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Literature summary extracted from

  • Prüss, B.; Meyer, H.E.; Holldorf, A.W.
    Characterization of the glyceraldehyde 3-phosphate dehydrogenase from the extremely halophilic archaebacterium Haloarcula vallismortis (1993), Arch. Microbiol., 160, 5-11.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.2.1.12 it cannot be stabilized with sorbitol, glucose, polyethylene glycol 400, beta-alanine, glycine or glycerol Haloarcula vallismortis
1.2.1.12 stable for many days in all buffers, containing more than 2 mol/l salt Haloarcula vallismortis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.12 0.5 1 NAD+ 45°C, pH 7.8 Haloarcula vallismortis
1.2.1.12 1.25
-
 phosphate 45°C, pH 7.8 Haloarcula vallismortis
1.2.1.12 8.3
-
 arsenate 45°C, pH 7.8 Haloarcula vallismortis
1.2.1.12 15
-
 D-glyceraldehyde 3-phosphate 45°C, pH 7.8 Haloarcula vallismortis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.1.12 KCl exhibits its highest activity in 2 mol/l KCl at 45°C Haloarcula vallismortis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.12 38000
-
 4 * 38000, cetyltrimethyl ammonium bromide PAGE Haloarcula vallismortis
1.2.1.12 160000
-
 gel filtration Haloarcula vallismortis

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.12 Haloarcula vallismortis
-
-
-
1.2.1.12 Haloarcula vallismortis ATCC 29715
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.12
-
 Haloarcula vallismortis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.12 D-glyceraldehyde 3-phosphate + arsenate + NAD+ strictly NAD+-dependent enzyme. The maximal velocity for the reaction with arsenate instead of phosphate is about 10 times higher. The maximal reaction velocity is higher with arsenate because the degradation of the instable product phospho-arseno glyceric acid pushes the reaction into the direction of phospho-arseno glyceric acid formation Haloarcula vallismortis 3-phospho-D-glyceroyl arsenate + NADH + H+
-
 ?
1.2.1.12 D-glyceraldehyde 3-phosphate + arsenate + NAD+ strictly NAD+-dependent enzyme. The maximal velocity for the reaction with arsenate instead of phosphate is about 10 times higher. The maximal reaction velocity is higher with arsenate because the degradation of the instable product phospho-arseno glyceric acid pushes the reaction into the direction of phospho-arseno glyceric acid formation Haloarcula vallismortis ATCC 29715 3-phospho-D-glyceroyl arsenate + NADH + H+
-
 ?
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+ strictly NAD+-dependent enzyme Haloarcula vallismortis 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
1.2.1.12 D-glyceraldehyde 3-phosphate + phosphate + NAD+ strictly NAD+-dependent enzyme Haloarcula vallismortis ATCC 29715 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.12 tetramer 4 * 38000, cetyltrimethyl ammonium bromide PAGE Haloarcula vallismortis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.12 45
-
 the enzyme exhibits its highest activity in 2 mol/l KCl at 45°C Haloarcula vallismortis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.2.1.12 15
-
 activity is lost after several min below 15°C Haloarcula vallismortis
1.2.1.12 22
-
 at room temperature the enzyme is stable for several weeks Haloarcula vallismortis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.12 7.8
-
 assay at Haloarcula vallismortis

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.12 NAD+ strictly NAD+-dependent enzyme. No acitivity with NADP + as coenzyme can be detected Haloarcula vallismortis

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.2.1.12 Haloarcula vallismortis isoelectric focusing
-
 4.25