Biology:Goodpasture-antigen-binding protein kinase

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Goodpasture-antigen-binding protein kinase
Identifiers
EC number2.7.11.9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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 [math]\displaystyle{ \rightleftharpoons }[/math] 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

  • "Characterization of a novel type of serine/threonine kinase that specifically phosphorylates the human goodpasture antigen". J. Biol. Chem. 274 (18): 12642–9. 1999. doi:10.1074/jbc.274.18.12642. PMID 10212244. 
  • "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. 2000. doi:10.1074/jbc.M002769200. PMID 11007769.