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Literature summary for 1.2.1.12 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
Search for more literature for 1.2.1.12

General Stability

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

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Haloarcula vallismortis
-
-
-
Haloarcula vallismortis ATCC 29715
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Haloarcula vallismortis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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+
-
 ?
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+
-
 ?
D-glyceraldehyde 3-phosphate + phosphate + NAD+ strictly NAD+-dependent enzyme Haloarcula vallismortis 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
D-glyceraldehyde 3-phosphate + phosphate + NAD+ strictly NAD+-dependent enzyme Haloarcula vallismortis ATCC 29715 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?

Subunits

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

Temperature Optimum [°C]

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

Temperature Stability [°C]

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

pH Optimum

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

Cofactor

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

pI Value

Organism Comment pI Value Maximum pI Value
Haloarcula vallismortis isoelectric focusing
-
 4.25