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Literature summary for 1.2.1.12 extracted from

  • Sangolgi, P.B.; Balaji, C.; Dutta, S.; Jindal, N.; Jarori, G.K.
    Cloning, expression, purification and characterization of Plasmodium spp. glyceraldehyde-3-phosphate dehydrogenase (2016), Protein Expr. Purif., 117, 17-25 .
    View publication on PubMed

Application

Application Comment Organism
drug development Gapdh can be an effective target for anti-malarial chemotherapeutics Plasmodium yoelii
drug development Gapdh can be an effective target for anti-malarial chemotherapeutics. Enzyme PfGapdh shows an extra ligand binding capacity in the vicinity of the NAD+ binding region of the active site that may offer an opportunity to design and develop novel antimalarials Plasmodium falciparum

Cloned(Commentary)

Cloned (Comment) Organism
Gapdh gene is located on chromosome 14, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3), addition of 36 amino acid residues (MGS SHHHHHHSSGLVPRGSHMASMTGGNNMGRGSGF-) at the N-terminus of rPfGapdh Plasmodium falciparum

Inhibitors

Inhibitors Comment Organism Structure
ferriprotoporphyrin IX strongly inhibits PfGapdh, in contrast to the human GAPDH Plasmodium falciparum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics Plasmodium falciparum
0.25
-
D-glyceraldehyde 3-phosphate recombinant enzyme, pH and temperature not specified in the publication Plasmodium falciparum
0.28
-
NAD+ recombinant enzyme, pH and temperature not specified in the publication Plasmodium falciparum

Localization

Localization Comment Organism GeneOntology No. Textmining
cell membrane
-
Plasmodium yoelii
-
-
cytoskeleton
-
Plasmodium yoelii 5856
-
cytosol
-
Plasmodium yoelii 5829
-
additional information analysis of the subcellular distribution of Gapdh, overview Plasmodium yoelii
-
-
nucleus
-
Plasmodium yoelii 5634
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
150000
-
recombinant N-terminally prolongated enzyme, gel filtration Plasmodium falciparum
161984
-
recombinant N-terminally prolongated enzyme, mass spectrometry Plasmodium falciparum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+ Plasmodium falciparum
-
3-phospho-D-glyceroyl phosphate + NADH + H+
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+ Plasmodium yoelii
-
3-phospho-D-glyceroyl phosphate + NADH + H+
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+ Plasmodium yoelii 17XL
-
3-phospho-D-glyceroyl phosphate + NADH + H+
-
?
additional information Plasmodium falciparum interaction of recombinant PfGapdh with Pfeno, human plasminogen, lysozyme and alpha-tubulin ?
-
?

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum Q8T6B1
-
-
Plasmodium yoelii V7PVE5 grown in mice
-
Plasmodium yoelii 17XL V7PVE5 grown in mice
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information Plasmodium yoelii, Gapdh undergoes multiple posttranslational modifications Plasmodium yoelii
phosphoprotein multiple phosphorylations changing the pI of the enzyme, overview Plasmodium yoelii

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme 2.8fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Plasmodium falciparum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
12.6
-
purified recombinant enzyme, pH and temperature not specified in the publication Plasmodium falciparum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
Plasmodium falciparum 3-phospho-D-glyceroyl phosphate + NADH + H+
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
Plasmodium yoelii 3-phospho-D-glyceroyl phosphate + NADH + H+
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
Plasmodium yoelii 17XL 3-phospho-D-glyceroyl phosphate + NADH + H+
-
?
additional information interaction of recombinant PfGapdh with Pfeno, human plasminogen, lysozyme and alpha-tubulin Plasmodium falciparum ?
-
?

Subunits

Subunits Comment Organism
? x * 27000 + x * 37000 + x * 51000, SDS-PAGE Plasmodium yoelii
homotetramer 4 * 36636, wild-type enzyme, sequence calculation, 4 * 40000, about, recombinant N-terminally prolongated enzyme, SDS-PAGE, 4 * 40355, recombinant N-terminally prolongated enzyme, sequence calculation Plasmodium falciparum
More the 51 kDa enzyme form is present only in the soluble fraction of the cell extract Plasmodium yoelii

Synonyms

Synonyms Comment Organism
glyceraldehyde-3-phosphate dehydrogenase
-
Plasmodium falciparum
glyceraldehyde-3-phosphate dehydrogenase
-
Plasmodium yoelii
PfGAPDH
-
Plasmodium falciparum
PyGapdh
-
Plasmodium yoelii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.6
-
assay at Plasmodium yoelii
9
-
recombinant enzyme Plasmodium falciparum

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Plasmodium falciparum
NAD+
-
Plasmodium yoelii

pI Value

Organism Comment pI Value Maximum pI Value
Plasmodium yoelii in the cytosolic fraction, variants with mass of about 37 kDa have multiple spots. There are 3-4 spots that have a pI below 8. These spots have a pI of 7.6, 7.2 and 7.0, indicative of multiple phosphorylations, the binding of rPfGapdh with Pfeno, plasminogen, alpha-tubulin and lysozyme is specific
-
additional information
Plasmodium falciparum recombinant wild-type enzyme, sequence calculation and isoelectric focusing
-
7.77
Plasmodium yoelii sequence calculation
-
7.95
Plasmodium falciparum recombinant N-terminally prolongated enzyme, sequence calculation and isoelectric focusing
-
8.33

General Information

General Information Comment Organism
physiological function enzyme Gapdh is likely to have multiple nonglycolytic functions in the parasite in additon to its function in glycolysis. During intra-erythrocytic phage of its life cycle in humans, the parasite solely relies on glycolysis for its energy needs Plasmodium falciparum
physiological function enzyme Gapdh is likely to have multiple nonglycolytic functions in the parasite in additon to its function in glycolysis. During intra-erythrocytic phage of its life cycle in humans, the parasite solely relies on glycolysis for its energy needs. PfGapdh appearing on the parasite cell surface can bind to extracellular proteins for moonlighting functions due to its specific interactions with with Pfeno, plasminogen, alpha-tubulin and lysozyme Plasmodium yoelii