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Literature summary extracted from

  • Hua, S.S.T.; Lichens, G.M.; Guirao, A.; Tsai, V.Y.
    Biochemical properties of glutamate synthase of salt-tolerant Bradyrhizobium sp. Strain WR1001 (1986), FEMS Microbiol. Lett., 37, 209-213.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.1.13 D-glutamate no inhibition: 50-200 mM Bradyrhizobium sp.
1.4.1.13 L-glutamate 30% inhibition at 500 mM Bradyrhizobium sp.

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.13 Bradyrhizobium sp.
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.4.1.13 additional information
-
-
 Bradyrhizobium sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+ ammonia does not replace L-glutamine as amino donor Bradyrhizobium sp. L-glutamate + NADP+
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.4.1.13
-
-
 stable for 6-8 h in crude extract Bradyrhizobium sp.
1.4.1.13 40
-
 10 min, 80% loss of activity, enzyme in crude extract Bradyrhizobium sp.
1.4.1.13 45
-
 3 min, 80% loss of activity, enzyme in crude extract Bradyrhizobium sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.1.13 8.3
-
-
 Bradyrhizobium sp.

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.4.1.13 7.4 9.1 at pH 7.4 and 9.1 about 50% of activity maximum Bradyrhizobium sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.13 NADPH
-
 Bradyrhizobium sp.