EC Number   |
Posttranslational Modification |
Reference |
|---|
   2.7.3.2 | more |
enzyme activity depends on free sulfhydryl groups |
642402, 642411, 642415 |
| 2.7.3.2 | more |
titration of two thiol groups leads to almost complete loss of activity |
642408 |
| 2.7.3.2 | phosphoprotein |
soluble creatine kinase from euthermic squirrels is a mix of phosphorylated and dephosphorylated forms. In hibernating animals only phospho-enzyme is detected. High and low phosphate enzyme forms show different affinities for ATP and creatine substrates, but do not differ in stability to urea denaturation |
671627 |
| 2.7.3.2 | phosphoprotein |
the cellular energy sensor AMP-activated protein kinase (AMPK) is able to phosphorylate brain-type cratine kinase at Ser6 to trigger the enzyme's localization at the endoplasmic reticulum, in close vicinity of the highly energy-demanding Ca2+ ATPase pump |
737427 |
| 2.7.3.2 | phosphoprotein |
the cellular energy sensor AMP-activated protein kinase (AMPK) is able to phosphorylate brain-type cratine kinase at Ser6 to trigger the enzyme's localization at the endoplasmic reticulum, in close vicinity of the highly energy-demanding Ca2+ ATPase pump. BCK phosphorylation is a regulatory process for cellular localization that involves a particular physiological signal (energy stress) which is highly specific for a defined protein kinase (AMPK) and a specific BCK site (Ser6), and provides colocalization between BCK and an ATPase |
-, 737427 |
| 2.7.3.2 | side-chain modification |
intrachain disulfide bond in oxidized form of enzyme is formed between C74 and C146 |
674788 |
