Literature summary for 3.5.99.6 extracted from

Zonszein, S.; Alvarez-Anorve, L.I.; Vazquez-Nunez, R.J.; Calcagno, M.L.
The tertiary origin of the allosteric activation of E. coli glucosamine-6-phosphate deaminase studied by sol-gel nanoencapsulation of its T conformer (2014), PLoS ONE, 9, e96536.

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Protein Variants

Protein Variants	Comment	Organism
C118Ser/C228S/C239S/D165C/S206W	the mutant shows reduced turnover number compared to the wild type enzyme	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
alpha-D-glucosamine 6-phosphate + H2O	Escherichia coli	-	D-fructose 6-phosphate + NH3	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A759	-	-

Purification (Commentary)

Purification (Comment)	Organism
N-6-aminohexanoyl-glucosamine 6-phosphate agarose column chromatography	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
alpha-D-glucosamine 6-phosphate + H2O	-	Escherichia coli	D-fructose 6-phosphate + NH3	-	?

Synonyms

Synonyms	Comment	Organism
GNPDA	-	Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
107	-	alpha-D-glucosamine 6-phosphate	mutant C118Ser/C228S/C239S/D165C/S206W, at pH 7.8 and 30°C	Escherichia coli
158	-	alpha-D-glucosamine 6-phosphate	wild type enzyme, at pH 7.8 and 30°C	Escherichia coli

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Release 2023.1 (January 2023)