Naslov
How tyrosine phosphorylation affects the UDP-glucose dehydrogenase activity of Bacillus subtilis YwqF

Autori
Mijaković, Ivan ; Petranović, Dina ; Deutscher, Joseph

Izvornik
Journal of molecular microbiology and biotechnology (1464-1801) 8 (2004), 1; 19-25

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
tyrosine phosphorylation; UDP-glucose dehydrogenase; IwqF

Sažetak
The UDP-glucose dehydrogenase activity of Bacillus subtilis YwqF is regulated by reversible phosphorylation on a tyrosine residue. This reaction, which is catalyzed by the protein-tyrosine kinase YwqD, activates the enzyme, while dephosphorylation of phosphotyrosine-YwqF by the phosphotyrosine-protein phosphatase YwqE reduces its enzyme activity. Our kinetic data indicate that the phosphorylated and unphosphorylated forms of YwqF differ in binding the substrates. The UDP-glucose dehydrogenase reaction catalyzed by YwqF is inhibited by one of its substrates, UDP-glucose, and the extent of this inhibition seems to be reduced upon YwqF phosphorylation. We propose that this effect could at least partly account for the observed activation of YwqF induced by tyrosine phosphorylation. Potential physiological implications of this finding are discussed.

Izvorni jezik
Engleski

Znanstvena područja
Biologija

POVEZANOST RADA