EC Number |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
---|
1.4.1.13 | 391443 |
The enzymes of the ammonia assimilation in Pseudomonas aeruginosa |
Arch. Microbiol. |
124 |
197-203 |
1980 |
Pseudomonas aeruginosa |
6102851 |
1.4.1.13 | 391465 |
The recombinant alpha subunit of glutamate synthase: spectroscopic and catalytic properties |
Biochemistry |
37 |
1828-1838 |
1998 |
Azospirillum brasilense |
9485308 |
1.4.1.13 | 687801 |
The subnanometer resolution structure of the glutamate synthase 1.2-MDa hexamer by cryoelectron microscopy and its oligomerization behavior in solution: functional implications |
J. Biol. Chem. |
283 |
8237-8249 |
2008 |
Azospirillum brasilense |
18199747 |
1.4.1.13 | 654382 |
The unexpected structural role of glutamate synthase [4Fe-4S](+1,+2) clusters as demonstrated by site-directed mutagenesis of conserved C residues at the N-terminus of the enzyme beta subunit |
Arch. Biochem. Biophys. |
436 |
355-366 |
2005 |
Azospirillum brasilense |
15797248 |
1.4.1.13 | 725401 |
Two atypical L-cysteine-regulated NADPH-dependent oxidoreductases involved in redox maintenance, L-cystine and iron reduction, and metronidazole activation in the enteric protozoan Entamoeba histolytica |
J. Biol. Chem. |
285 |
26889-26899 |
2010 |
Entamoeba histolytica |
20592025 |
1.4.1.13 | 725401 |
Two atypical L-cysteine-regulated NADPH-dependent oxidoreductases involved in redox maintenance, L-cystine and iron reduction, and metronidazole activation in the enteric protozoan Entamoeba histolytica |
J. Biol. Chem. |
285 |
26889-26899 |
2010 |
Entamoeba histolytica HM1:IMSS cl 6 |
20592025 |