Type | Description |
---|---|
Definition | 6-phosphofructokinase II |
Date | Results | Publications |
---|---|---|
2017-02-04 10:45:00 | Data show that interactions between fructose-6-P and allosteric sites for ATP are operating within and between the phosphofructokinase-2 (Pfk-2) subunits. | 27591700 |
2011-10-08 11:25:00 | Data show an unstructured monomeric phosphofructokinase-2 intermediate and that most part of the dimer structure is reached as a slow concerted folding/association step with a quite folded transition state in terms of solvent exposure. | 21627967 |
2010-09-27 12:28:00 | Site-directed mutagenesis of R90 and D256 indicate that R90 participates in the binding of the phosphorylated substrate and that D256 is involved in the phosphoryl transfer mechanism. | 20599671 |
2010-01-21 00:00:00 | Results describe the structure of phosphofructokinase-2 in its inhibited tetrameric form, with each subunit bound to two ATP molecules and two Mg ions. | 18762190 |
2010-01-21 00:00:00 | Subunit contacts are critical for the maintenance of the overall structure of Pfk-2 and for the binding of ligands, explaining the reported importance of the dimeric state for enzymatic activity. | 17469854 |
Type | IDs |
---|---|
Synonymous | ECK1721 |
Gene |
UniProtKB-ID:
PFKB_ECOLI
UniprotKB:
P06999
UniParc:
UPI000012DB3D
EMBL:
K00128,
U00096,
K02500,
AP009048
EnsemblGenome:
b1723,
BAA15500
KO:
eco:b1723,
ecj:JW5280
|
Nucleutide sequences |
EMBL-CDS:
AAA24320.1,
AAA24321.1,
BAA15500.2,
AAC74793.1
EnsemblGenome_TRS:
BAA15500,
AAC74793
|
Protein sequencees |
EnsemblGenome_PRO:
BAA15500,
AAC74793
RefSeq:
NP_416237.3
|
Others |
UniRef100:
UniRef100_P06999
UniRef90:
UniRef90_P06999
UniRef50:
UniRef50_P06999
|
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