Literature summary for 6.3.1.2 extracted from

Saum, S.H.; Sydow, J.F.; Palm, P.; Pfeiffer, F.; Oesterhelt, D.; Mueller, V.
Biochemical and molecular characterization of the biosynthesis of glutamine and glutamate, two major compatible solutes in the moderately halophilic bacterium Halobacillus halophilus (2006), J. Bacteriol., 188, 6808-6815.

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Inhibitors

Inhibitors	Comment	Organism	Structure
NaNO3	the specific activity of glutamine synthetase is reduced 66% in the presence of NaNO3	Halobacillus halophilus
sodium gluconate	the specific activity of glutamine synthetase is reduced 34% in the presence of sodium gluconate	Halobacillus halophilus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cl-	chloride stimulates the production of active enzyme by about 300%, in the absence of chloride in the assay buffer, glutamine synthetase activity is decreased by as much as 90%	Halobacillus halophilus
Cl-	Cl- dependence of glutamine synthetase activity	Halobacillus halophilus
Na+	3 mM, highest activity	Halobacillus halophilus

Organism

Organism	UniProt	Comment	Textmining
Halobacillus halophilus	Q0E5H8	strain DSMZ 2266T	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
1.53	-	in the presence of 3 mM NaCl	Halobacillus halophilus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-Glu + NH4+	-	Halobacillus halophilus	ADP + phosphate + L-Gln	-	?

Synonyms

Synonyms	Comment	Organism
GlnA2	-	Halobacillus halophilus
Glutamine synthetase	-	Halobacillus halophilus

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Release 2023.1 (January 2023)