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Literature summary extracted from

  • Shyur, L.F.; Aleshin, A.E.; Honzatko, R.B.; Fromm, H.J.
    Biochemical properties of mutant and wild-type fructose-1,6-bisphosphatases are consistent with the coupling of intra- and intersubunit conformational changes in the T- and R-state transition (1996), J. Biol. Chem., 271, 33301-33307.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.11 G191A decreased Km-value for fructose 1,6-diphosphate, decreased inhibition constant for fructose 1,6-diphosphate and decreased Mg2+ affinity compared to the wild type enzyme. The 50% inhibiting concentration of AMP is increased over 2000fold relative to the wild type enzyme, loss of AMP cooperativity, mechanism of AMP inhibition changes from competitive to noncompetitive Sus scrofa
3.1.3.11 I190T decreased Km-value for fructose 1,6-diphosphate, decreased inhibition constant for fructose 1,6-diphosphate decreased Mg2+ affinity compared to the wild type enzyme. The 50% inhibiting concentration of AMP is increased over 2000fold relative to the wild type enzyme, loss of AMP cooperativity, mechanism of AMP inhibition changes from competitive to noncompetitive Sus scrofa
3.1.3.11 K42E decreased Km-value for fructose 1,6-diphosphate, decreased inhibition constant for fructose 1,6-diphosphate and decreased Mg2+ affinity compared to the wild type enzyme. The 50% inhibiting concentration of AMP is increased over 2000fold relative to the wild type enzyme, loss of AMP cooperativity Sus scrofa
3.1.3.11 K42T decreased Km-value for fructose 1,6-diphosphate, decreased inhibition constant for fructose 1,6-diphosphate decreased Mg2+ affinity compared to the wild type enzyme. The 50% inhibiting concentration of AMP is increased over 2000fold relative to the wild type enzyme, loss of AMP cooperativity, mechanism of AMP inhibition changes from competitive to noncompetitive Sus scrofa
3.1.3.11 Q32L decreased Km-value for fructose 1,6-diphosphate and decreased inhibition constant for fructose 1,6-diphosphate compared to the wild type enzyme. 1.7fold increase in turnover number, 8fold increase in Mg2+ affinity. 8fold increase in 50% inhibiting concentration of AMP Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.11 0.00084
-
 fructose 1,6-diphosphate mutant enzyme G191A Sus scrofa
3.1.3.11 0.00142
-
 fructose 1,6-diphosphate mutant enzyme Q32L Sus scrofa
3.1.3.11 0.00153
-
 fructose 1,6-diphosphate mutant enzyme K42T Sus scrofa
3.1.3.11 0.00167
-
 fructose 1,6-diphosphate mutant enzyme K42E Sus scrofa
3.1.3.11 0.00181
-
 fructose 1,6-diphosphate mutant enzyme I190T Sus scrofa
3.1.3.11 0.00351
-
 fructose 1,6-diphosphate wild type enzyme Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.11 Sus scrofa P00636
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.11 wild type and mutant enzymes Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.11 D-fructose 1,6-diphosphate + H2O
-
 Sus scrofa D-fructose 6-phosphate + phosphate
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.3.11 2.3
-
 fructose 1,6-diphosphate mutant enzyme G191A Sus scrofa
3.1.3.11 18
-
 fructose 1,6-diphosphate wild type enzyme Sus scrofa
3.1.3.11 18.3
-
 fructose 1,6-diphosphate mutant enzyme K42T Sus scrofa
3.1.3.11 19.3
-
 fructose 1,6-diphosphate mutant enzyme K42E Sus scrofa
3.1.3.11 21.1
-
 fructose 1,6-diphosphate mutant enzyme I190T Sus scrofa
3.1.3.11 32.1
-
 fructose 1,6-diphosphate mutant enzyme Q32L Sus scrofa