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Literature summary for 1.1.1.8 extracted from

  • He, Y.; Meng, X.; Fan, Q.; Sun, X.; Xu, Z.; Song, R.
    Cloning and characterization of two novel chloroplastic glycerol-3-phosphate dehydrogenases from Dunaliella viridis (2009), Plant Mol. Biol., 71, 193-205.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information the GPDH genes exhibit transient transcriptional induction of gene expression upon hypersalinity shock followed by a negative feedback of gene expression, the level of GPDH1 transcript reaches a maximum in 2 M NaCl, which is about 2fold more than that in 0.5 M NaCl Dunaliella viridis
additional information the GPDH genes exhibit transient transcriptional induction of gene expression upon hypersalinity shock followed by a negative feedback of gene expression, the level of isozyme GPDH2 transcript reaches a maximum in 1 M NaCl and although the GPDH2 transcript level almost remains constant in salinities ranging from 3 to 5 M NaCl Dunaliella viridis

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) pLysS cells Dunaliella viridis
expressed in Escherichia coli BL21(DE3) pLysScells Dunaliella viridis

Inhibitors

Inhibitors Comment Organism Structure
additional information GPDH1 transcript level decreases progressively with NaCl concentrations above 3-5 M, the expression level of GPDH1 in 5 M NaCl is only approximately a quarter of that in 2 M NaCl; the GPDH2 transcript level decreases to less than half the level in 1 M NaCl Dunaliella viridis
NaCl isozyme GPDH1 is severely inhibited by the addition of 100-200 mM NaCl; isozyme GPDH2 is severely inhibited by the addition of 100-200 mM NaCl Dunaliella viridis
phosphate phosphate at 5-10 mM severely inhibits the enzymatic activity of isozyme GPDH1; phosphate at 5-10 mM severely inhibits the enzymatic activity of isozyme GPDH2 Dunaliella viridis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0589
-
NADPH isozyme GPDH1 Dunaliella viridis
0.0589
-
NADH recombinant isozyme GDH2 Dunaliella viridis
0.0592
-
NADH isozyme GPDH2 Dunaliella viridis
0.0592
-
NADPH recombinant isozyme GDH1 Dunaliella viridis
0.0726
-
NADPH isozyme GPDH2 Dunaliella viridis
0.0726
-
NADPH recombinant isozyme GDH2 Dunaliella viridis
0.0905
-
NADH isozyme GPDH1 Dunaliella viridis
0.0905
-
NADH recombinant isozyme GDH1 Dunaliella viridis

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Dunaliella viridis 9507
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
76200
-
calculated from amino acid sequence Dunaliella viridis
77200
-
calculated from amino acid sequence Dunaliella viridis

Organism

Organism UniProt Comment Textmining
Dunaliella viridis C5H3W0
-
-
Dunaliella viridis C5H3W0 isozyme GPDH1
-
Dunaliella viridis C5H3W1
-
-
Dunaliella viridis C5H3W1 isozyme GPDH2
-
Dunaliella viridis SHU C5H3W0 isozyme GPDH1
-
Dunaliella viridis SHU C5H3W1 isozyme GPDH2
-

Purification (Commentary)

Purification (Comment) Organism
GSTrap column chromatography Dunaliella viridis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sn-glycerol 3-phosphate + NAD+
-
Dunaliella viridis dihydroxyacetone phosphate + NADH + H+
-
?
sn-glycerol 3-phosphate + NAD+ isozymes GPDH1 can utilize both NADH and NADPH as coenzymes but exhibits significantly higher activities when NADH is used as the coenzyme Dunaliella viridis dihydroxyacetone phosphate + NADH + H+
-
?
sn-glycerol 3-phosphate + NAD+
-
Dunaliella viridis SHU dihydroxyacetone phosphate + NADH + H+
-
?
sn-glycerol 3-phosphate + NAD+ isozymes GPDH1 can utilize both NADH and NADPH as coenzymes but exhibits significantly higher activities when NADH is used as the coenzyme Dunaliella viridis SHU dihydroxyacetone phosphate + NADH + H+
-
?
sn-glycerol 3-phosphate + NADP+
-
Dunaliella viridis dihydroxyacetone phosphate + NADPH + H+ the measured GPDH activity of isozyme GPDH1 with NADH is approximately twice of that observed with NADPH ?
sn-glycerol 3-phosphate + NADP+
-
Dunaliella viridis dihydroxyacetone phosphate + NADPH + H+ the measured GPDH activity of isozyme GPDH2 with NADH is approximately twice of that observed with NADPH ?
sn-glycerol 3-phosphate + NADP+ isozymes GPDH1 can utilize both NADH and NADPH as coenzymes but exhibits significantly higher activities when NADH is used as the coenzyme Dunaliella viridis dihydroxyacetone phosphate + NADPH + H+
-
?
sn-glycerol 3-phosphate + NADP+
-
Dunaliella viridis SHU dihydroxyacetone phosphate + NADPH + H+ the measured GPDH activity of isozyme GPDH1 with NADH is approximately twice of that observed with NADPH ?
sn-glycerol 3-phosphate + NADP+ isozymes GPDH1 can utilize both NADH and NADPH as coenzymes but exhibits significantly higher activities when NADH is used as the coenzyme Dunaliella viridis SHU dihydroxyacetone phosphate + NADPH + H+
-
?
sn-glycerol 3-phosphate + NADP+
-
Dunaliella viridis SHU dihydroxyacetone phosphate + NADPH + H+ the measured GPDH activity of isozyme GPDH2 with NADH is approximately twice of that observed with NADPH ?

Synonyms

Synonyms Comment Organism
GPDH1 isozyme Dunaliella viridis
GPDH1 isozyme, contains an extra phosphoserine phosphatase domain at the N-terminus in addition to C-terminal GPDH domains Dunaliella viridis
GPDH2 isozyme Dunaliella viridis
GPDH2 isozyme, contains an extra phosphoserine phosphatase domain at the N-terminus in addition to C-terminal GPDH domains Dunaliella viridis

Cofactor

Cofactor Comment Organism Structure
NADH isozyme GPDH1 can utilize both NADH and NADPH as coenzymes and exhibits significantly higher GPDH activity when NADH is used as the coenzyme Dunaliella viridis
NADH isozyme GPDH1 can utilize both NADH and NADPH as coenzymes but exhibit significantly higher activities when NADH is used as the coenzyme Dunaliella viridis
NADH isozyme GPDH2 can utilize both NADH and NADPH as coenzymes and exhibits significantly higher GPDH activity when NADH is used as the coenzyme Dunaliella viridis
NADH isozyme GPDH2 can utilize both NADH and NADPH as coenzymes but exhibit significantly higher activities when NADH is used as the coenzyme Dunaliella viridis