Literature summary for 1.4.1.13 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.

Search for more literature for 1.4.1.13

Application

Application	Comment	Organism
molecular biology	GltA shows 73% identity to the corresponding protein of Oceanobacillus iheyensis	Halobacillus halophilus
molecular biology	GltB1 shows 74% identity to the corresponding protein of Oceanobacillus iheyensis	Halobacillus halophilus
molecular biology	GltB2 shows 73% identity to the glutamate synthase of Geobacillus kaustophilus	Halobacillus halophilus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
additional information	expression is not salt dependent, nor is the corresponding enzymatic activity detectable in cell extracts of cells grown at different salinities	Halobacillus halophilus

Organism

Organism	UniProt	Comment	Textmining
Halobacillus halophilus	Q0E5H3	strain DSMZ 2266T	-
Halobacillus halophilus	Q0E5H4	strain DSMZ 2266T	-
Halobacillus halophilus	Q0E5H5	strain DSMZ 2266T	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	glutamate synthase activity in cell extracts rarely detectable	Halobacillus halophilus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-glutamine + 2-oxoglutarate + NADPH	-	Halobacillus halophilus	L-glutamate + NADP+	-	?

Synonyms

Synonyms	Comment	Organism
gltA	-	Halobacillus halophilus
GltB1	-	Halobacillus halophilus
GltB2	-	Halobacillus halophilus

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	-	Halobacillus halophilus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)