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Literature summary for 1.2.1.12 extracted from

  • Zinsser, V.L.; Hoey, E.M.; Trudgett, A.; Timson, D.J.
    Biochemical characterisation of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) from the liver fluke, Fasciola hepatica (2014), Biochim. Biophys. Acta, 1844, 744-749 .
    View publication on PubMed

Application

Application Comment Organism
drug development development of GAPDH inhibitors as anti-cancer and anti-parasitic agents Fasciola hepatica

Cloned(Commentary)

Cloned (Comment) Organism
FhGAPDH sequence comparisons, functional recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta(DE3) Fasciola hepatica

Inhibitors

Inhibitors Comment Organism Structure
additional information development of GAPDH inhibitors as anti-cancer and anti-parasitic agents Fasciola hepatica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information the recombinant protein shows no cooperativity towards glyceraldehyde 3-phosphate as a substrate, Michaelis-Menten kinetics with glyceraldehyde 3-phosphate as a substrate Fasciola hepatica

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
113000
-
recombinant enzyme, gel filtration Fasciola hepatica

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+ Fasciola hepatica
-
3-phospho-D-glyceroyl phosphate + NADH + H+
-
?

Organism

Organism UniProt Comment Textmining
Fasciola hepatica A0A068LJN3
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain Rosetta(DE3) by nickel affinity chromatography Fasciola hepatica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
Fasciola hepatica 3-phospho-D-glyceroyl phosphate + NADH + H+
-
?

Subunits

Subunits Comment Organism
dimer 2 * 37000, about, sequence calculation, ligands bound Fasciola hepatica
More purified recombinant FhGAPDH is a mixture of homodimers and tetramers, as judged by protein-protein crosslinking and analytical gel filtration. The addition of either NAD+ or glyceraldehyde 3-phosphate shifts this equilibrium towards a compact dimer, that is more stable than the unliganded one. Molecular modeling of FhGAPDH monomer, and of the enzyme as a tetramer, the quaternary structure is shown as a dimer of dimers arrangement, overview. Substrate binding induces conformational and oligomerisation changes in FhGAPDH, both glyceraldehyde 3-phosphate and NAD+ appear to favour the formation of dimers over tetramers Fasciola hepatica
tetramer 4 * 37000, about, sequence calculation and modeling Fasciola hepatica

Synonyms

Synonyms Comment Organism
FhGAPDH
-
Fasciola hepatica
GAPDH
-
Fasciola hepatica
glyceraldehyde 3-phosphate dehydrogenase
-
Fasciola hepatica

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at, NAD+ reduction Fasciola hepatica

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
the addition of either NAD+ or glyceraldehyde 3-phosphate shifts this equilibrium towards a compact dimer, that is more stable than the unliganded one, thermal scanning fluorimetry Fasciola hepatica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
assay at, NAD+ reduction Fasciola hepatica

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Fasciola hepatica
NADH
-
Fasciola hepatica

pI Value

Organism Comment pI Value Maximum pI Value
Fasciola hepatica sequence calculation
-
7.1

General Information

General Information Comment Organism
malfunction inhibition of GAPDH leads to substantially reduced energy generation Fasciola hepatica
additional information molecular modeling of FhGAPDH monomer, overview. Substrate binding induces conformational and oligomerisation changes in FhGAPDH, both glyceraldehyde 3-phosphate and NAD+ appear to favour the formation of dimers over tetramers Fasciola hepatica
physiological function glyceraldehyde 3-phosphate dehydrogenase (GAPDH) catalyses one of the two steps in glycolysis which generate the reduced coenzyme NADH. This reaction precedes the two ATP generating steps Fasciola hepatica