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Literature summary for 1.4.7.1 extracted from

  • Pire, C.; Martínez-Espinosa, R.M.; Perez-Pomares, F.; Esclapez, J.; Bonete, M.J.
    Ferredoxin-dependent glutamate synthase: involvement in ammonium assimilation in Haloferax mediterranei (2013), Extremophiles, 18, 147-159.
    View publication on PubMed
Search for more literature for 1.4.7.1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.018
-
 reduced ferredoxin pH 7.5, 40°C, 3 M NaCl Haloferax mediterranei
2.1
-
 L-glutamine pH 7.5, 40°C, 3 M NaCl Haloferax mediterranei
31
-
 2-oxoglutarate pH 7.5, 40°C, 3 M NaCl Haloferax mediterranei

Metals/Ions

Metals/Ions Comment Organism Structure
NaCl maximal activity at salt concentrations from 3 to 4 M NaCl Haloferax mediterranei

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
163780
-
 1 * 163780, calculated from sequence Haloferax mediterranei
198000
-
 gel filtration Haloferax mediterranei

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 L-glutamate + 2 oxidized ferredoxin Haloferax mediterranei overall reaction. The enzyme is involved in the ammonium assimilation pathway which enables Haloferax mediterranei to thrive in media with low ammonium concentration or containing just nitrate as single nitrogen source L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
-
 ?
2 L-glutamate + 2 oxidized ferredoxin Haloferax mediterranei ATCC 33500 overall reaction. The enzyme is involved in the ammonium assimilation pathway which enables Haloferax mediterranei to thrive in media with low ammonium concentration or containing just nitrate as single nitrogen source L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
-
 ?

Organism

Organism UniProt Comment Textmining
Haloferax mediterranei C0MP41
-
-
Haloferax mediterranei ATCC 33500 C0MP41
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 L-glutamate + 2 oxidized ferredoxin overall reaction. The enzyme is involved in the ammonium assimilation pathway which enables Haloferax mediterranei to thrive in media with low ammonium concentration or containing just nitrate as single nitrogen source Haloferax mediterranei L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
-
 ?
2 L-glutamate + 2 oxidized ferredoxin overall reaction. The enzyme is involved in the ammonium assimilation pathway which enables Haloferax mediterranei to thrive in media with low ammonium concentration or containing just nitrate as single nitrogen source Haloferax mediterranei ATCC 33500 L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
-
 ?
L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+ no activity is detected in presence of either 5 mM NADH or 0.5 mM NADPH. Methyl viologen at 20 mM and 0.004 mM ferredoxin I are also tested under the same conditions: activity with 0.004 mM ferredoxin I as reducing agent is approximately 3fold higher than that measured with 20 mM methyl viologen. For the other ferrodoxin isoform found in Haloferax mediterranei, ferrodoxin II, the activity is approximately 8fold lower than that for ferredoxin I Haloferax mediterranei 2 L-glutamate + 2 oxidized ferredoxin
-
 ?
L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+ no activity is detected in presence of either 5 mM NADH or 0.5 mM NADPH. Methyl viologen at 20 mM and 0.004 mM ferredoxin I are also tested under the same conditions: activity with 0.004 mM ferredoxin I as reducing agent is approximately 3fold higher than that measured with 20 mM methyl viologen. For the other ferrodoxin isoform found in Haloferax mediterranei, ferrodoxin II, the activity is approximately 8fold lower than that for ferredoxin I Haloferax mediterranei ATCC 33500 2 L-glutamate + 2 oxidized ferredoxin
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 163780, calculated from sequence Haloferax mediterranei

Synonyms

Synonyms Comment Organism
ferredoxin-dependent glutamate synthase
-
 Haloferax mediterranei
GltS
-
 Haloferax mediterranei
GOGAT
-
 Haloferax mediterranei

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
 Haloferax mediterranei

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 80 30°C: about 75% of maximal activity, 80°C: about 55% of maximal activity Haloferax mediterranei

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Haloferax mediterranei

pH Range

pH Minimum pH Maximum Comment Organism
5 10 pH 5.0: about 45% of maximal activity, pH 10.0: about 55% of maximal activity Haloferax mediterranei

Expression

Organism Comment Expression
Haloferax mediterranei expression is induced under conditions of ammonium restriction up