Literature summary for 2.6.1.16 extracted from

Mouilleron, S.; Badet-Denisot, M.A.; Pecqueur, L.; Madiona, K.; Assrir, N.; Badet, B.; Golinelli-Pimpaneau, B.
Structural basis for morpheein-type allosteric regulation of Escherichia coli glucosamine-6-phosphate synthase: equilibrium between inactive hexamer and active dimer (2012), J. Biol. Chem., 287, 34533-34546.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
the crystal structure of the C1A mutant of Escherichia coli GlmS, solved at 2.5 A resolution, is organized as a hexamer, where the glutaminase domains adopt an inactive conformation	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
C1A	the structure of the inactive C1A mutant, crystallized in the presence of D-fructose 6-phosphate and Gln is deterimined. The C1A-GlmS structure is organized as a hexamer. The enzyme is regulated by a morpheein-type allosteric mechanism, in which functional dimeric GlmS is in equilibrium with the inactive hexamer	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P17169	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-glutamine + D-fructose 6-phosphate	-	Escherichia coli	L-glutamate + D-glucosamine 6-phosphate	-	?

Subunits

Subunits	Comment	Organism
dimer	the enzyme is regulated by a morpheein-type allosteric mechanism, in which functional dimeric GlmS is in equilibrium with the inactive hexamer	Escherichia coli
hexamer	the enzyme is regulated by a morpheein-type allosteric mechanism, in which functional dimeric GlmS is in equilibrium with the inactive hexamer	Escherichia coli

Synonyms

Synonyms	Comment	Organism
GlmS	-	Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.2	-	assay at	Escherichia coli

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Release 2023.1 (January 2023)