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Information on EC 1.4.7.1 - glutamate synthase (ferredoxin)
for references in articles please use BRENDA:EC1.4.7.1
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EC Tree 1 Oxidoreductases
1.4 Acting on the CH-NH2 group of donors
1.4.7 With an iron-sulfur protein as acceptor
1.4.7.1 glutamate synthase (ferredoxin)
IUBMB Comments
Binds a [3Fe-4S] cluster as well as FAD and FMN. The protein is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate. The NH3 is channeled through a 24 Å channel in the active protein. No hydrolysis of glutamine takes place without ferredoxin and 2-oxoglutarate being bound to the protein [5,6].
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
showSynonyms
fd-gogat, ferredoxin-dependent glutamate synthase, fd-dependent glutamate synthase, ferredoxin-glutamate synthase, ferredoxin-gogat, ferredoxin-dependent gogat, fd-gogat1, ferredoxin-dependent glts, fdgogat, ferredoxin-dependent glutamate synthase1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
abc1
Fd-GOGAT
Fd-GOGAT1
ferredoxin-dependent glutamate synthase
ferredoxin-dependent glutamate synthase1
ferredoxin-dependent GOGAT
ferredoxin-glutamate synthase
GltS
Glu1
glutamate synthase (ferredoxin-dependent)
-
-
-
-
glutamine:2-oxoglutarate amidotransferase
GOGAT
Fd-GOGAT
-
-
-
-
ferredoxin-dependent glutamate synthase
-
-
-
-
ferredoxin-dependent glutamate synthase
exhibits also glutaminase activity and does not react with a plant-type ferredoxin (Fd3) containing a [2Fe-2S] cluster, but does react with bacterial ferredoxins (Fd1 and Fd2) containing [4Fe-4S] clusters
ferredoxin-dependent glutamate synthase
Hydrogenobacter thermophilus TK-6 / IAM 12695
exhibits also glutaminase activity and does not react with a plant-type ferredoxin (Fd3) containing a [2Fe-2S] cluster, but does react with bacterial ferredoxins (Fd1 and Fd2) containing [4Fe-4S] clusters
-
ferredoxin-glutamate synthase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 L-glutamate + oxidized ferredoxin = L-glutamine + 2-oxoglutarate + reduced ferredoxin + 2 H+
L-glutamate + 2 oxidized ferredoxin + H2O = NH3 + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
1b
-
-
-
L-glutamate + NH3 = L-glutamine + H2O
1a
-
-
-
2 L-glutamate + oxidized ferredoxin = L-glutamine + 2-oxoglutarate + reduced ferredoxin + 2 H+
proposed electron-transfer pathway
-
2 L-glutamate + oxidized ferredoxin = L-glutamine + 2-oxoglutarate + reduced ferredoxin + 2 H+
overall reaction
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
transamination
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
ammonia assimilation cycle II, GABA shunt II, L-glutamate biosynthesis V, nitrogen remobilization from senescing leaves
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate:ferredoxin oxidoreductase (transaminating)
Binds a [3Fe-4S] cluster as well as FAD and FMN. The protein is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate. The NH3 is channeled through a 24 A channel in the active protein. No hydrolysis of glutamine takes place without ferredoxin and 2-oxoglutarate being bound to the protein [5,6].
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CAS REGISTRY NUMBER
COMMENTARY
62213-56-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 L-glutamate + 2 oxidized ferredoxin
L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
L-glutamate + oxidized iodonitrotetrazolium
2-oxoglutarate + NH3 + reduced iodonitrotetrazolium
-
Substrates: enzyme exhibits L-glutamate:iodonitrotetrazolium oxidoreductase activity at pH 7.5-9.5
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L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
2 L-glutamate + 2 oxidized ferredoxin
L-glutamine + 2-oxoglutarate + 2 reduced methyl viologen
2 L-glutamate + 2 oxidized methyl viologen
Substrates: reductant: Na2S2O4
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L-glutamine + 2-oxoglutarate + 2 reduced methyl viologen + 2 H+
2 L-glutamate + 2 oxidized methyl viologen
Substrates: -
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?
L-glutamine + 2-oxoglutarate + reduced bacterial ferredoxin 1
L-glutamate + oxidized bacterial ferredoxin 1
L-glutamine + 2-oxoglutarate + reduced bacterial ferredoxin 2
L-glutamate + oxidized bacterial ferredoxin 2
L-glutamine + 2-oxoglutarate + reduced ferredoxin + NADPH + H+
L-glutamate + oxidized ferredoxin + NADP+
-
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced iodonitrotetrazolium + H+
L-glutamate + oxidized iodonitrotetrazolium
-
Substrates: -
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r
L-glutamine + 2-oxoglutarate + reduced methyl viologen + H+
L-glutamate + oxidized methyl viologen
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
2 L-glutamate + 2 oxidized ferredoxin
L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
Substrates: -
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?
2 L-glutamate + 2 oxidized ferredoxin
L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
Substrates: 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
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2 L-glutamate + 2 oxidized ferredoxin
L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
Substrates: 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
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2 L-glutamate + 2 oxidized ferredoxin
L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
Substrates: -
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?
L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
2 L-glutamate + 2 oxidized ferredoxin
Substrates: 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
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L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
2 L-glutamate + 2 oxidized ferredoxin
Substrates: 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
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L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
2 L-glutamate + 2 oxidized ferredoxin
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced bacterial ferredoxin 1
L-glutamate + oxidized bacterial ferredoxin 1
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced bacterial ferredoxin 1
L-glutamate + oxidized bacterial ferredoxin 1
Hydrogenobacter thermophilus TK-6 / IAM 12695
Substrates: -
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?
L-glutamine + 2-oxoglutarate + reduced bacterial ferredoxin 2
L-glutamate + oxidized bacterial ferredoxin 2
Substrates: -
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?
L-glutamine + 2-oxoglutarate + reduced bacterial ferredoxin 2
L-glutamate + oxidized bacterial ferredoxin 2
Hydrogenobacter thermophilus TK-6 / IAM 12695
Substrates: -
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?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
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Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: -
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?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
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Substrates: highly specific for glutamine and 2-oxoglutarate
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: about 35% of activity with methylviologen
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
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Substrates: enzyme may be linked to light driven electron transport
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: -
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?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: -
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?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
Substrates: -
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?
L-glutamine + 2-oxoglutarate + reduced ferredoxin + H+
L-glutamate + oxidized ferredoxin
-
Substrates: -
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r
L-glutamine + 2-oxoglutarate + reduced ferredoxin + H+
L-glutamate + oxidized ferredoxin
-
Substrates: -
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r
L-glutamine + 2-oxoglutarate + reduced ferredoxin + H+
L-glutamate + oxidized ferredoxin
-
Substrates: -
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r
L-glutamine + 2-oxoglutarate + reduced ferredoxin + H+
L-glutamate + oxidized ferredoxin
-
Substrates: -
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r
L-glutamine + 2-oxoglutarate + reduced ferredoxin + H+
L-glutamate + oxidized ferredoxin
-
Substrates: -
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r
L-glutamine + 2-oxoglutarate + reduced ferredoxin + H+
L-glutamate + oxidized ferredoxin
-
Substrates: -
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?
L-glutamine + 2-oxoglutarate + reduced ferredoxin + H+
L-glutamate + oxidized ferredoxin
-
Substrates: -
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?
L-glutamine + 2-oxoglutarate + reduced ferredoxin + H+
L-glutamate + oxidized ferredoxin
-
Substrates: -
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r
L-glutamine + 2-oxoglutarate + reduced ferredoxin + H+
L-glutamate + oxidized ferredoxin
-
Substrates: -
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r
L-glutamine + 2-oxoglutarate + reduced ferredoxin + H+
L-glutamate + oxidized ferredoxin
-
Substrates: -
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r
L-glutamine + 2-oxoglutarate + reduced ferredoxin + H+
L-glutamate + oxidized ferredoxin
Substrates: -
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?
L-glutamine + 2-oxoglutarate + reduced methyl viologen + H+
L-glutamate + oxidized methyl viologen
Substrates: -
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?
L-glutamine + 2-oxoglutarate + reduced methyl viologen + H+
L-glutamate + oxidized methyl viologen
-
Substrates: -
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?
L-glutamine + 2-oxoglutarate + reduced methyl viologen + H+
L-glutamate + oxidized methyl viologen
Substrates: -
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?
L-glutamine + 2-oxoglutarate + reduced methyl viologen + H+
L-glutamate + oxidized methyl viologen
Substrates: -
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?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
-
Substrates: artificial elctron donor
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L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
-
Substrates: artificial elctron donor
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L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
-
Substrates: artificial elctron donor
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L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
-
Substrates: artificial elctron donor
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L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
-
Substrates: similar activity as with ferredoxin
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L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
Hydrogenobacter thermophilus TK-6 / IAM 12695
Substrates: -
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?
L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
-
Substrates: artificial elctron donor
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L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
-
Substrates: artificial elctron donor
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L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
-
Substrates: 60% of ferredoxin activity
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L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
-
Substrates: artificial elctron donor
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L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
-
Substrates: artificial elctron donor
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L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
-
Substrates: artificial elctron donor
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L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
-
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
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Substrates: only in the presence of ferredoxin
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L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
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Substrates: -
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L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
-
Substrates: significantly higher activity with ferredoxin than with methyl viologen
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L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
-
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced methylviologen
L-glutamate + oxidized methylviologen
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Substrates: artificial elctron donor
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?
additional information
?
-
-
Substrates: does not react with plant ferredoxin 3
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additional information
?
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Substrates: does not react with plant ferredoxin 3
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?
additional information
?
-
Hydrogenobacter thermophilus TK-6 / IAM 12695
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Substrates: does not react with plant ferredoxin 3
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?
additional information
?
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Hydrogenobacter thermophilus TK-6 / IAM 12695
Substrates: does not react with plant ferredoxin 3
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?
additional information
?
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Substrates: key enzyme of N-assimilation and biosynthesis of amino acids, decreases in leaves in response to salt stress
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additional information
?
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Substrates: the GS2/Fd-GOGAT cycle is the major pathway for ammonium assimilation in higher plants. Alternative metabolic pathways may be transiently activated during a day/night cycle in plants with low Fd-GOGAT activity
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additional information
?
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Substrates: enzyme provides amino acids for nitrogen translocation
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additional information
?
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Substrates: role of enzyme in supplying L-glutamate for the synthesis and transport of amino acids
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additional information
?
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Substrates: existence of the enzyme in the companion cells, which are adjacent to the sieve elements, of the central cylinder in rice roots is advantageous for the access and efficient utilization of glutamine and carbohydrate transported through the sieve elements under anaerobic conditions
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additional information
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Substrates: levels of Fd-GOGAT are coordinated by light, nitrate is necessary for the light regulation. Single or repeated red light pulses induce the activity of the enzymes and this effect is reverted by subsequent far-red light
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 L-glutamate + 2 oxidized ferredoxin
L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
L-glutamine + 2-oxoglutarate + reduced ferredoxin + NADPH + H+
L-glutamate + oxidized ferredoxin + NADP+
-
Substrates: -
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2 L-glutamate + 2 oxidized ferredoxin
L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
Substrates: -
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2 L-glutamate + 2 oxidized ferredoxin
L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
Substrates: 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
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2 L-glutamate + 2 oxidized ferredoxin
L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
Substrates: 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
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: -
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?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: -
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?
L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: highly specific for glutamine and 2-oxoglutarate
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
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Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
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Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
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Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
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Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
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Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
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Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
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Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
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Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: enzyme may be linked to light driven electron transport
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
-
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
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Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
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Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
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Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin
L-glutamate + oxidized ferredoxin
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Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin + H+
L-glutamate + oxidized ferredoxin
-
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin + H+
L-glutamate + oxidized ferredoxin
-
Substrates: -
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L-glutamine + 2-oxoglutarate + reduced ferredoxin + H+
L-glutamate + oxidized ferredoxin
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Substrates: key enzyme of N-assimilation and biosynthesis of amino acids, decreases in leaves in response to salt stress
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Substrates: the GS2/Fd-GOGAT cycle is the major pathway for ammonium assimilation in higher plants. Alternative metabolic pathways may be transiently activated during a day/night cycle in plants with low Fd-GOGAT activity
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Substrates: enzyme provides amino acids for nitrogen translocation
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Substrates: role of enzyme in supplying L-glutamate for the synthesis and transport of amino acids
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Substrates: existence of the enzyme in the companion cells, which are adjacent to the sieve elements, of the central cylinder in rice roots is advantageous for the access and efficient utilization of glutamine and carbohydrate transported through the sieve elements under anaerobic conditions
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Substrates: levels of Fd-GOGAT are coordinated by light, nitrate is necessary for the light regulation. Single or repeated red light pulses induce the activity of the enzymes and this effect is reverted by subsequent far-red light
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ferredoxin
-
enzyme forms an electrostatically stabilized complex with ferredoxin
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Ferredoxin
enzyme does not react with plant-type ferredoxin but with a bacterial-type ferredoxin containing [4Fe-4S] clusters
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Ferredoxin
1:2 molar ratio between the wild-type glutamate synthase and ferredoxin
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FMN
-
in contrast to earlier conclusions the enzyme contains 1 mol of FMN per mol enzyme but no FAD
FMN
the FMN-binding domain of FdGOGAT is essential for specific binding of the protein to UDP-sulfoquinovose synthase
FMN
purified Fd-GltS shows absorption peaks of FMN and [3Fe4S] cluster at 345, 417, 440 and 476 nm
[3Fe-4S]-center
purified Fd-GltS shows absorption peaks of FMN and [3Fe4S] cluster at 345, 417, 440 and 476 nm
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
NaCl
maximal activity at salt concentrations from 3 to 4 M NaCl
Iron
-
enzyme may contain two [2Fe-2S] clusters rather than a single [4Fe-4S] cluster
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cycloheximide
-
complete disappearance of enzyme in roots and 90% decrease in leaves after 24 h
iodoacetamide
-
90% inactivation after 15 h, L-glutamine protects from inactivation
N-ethylmaleimide
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15 mM, 93% inactivation after 15 h, L-glutamine protects from inactivation