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Literature summary for 2.6.1.1 extracted from

  • Muriana, F.J.G.; Alvarez-Ossorio, M.C.; Relimpio, A.
    Purification and characterization of aspartate aminotransferase from the halophile archaebacterium Haloferax mediterranei (1991), Biochem. J., 278, 149-154.
No PubMed abstract available
Search for more literature for 2.6.1.1

General Stability

General Stability Organism
inactivation at 1.3 M NaCl and KCl Haloferax mediterranei

Inhibitors

Inhibitors Comment Organism Structure
KCl 1.3 M Haloferax mediterranei
NaCl 1.3 M Haloferax mediterranei

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Haloferax mediterranei

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32500
-
 2 * 32500, SDS-PAGE Haloferax mediterranei
64200 68200 gel filtration, PAGE, diffusion and sedimentation equilibrium Haloferax mediterranei

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate + 2-oxoglutarate Haloferax mediterranei
-
 oxaloacetate + L-glutamate
-
 ?
L-aspartate + 2-oxoglutarate Haloferax mediterranei R-4 / ATCC 33500
-
 oxaloacetate + L-glutamate
-
 ?

Organism

Organism UniProt Comment Textmining
Haloferax mediterranei
-
-
-
Haloferax mediterranei R-4 / ATCC 33500
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Haloferax mediterranei

Renatured (Commentary)

Renatured (Comment) Organism
thermal denaturation is not reversible Haloferax mediterranei

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.53
-
 purified enzyme Haloferax mediterranei

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate + 2-oxoglutarate
-
 Haloferax mediterranei oxaloacetate + L-glutamate
-
 ?
L-aspartate + 2-oxoglutarate
-
 Haloferax mediterranei R-4 / ATCC 33500 oxaloacetate + L-glutamate
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 32500, SDS-PAGE Haloferax mediterranei

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
 3.5 M KCl Haloferax mediterranei

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 thermal denaturation is not reversible, denaturation temperature of holoenzyme is 78.5°C Haloferax mediterranei
78.5
-
 denaturation Haloferax mediterranei

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6 7.9
-
 Haloferax mediterranei

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate 2 mol of pyridoxal phosphate per mol of enzyme Haloferax mediterranei
pyridoxal 5'-phosphate a pyridoxal 5'-phosphate protein Haloferax mediterranei