Literature summary for 2.7.1.11 extracted from

Ramirez-Sarmiento, C.A.; Baez, M.; Zamora, R.A.; Balasubramaniam, D.; Babul, J.; Komives, E.A.; Guixe, V.
The folding unit of phosphofructokinase-2 as defined by the biophysical properties of a monomeric mutant (2015), Biophys. J., 108, 2350-2361.

Search for more literature for 2.7.1.11

Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
L93A	single-point mutant, constructed to destabilize the interface of isoform Pfk2. The mutant is an inactive monomer at protein concentrations below 30 microM. Active dimer formation can be induced by increasing the protein concentration and by addition of its substrate fructose-6-phosphate. Unfolding occurs noncooperatively and the isolated subunit is partially unstructured and marginally stable	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P06999	-	-

Subunits

Subunits	Comment	Organism
More	the isolated subunit has overall higher solvent accessibility than the native dimer, with the exception of residues 240-309, corresponding to most of the beta-meander module. The hydrophobic core of the isolated monomer of Pfk2 is solvent-penetrated in native conditions and the beta-meander module is not affected by monomerizing mutations	Escherichia coli

Synonyms

Synonyms	Comment	Organism
ATP-dependent 6-phosphofructokinase isozyme 2	-	Escherichia coli
pfkB	-	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)