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Literature summary extracted from

  • Midelfort, C.F.; Rose, I.A.
    Studies on the mechanism of Escherichia coli glucosamine-6-phosphate isomerase (1977), Biochemistry, 16, 1590-1596.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.99.6 2-deoxy-2-amino-D-glucitol 6-phosphate
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.99.6 0.4
-
 D-glucosamine 6-phosphate pH 7.8, 25°C Escherichia coli

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.99.6
-
 Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
3.5.99.6 alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3 reaction mechanism involves a ring-opening step, followed by an enolization step that proceeds through a cis-enolamine and its tautomeric imine as reaction intermediates Escherichia coli
a

Storage Stability

EC Number Storage Stability Organism
3.5.99.6 0-5°C, in liquid N2, little loss of activity after 2-5 months Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.99.6 D-glucosamine 6-phosphate + H2O active towards alpha-anomer, inactive towards the beta-anomer. Strong affinity for the open-chain form of glucosamine 6-phosphate Escherichia coli D-fructose 6-phosphate + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.99.6 ? x * 28000-30000, SDS-PAGE Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.5.99.6 0.002
-
 2-deoxy-2-amino-D-glucitol 6-phosphate pH 7.8, 25°C, substrate : D-glucosamine-6-phosphate Escherichia coli