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Literature summary for 3.1.3.11 extracted from

  • Kelley-Loughnane, N.; Kantrowitz, E.R.
    Binding of AMP to two of the four subunits of pig kidney fructose-1,6-bisphosphatase induces the allosteric transition (2001), Proteins Struct. Funct. Genet., 44, 255-261.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
AMP study of allosteric inhibition, two classes of binding sites with two distinct affinities for AMP are possible Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information comparison of KM of wild-type and hybrid enzymes Sus scrofa

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information construction of hybrids in which subunits have either their active or regulatory sited rendered non-functional by specific mutations Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 1,6-bisphosphate + H2O
-
Sus scrofa D-fructose 6-phosphate + phosphate
-
?
D-fructose 1,6-bisphosphate + H2O enzyme is usually regarded as a regulatory enzyme of gluconeogenesis Sus scrofa D-fructose 6-phosphate + phosphate
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information comparison of kcat of wild-type and hybrid enzymes Sus scrofa