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Literature summary for 1.4.1.13 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

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

Organism

Organism UniProt Comment Textmining
Bradyrhizobium sp.
-
-
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Temperature Stability [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.3
-
-
Bradyrhizobium sp.

pH Range

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

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Bradyrhizobium sp.