title: pHmetrical determination of the glucosamine-6-phosphate isomerase deaminase reverse reaction.
abstract: In the reverse direction, the reaction catalyzed by glucosamine 6-phosphate isomerase deaminase consumes ammonia and forms GlcN6P. As a consequence of the formation of a product with a lower pK than the substrates, a measurable pH drop in the reaction medium is produced. This property can be used to follow potentiometrically the course of the reaction. This property can be used to follow potentiometrically the course of the reaction. The usefulness of the method is demonstrated obtaining the inhibition pattern by GlcN6P when Fru6P is the varied substrate.
authors.forename: G
authors.initials: G
authors.lastname: Mulliert
authors.forename: R
authors.initials: R
authors.lastname: Lara-Lemus
authors.forename: M
authors.initials: M
authors.lastname: Calcagno
mesh_terms: D004926:Escherichia coli / Q000201:enzymology; D005636:Fructosephosphates / Q000494:pharmacology; D005945:Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D000637:Transaminases / Q000378:metabolism*
chemical_list: D005636:Fructosephosphates; C027618:fructose-6-phosphate; D000637:Transaminases; D005945:Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)