EC Number   |
Posttranslational Modification |
Reference |
|---|
    2.7.1.11 | phosphoprotein |
in Aspergillus niger cells spontaneous posttranslational modification of 6-phosphofructo-1-kinase occurs in a two step process. The native enzyme (85 kDa) is first cleaved to an inactive fragment (49 kDa) that regains its activity after phosphorylation of the protein, the shorter fragment exhibits changed kinetics, such as resistance to citrate inhibition |
704771 |
| 2.7.1.11 | phosphoprotein |
insulin increases phosphorylation of human erythrocyte enzyme |
676017 |
| 2.7.1.11 | phosphoprotein |
phosphorylation of PFKM may exert a major role during starvation in fish muscle |
672415 |
| 2.7.1.11 | phosphoprotein |
the enzyme is regulated by phosphorylation |
673170 |
| 2.7.1.11 | proteolytic modification |
spontaneous posttranslational modification of PFK1 leads to significant changes in allosteric regulation of the enzyme activity |
671410 |
| 2.7.1.11 | proteolytic modification |
the 49000 Da fragment is formed from the 85000 Da native enzyme by posttranslational modification. The native 85000 Da enzyme is moderately inhibited by citrate, the 49000 Da shorter fragment of PFK1 proves to be completely resistant to inhibition by citrate |
671462 |
| 2.7.1.11 | side-chain modification |
- |
640456 |
| 2.7.1.11 | side-chain modification |
2 putative cAMP-dependent protein kinase phosphorylation sites at Ser 293 and Ser 559 |
640505 |
| 2.7.1.11 | side-chain modification |
4.2 mol phosphate/mol of enzyme in rats treated with 3 doses of isoproterenol, 3 mol phosphate/mol enzyme after dephosphorylation, presence of phosphate groups influences the kinetic properties of PFK-1 |
640524 |
| 2.7.1.11 | side-chain modification |
in vitro phosphorylation of PFK fragment containing a cAMP-dependent protein kinase consensus site |
640502 |
