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Protein Kinases and Phosphatases

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

Phosphorylation

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...

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Related Experiment Video

Updated: Jan 6, 2026

Colorimetric Analysis of Alkaline Phosphatase Activity in S. aureus Biofilm

Colorimetric Analysis of Alkaline Phosphatase Activity in S. aureus Biofilm

Published on: April 12, 2019

Rapidly Changing Alkaline Phosphatase

Christopher W Farnsworth¹, Andrew E O Hughes², Melissa M Budelier²

¹Department of Pathology and Immunology, Division of Laboratory and Genomic Medicine, Washington University School of Medicine, Saint Louis, MO. cwfarnsworth@wustl.edu.

Clinical Chemistry

|October 2, 2019

Summary

No abstract available in PubMed .

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