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Literature summary 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.
    View publication on PubMedView publication on EuropePMC

Protein Variants

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
3.5.99.6 Escherichia coli P0A759
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
3.5.99.6 GNPDA
-
 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.99.6 107
-
 alpha-D-glucosamine 6-phosphate mutant C118Ser/C228S/C239S/D165C/S206W, at pH 7.8 and 30°C Escherichia coli
3.5.99.6 158
-
 alpha-D-glucosamine 6-phosphate wild type enzyme, at pH 7.8 and 30°C Escherichia coli