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Literature summary extracted from

  • Brestic, M.; Zivcak, M.; Olsovska, K.; Shao, H.B.; Kalaji, H.M.; Allakhverdiev, S.I.
    Reduced glutamine synthetase activity plays a role in control of photosynthetic responses to high light in barley leaves (2014), Plant Physiol. Biochem., 81, 74-83 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
6.3.1.2 additional information determination and photosynthetic responses of GS2 mutant of barley with reduced activity of chloroplastic glutamine synthetase, overview. The mutation of the enzyme not directly associated with conversion of light energy leads to significant modifications of structure and function of photosystems Hordeum vulgare

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
6.3.1.2 chloroplast
-
 Hordeum vulgare 9507
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.1.2 Mg2+ required Hordeum vulgare

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.1.2 ATP + L-glutamate + NH3 Hordeum vulgare
-
 ADP + phosphate + L-glutamine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.1.2 Hordeum vulgare
-
 cv. Kompakt
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.3.1.2 leaf
-
 Hordeum vulgare
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.1.2 ATP + L-glutamate + NH3
-
 Hordeum vulgare ADP + phosphate + L-glutamine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.3.1.2 GS2
-
 Hordeum vulgare

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.1.2 ATP
-
 Hordeum vulgare

General Information

EC Number General Information Comment Organism
6.3.1.2 physiological function the rate-limiting step in photorespiration is the reassimilation of ammonia catalyzed by chloroplastic glutamine synthetase isozyme 2 (GS2). In plants, GS2 together with ferredoxin-dependent glutamate synthase (Fd-GOGAT) plays a major role in re-assimilation of ammonium liberated in mitochondria by the glycine decarboxylase, in the pathway known as glutamine synthetase/glutamate synthase (GS/GOGAT) cycle in chloroplasts. The product of this cycle, glutamate, is required for one of the peroxisomal transamination reactions Hordeum vulgare