BRENDA - Enzyme Database show

Ferredoxin-dependent glutamate synthase: involvement in ammonium assimilation in Haloferax mediterranei

Pire, C.; Martínez-Espinosa, R.M.; Perez-Pomares, F.; Esclapez, J.; Bonete, M.J.; Extremophiles 18, 147-159 (2013)

Data extracted from this reference:

KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.4.7.1
0.018
-
reduced ferredoxin
pH 7.5, 40°C, 3 M NaCl
Haloferax mediterranei
1.4.7.1
2.1
-
L-glutamine
pH 7.5, 40°C, 3 M NaCl
Haloferax mediterranei
1.4.7.1
31
-
2-oxoglutarate
pH 7.5, 40°C, 3 M NaCl
Haloferax mediterranei
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
1.4.7.1
NaCl
maximal activity at salt concentrations from 3 to 4 M NaCl
Haloferax mediterranei
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.4.7.1
163780
-
1 * 163780, calculated from sequence
Haloferax mediterranei
1.4.7.1
198000
-
gel filtration
Haloferax mediterranei
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.4.7.1
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+
-
-
?
1.4.7.1
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
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.4.7.1
Haloferax mediterranei
C0MP41
-
-
1.4.7.1
Haloferax mediterranei ATCC 33500
C0MP41
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.4.7.1
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
727444
Haloferax mediterranei
L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
-
-
-
?
1.4.7.1
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
727444
Haloferax mediterranei ATCC 33500
L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
-
-
-
?
1.4.7.1
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
727444
Haloferax mediterranei
2 L-glutamate + 2 oxidized ferredoxin
-
-
-
?
1.4.7.1
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
727444
Haloferax mediterranei ATCC 33500
2 L-glutamate + 2 oxidized ferredoxin
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
1.4.7.1
monomer
1 * 163780, calculated from sequence
Haloferax mediterranei
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.4.7.1
50
-
-
Haloferax mediterranei
Temperature Range [°C]
EC Number
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
1.4.7.1
30
80
30°C: about 75% of maximal activity, 80°C: about 55% of maximal activity
Haloferax mediterranei
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.4.7.1
7.5
-
-
Haloferax mediterranei
pH Range
EC Number
pH Minimum
pH Maximum
Commentary
Organism
1.4.7.1
5
10
pH 5.0: about 45% of maximal activity, pH 10.0: about 55% of maximal activity
Haloferax mediterranei
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.4.7.1
0.018
-
reduced ferredoxin
pH 7.5, 40°C, 3 M NaCl
Haloferax mediterranei
1.4.7.1
2.1
-
L-glutamine
pH 7.5, 40°C, 3 M NaCl
Haloferax mediterranei
1.4.7.1
31
-
2-oxoglutarate
pH 7.5, 40°C, 3 M NaCl
Haloferax mediterranei
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
1.4.7.1
NaCl
maximal activity at salt concentrations from 3 to 4 M NaCl
Haloferax mediterranei
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.4.7.1
163780
-
1 * 163780, calculated from sequence
Haloferax mediterranei
1.4.7.1
198000
-
gel filtration
Haloferax mediterranei
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.4.7.1
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+
-
-
?
1.4.7.1
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+
-
-
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.4.7.1
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
727444
Haloferax mediterranei
L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
-
-
-
?
1.4.7.1
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
727444
Haloferax mediterranei ATCC 33500
L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
-
-
-
?
1.4.7.1
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
727444
Haloferax mediterranei
2 L-glutamate + 2 oxidized ferredoxin
-
-
-
?
1.4.7.1
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
727444
Haloferax mediterranei ATCC 33500
2 L-glutamate + 2 oxidized ferredoxin
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.4.7.1
monomer
1 * 163780, calculated from sequence
Haloferax mediterranei
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.4.7.1
50
-
-
Haloferax mediterranei
Temperature Range [°C] (protein specific)
EC Number
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
1.4.7.1
30
80
30°C: about 75% of maximal activity, 80°C: about 55% of maximal activity
Haloferax mediterranei
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.4.7.1
7.5
-
-
Haloferax mediterranei
pH Range (protein specific)
EC Number
pH Minimum
pH Maximum
Commentary
Organism
1.4.7.1
5
10
pH 5.0: about 45% of maximal activity, pH 10.0: about 55% of maximal activity
Haloferax mediterranei
Expression
EC Number
Organism
Commentary
Expression
1.4.7.1
Haloferax mediterranei
expression is induced under conditions of ammonium restriction
up
Expression (protein specific)
EC Number
Organism
Commentary
Expression
1.4.7.1
Haloferax mediterranei
expression is induced under conditions of ammonium restriction
up