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Literature summary for 1.4.1.14 extracted from

  • Hossain, M.; Uddin, M.; Ismail, M.; Ashrafuzzaman, M.
    Responses of glutamine synthetase-glutamate synthase cycle enzymes in tomato leaves under salinity stress (2012), Int. J. Agric. Biol., 14, 509-515.
No PubMed abstract available

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 L-glutamate + NAD+ Solanum lycopersicum
-
L-glutamine + 2-oxoglutarate + NADH + H+
-
r
2 L-glutamate + NAD+ Solanum lycopersicum BINATomato-5
-
L-glutamine + 2-oxoglutarate + NADH + H+
-
r

Organism

Organism UniProt Comment Textmining
Solanum lycopersicum
-
-
-
Solanum lycopersicum BINATomato-5
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Solanum lycopersicum
-
seedling
-
Solanum lycopersicum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 L-glutamate + NAD+
-
Solanum lycopersicum L-glutamine + 2-oxoglutarate + NADH + H+
-
r
2 L-glutamate + NAD+
-
Solanum lycopersicum BINATomato-5 L-glutamine + 2-oxoglutarate + NADH + H+
-
r

Synonyms

Synonyms Comment Organism
GOGAT
-
Solanum lycopersicum
NADH-dependent glutamate synthase
-
Solanum lycopersicum
NADH-GOGAT
-
Solanum lycopersicum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Solanum lycopersicum

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Solanum lycopersicum
NADH
-
Solanum lycopersicum

General Information

General Information Comment Organism
physiological function the glutamine synthetase-glutamate synthase cycle plays an important role for proline synthesis in tomato leaves during salinity stress, while NADH-dependent glutamate synthase (NADHGOGAT) activity is unchanged due to salinity stress Solanum lycopersicum