Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.16 (calcineurin)
 17,112 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Autophosphorylation of protein-tyrosine kinases (PTKs) involved in exopolysaccharide and capsular polysaccharide biosynthesis and transport has been observed in a number of Gram-negative and Gram-positive bacteria. However, besides their own phosphorylation, little is known about other substrates targeted by these protein-modifying enzymes. Here, we present evidence that the protein-tyrosine kinase Wzc of Escherichia coli is able to phosphorylate an endogenous enzyme, UDP-glucose dehydrogenase (Ugd), which participates in the synthesis of the exopolysaccharide colanic acid. The process of phosphorylation of Ugd by Wzc was shown to be stimulated by previous autophosphorylation of Wzc on tyrosine 569. The phosphorylation of Ugd was demonstrated to actually occur on tyrosine and result in a significant increase of its dehydrogenase activity. In addition, the phosphotyrosine-protein phosphatase Wzb, which is known to effectively dephosphorylate Wzc, exhibited only a low effect, if any, on the dephosphorylation of Ugd. These data were related to the recent observation that two other UDP-glucose dehydrogenases have been also shown to be phosphorylated by a PTK in the Gram-positive bacterium Bacillus subtilis. Comparative analysis of the activities of PTKs from Gram-negative and Gram-positive bacteria showed that they are regulated by different mechanisms that involve, respectively, either the autophosphorylation of kinases or their interaction with a membrane protein activator.
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PMID:Autophosphorylation of the Escherichia coli protein kinase Wzc regulates tyrosine phosphorylation of Ugd, a UDP-glucose dehydrogenase. 1285 88

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.
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PMID:How tyrosine phosphorylation affects the UDP-glucose dehydrogenase activity of Bacillus subtilis YwqF. 1574 37