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Literature summary for 3.1.3.11 extracted from

  • Han, X.; Huang, Y.; Zhang, R.; Xiao, S.; Zhu, S.; Qin, N.; Hong, Z.; Wei, L.; Feng, J.; Ren, Y.; Feng, L.; Wan, J.
    New insight into the binding modes of TNP-AMP to human liver fructose-1,6-bisphosphatase (2016), Spectrochim. Acta A. Mol. Biomol. Spectrosc., 165, 155-160 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21 (DE3) Homo sapiens

Protein Variants

Protein Variants Comment Organism
K274L site-directed mutagenesis, active site mutant. The residue K274 is very important for AMP analogue TNP-AMP to bind to the active site of FBPase Homo sapiens
K274L equivalent activity to the wild-type enzyme. Wild-type and mutant FBPases behaved identically throughout expression and purification. When the residue K274 is mutated to L274, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate can not bind to the active site, but can bind to the allosteric site Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate able to bind not only to the AMP allosteric site but also to the fructose-1,6-bisphosphate active site Homo sapiens
AMP allosteric inhibition. The fluorescent AMP analogue, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate (TNP-AMP), is used as a fluorescent probe as it is able to competitively inhibit AMP binding to the AMP allosteric site Homo sapiens
fructose-2,6-bisphosphate
-
Homo sapiens
additional information the FBP active site works by stabilizing the FBPase, and the allosteric site impairs the activity of FBPase through its binding of a nonsubstrate molecule. Competitive inhibition of AMP, fructose 1,6-bisphosphate, or fructose 6-phosphate binding to FBPase with fluorescent AMP analogue, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate (TNP-AMP)-binding FBPase Homo sapiens
TNP-AMP a fluorescent AMP analogue, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate (TNP-AMP), is used as a fluorescent probe as it is able to competitively inhibit AMP binding to the AMP allosteric site. AMP and fructose 1,6-bisphosphate both can reduce the fluorescence from the bound TNP-AMP through competition for FBPase, suggesting that TNP-AMP binds not only to the AMP allosteric site but also to the FBP active site. The residue K274 is very important for TNP-AMP to bind to the active site of FBPase. When the residue K274 is mutated to L274, TNP-AMP cannot bind to the active site, but can bind to the allosteric site Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.018
-
D-fructose 1,6-bisphosphate pH 7.4, temperature not specified in the publication, wild-type enzyme Homo sapiens
0.04
-
D-fructose 1,6-bisphosphate pH 7.4, temperature not specified in the publication, mutant enzyme K274L Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activates Homo sapiens
Mg2+ Mg2+ or Mn2+ is required for activity Homo sapiens
Mn2+ activates Homo sapiens
Mn2+ Mg2+ or Mn2+ is required for activity Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-fructose 1,6-bisphosphate + H2O Homo sapiens
-
D-fructose 6-phosphate + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 1,6-bisphosphate + H2O
-
Homo sapiens D-fructose 6-phosphate + phosphate
-
?
additional information the FBP active site works by stabilizing the FBPase, and the allosteric site impairs the activity of FBPase through its binding of a nonsubstrate molecule. Competitive inhibition of AMP, fructose 1,6-bisphosphate, or fructose 6-phosphate binding to FBPase with fluorescent AMP analogue, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate (TNP-AMP)-binding FBPase Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
FBPase
-
Homo sapiens
fructose-1,6-bisphosphatase
-
Homo sapiens

General Information

General Information Comment Organism
metabolism regulatory enzyme in the gluconeogenesis pathway Homo sapiens
additional information the FBP active site works by stabilizing the FBPase, and the allosteric site impairs the activity of FBPase through its binding of a nonsubstrate molecule. Competitive inhibition of AMP, fructose 1,6-bisphosphate, or fructose 6-phosphate binding to FBPase with fluorescent AMP analogue, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate (TNP-AMP)-binding FBPase Homo sapiens