Goodpasture-antigen-binding protein kinase

In enzymology, a Goodpasture-antigen-binding protein kinase (EC 2.7.11.9) is an enzyme that catalyzes the chemical reaction

ATP + Goodpasture antigen-binding protein ${\displaystyle \rightleftharpoons }$ ADP + [Goodpasture antigen-binding phosphoprotein]

Thus, the two substrates of this enzyme are ATP and Goodpasture antigen-binding protein, whereas its two products are ADP and Goodpasture antigen-binding phosphoprotein.

This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is ATP:[Goodpasture antigen-binding protein] phosphotransferase. Other names in common use include GPBPK, GPBP kinase, STK11, and Goodpasture antigen-binding protein kinase. This enzyme participates in mTOR signaling pathway and adipocytokine signaling pathway.

References

• Raya A, Revert F, Navarro S, Saus J (1999). "Characterization of a novel type of serine/threonine kinase that specifically phosphorylates the human goodpasture antigen". J. Biol. Chem. 274 (18): 12642–9. doi:10.1074/jbc.274.18.12642. PMID 10212244.
• Vieites B, Granero F, Forteza J, Saus J (2000). "Goodpasture antigen-binding protein, the kinase that phosphorylates the goodpasture antigen, is an alternatively spliced variant implicated in autoimmune pathogenesis". J. Biol. Chem. 275 (51): 40392–9. doi:10.1074/jbc.M002769200. PMID 11007769.