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Literature summary 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

General Stability

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.6.1.1 KCl 1.3 M Haloferax mediterranei
2.6.1.1 NaCl 1.3 M Haloferax mediterranei

KM Value [mM]

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.6.1.1 32500
-
 2 * 32500, SDS-PAGE Haloferax mediterranei
2.6.1.1 64200 68200 gel filtration, PAGE, diffusion and sedimentation equilibrium Haloferax mediterranei

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.1
-
 Haloferax mediterranei

Renatured (Commentary)

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.6.1.1 1.53
-
 purified enzyme Haloferax mediterranei

Substrates and Products (Substrate)

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

Subunits

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.6.1.1 65
-
 3.5 M KCl Haloferax mediterranei

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.6.1.1 additional information
-
 thermal denaturation is not reversible, denaturation temperature of holoenzyme is 78.5°C Haloferax mediterranei
2.6.1.1 78.5
-
 denaturation Haloferax mediterranei

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.6.1.1 7.6 7.9
-
 Haloferax mediterranei

Cofactor

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