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Literature summary extracted from

  • Choe, J.Y.; Fromm, H.J.; Honzatko, R.B.
    Crystal structures of fructose 1,6-bisphosphatase: mechanism of catalysis and allosteric inhibition revealed in product complexes (2000), Biochemistry, 39, 8565-8574.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.11 expression in Escherichia coli Sus scrofa

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.3.11 In presence of AMP, the enzyme crystallizes in the T-state and AMP displaces loop 52-72 from its engaged conformation and abolishes metal association with sites 2 and 3. In the absence of AMP, enzyme is in the R-state and loop 52-72 associates with the active site. Three metal-binding sites are occupied by Zn2+ and two of three metal sites by Mg2+. Sus scrofa

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.11 AMP allosteric inhibitor Sus scrofa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.11 Mg2+ required Sus scrofa
3.1.3.11 Zn2+
-
 Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.3.11 D-fructose 1,6-diphosphate + H2O Sus scrofa enzyme is usually regarded as a regulatory enzyme of gluconeogenesis D-fructose 6-phosphate + phosphate
-
 ?

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 the recombinant enzyme 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
-
 ?
3.1.3.11 D-fructose 1,6-diphosphate + H2O enzyme is usually regarded as a regulatory enzyme of gluconeogenesis Sus scrofa D-fructose 6-phosphate + phosphate
-
 ?