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Literature summary for 1.2.1.12 extracted from

  • Fourrat, L.; Iddar, A.; Valverde, F.; Serrano, A.; Soukri, A.
    Cloning, gene expression and characterization of a novel bacterial NAD-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Neisseria meningitidis strain Z2491 (2007), Mol. Cell. Biochem., 305, 209-219.
    View publication on PubMed
Search for more literature for 1.2.1.12

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli XL1-blue cells transformed with pNeis2 Neisseria meningitidis

Inhibitors

Inhibitors Comment Organism Structure
beta-mercaptoethanol strong inhibition at 10 mM Neisseria meningitidis
dithiothreitol strong inhibition at 2 mM Neisseria meningitidis
additional information NADH, glucose-1-phosphate, AMP, ADP, ATP, and fructose-6-phosphate do not affect kinetic properties of GAPN and no change in cofactor preference from NAD+ to NADP+ in the presence of these metabolic intermediates is detected Neisseria meningitidis
NADP+ 75% inhibition in the presence of 2 mM NADP+ Neisseria meningitidis
NADPH
-
 Neisseria meningitidis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.057
-
 NAD+ recombinant enzyme, in the presence of D-glyceraldehyde 3-phosphate, in 50 mM Tricine buffer (pH 8.5), at 25°C Neisseria meningitidis
0.088
-
 NAD+ recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), in the presence of glyceraldehyde, at 25°C Neisseria meningitidis
0.109
-
 NAD+ recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), in the presence of acetaldehyde, at 25°C Neisseria meningitidis
0.2
-
 glyceraldehyde recombinant enzyme, at 25°C Neisseria meningitidis
0.31
-
 acetaldehyde recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), at 25°C Neisseria meningitidis
1.45
-
 D-glyceraldehyde 3-phosphate recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), at 25°C Neisseria meningitidis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
 4 * 50000, SDS-PAGE Neisseria meningitidis
51000
-
 4 * 51000, native PAGE slab gels with varying acrylamide concentrations of 5-10% (w/v) in the absence of SDS Neisseria meningitidis
200000
-
 SDS-PAGE Neisseria meningitidis
208000
-
 native PAGE slab gels with varying acrylamide concentrations of 5-10% (w/v) in the absence of SDS Neisseria meningitidis
209200
-
 calculated from amino acid sequence Neisseria meningitidis

Organism

Organism UniProt Comment Textmining
Neisseria meningitidis
-
-
-
Neisseria meningitidis Z2491
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, DEAE-cellulose DE-52 column chromatography, and Cibacron Blue Sepharose column chromatography Neisseria meningitidis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.52
-
 recombinant enzyme from crude extract, in 50 mM Tricine buffer (pH 8.5), at 25°C Neisseria meningitidis
2.16
-
 crude extract, at 25°C Neisseria meningitidis
25.1
-
 recombinant enzyme after 48.3fold purification, in 50 mM Tricine buffer (pH 8.5), at 25°C Neisseria meningitidis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetaldehyde + phosphate + NAD+
-
 Neisseria meningitidis acetyl phosphate + NADH
-
 ?
acetaldehyde + phosphate + NAD+
-
 Neisseria meningitidis Z2491 acetyl phosphate + NADH
-
 ?
D-glyceraldehyde 3-phosphate + NAD+
-
 Neisseria meningitidis D-3-phosphoglycerate + NADH
-
 ?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Neisseria meningitidis 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Neisseria meningitidis Z2491 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
glyceraldehyde + NAD+ + H2O
-
 Neisseria meningitidis glycerate + NADH + H+
-
 ?
glyceraldehyde + NAD+ + H2O
-
 Neisseria meningitidis Z2491 glycerate + NADH + H+
-
 ?
glyceraldehyde 3-phosphate + NAD+
-
 Neisseria meningitidis ? + NADH
-
 ?
glyceraldehyde 3-phosphate + NAD+
-
 Neisseria meningitidis Z2491 ? + NADH
-
 ?
additional information no activity with NADP+ Neisseria meningitidis ?
-
 ?
additional information no activity with NADP+ Neisseria meningitidis Z2491 ?
-
 ?

Subunits

Subunits Comment Organism
homotetramer 4 * 50000, SDS-PAGE Neisseria meningitidis
homotetramer 4 * 51000, native PAGE slab gels with varying acrylamide concentrations of 5-10% (w/v) in the absence of SDS Neisseria meningitidis

Synonyms

Synonyms Comment Organism
GAPDH
-
 Neisseria meningitidis
GAPN
-
 Neisseria meningitidis
NAD-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
 Neisseria meningitidis
NAD-dependent phosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
 Neisseria meningitidis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
64
-
-
 Neisseria meningitidis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.03
-
 acetaldehyde recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), at 25°C Neisseria meningitidis
4.35
-
 glyceraldehyde recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), at 25°C Neisseria meningitidis
24.51
-
 D-glyceraldehyde 3-phosphate recombinant enzyme, in 50 mM Tricine buffer (pH 8.5), at 25°C Neisseria meningitidis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9 10
-
 Neisseria meningitidis

Cofactor

Cofactor Comment Organism Structure
additional information undetectable activity with NADP+ Neisseria meningitidis
NAD+
-
 Neisseria meningitidis
NAD+ absolute specificity for NAD+ Neisseria meningitidis

pI Value

Organism Comment pI Value Maximum pI Value
Neisseria meningitidis isoelectric focusing
-
 6.3