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Literature summary for 2.7.1.106 extracted from

  • Rose, I.A.; Warms, J.V.B.; Wong, L.J.
    Inhibitors of glucose-1,6-bisphosphate synthase (1977), J. Biol. Chem., 252, 4262-4268.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
cis/trans-aconitate
-
Bos taurus
citrate
-
Bos taurus
D-fructose 1,6-diphosphate
-
Bos taurus
D-glucose 1,6-diphosphate
-
Bos taurus
Glutarate weak Bos taurus
glycerate 2,3-diphosphate
-
Bos taurus
Glycerate 3-phosphate
-
Bos taurus
isocitrate
-
Bos taurus
K+ weak Bos taurus
L-malate weak Bos taurus
Li+ strong, dilution, Co2+ or Zn2+ protects, not Ca2+, Mg2+ or Mn2+ Bos taurus
additional information no inhibition by adipate or succinate Bos taurus
Na+ weak Bos taurus
phosphate
-
Bos taurus
phosphoenolpyruvate strong Bos taurus
tricarballylate
-
Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000087
-
3-phospho-D-glyceroyl 1-phosphate 23°C, pH 8, Mg2+-enzyme in brain Bos taurus
0.000091
-
3-phospho-D-glyceroyl 1-phosphate 23°C, pH 8, Zn2+-enzyme in brain Bos taurus
0.09
-
D-glucose 1-phosphate 23°C, pH 8, Mg2+- and Zn2+-enzyme in brain Bos taurus

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ tightly bound, can replace Zn2+ Bos taurus
Mg2+ no activation of enzyme in Zn-form Bos taurus
Mg2+ activation, easily dissociates from enzyme protein Bos taurus
Mg2+ Km-value: 1 mM Bos taurus
Zn2+ Zn-form of the enzyme: tightly bound, about 65% of brain enzyme in Zn-form Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-phospho-D-glyceroyl phosphate + D-glucose 1-phosphate
-
Bos taurus 3-phospho-D-glycerate + D-glucose 1,6-bisphosphate
-
r

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Bos taurus