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Literature summary for 3.1.3.11 extracted from

  • Shi, R.; Chen, Z.Y.; Zhu, D.W.; Li, C.; Shan, Y.; Xu, G.; Lin, S.X.
    Crystal structures of human muscle fructose-1,6-bisphosphatase: novel quaternary states, enhanced AMP affinity, and allosteric signal transmission pathway (2013), PLoS ONE, 8, e71242.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.3.11

Cloned(Commentary)

Cloned (Comment) Organism
-
 Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
wild-type AMP-bound and product-bound complexes and mutant Q32R, to 1.6 A, 2.2 A, and 2.7 A resolution, respectively. The higher sensitivity of the muscle isozyme towards AMP originates from an additional water-mediated, H-bonded network established between AMP and the binding pocket. The tetrameric assembly of the structures deviates from the canonical R- or T-states, representing novel tetrameric assemblies Homo sapiens

Protein Variants

Protein Variants Comment Organism
Q32R conentration of AMP required for 50% inhibition of the Q32R mutant is increased 19fold, and the cooperativity of both AMP and Mg2+ is abolished or decreased. The mutation affects the conformations of both N-terminal residues and the dynamic loop 52–72 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
AMP
-
 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O00757 isoform FBP2
-

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
 Homo sapiens
-

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.00019
-
 wild-type, pH 7.4, 25°C, Hill-coefficient 1.34 Homo sapiens AMP
0.00365
-
 mutant Q32R, pH 7.4, 25°C, Hill-coefficient 0.59 Homo sapiens AMP