
35fold, about 95% purity
; by gel filtration, 113fold, to homogeneity
to homogeneity
-
to more than 75% homogeneity, by gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis
pET46-Ek/LIC-GAPOR vector expressed in Escherichia coli strains BL21(DE3) or Rosetta-gami 2(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation