Thiaminokinase in parent and pyrithiamine mutant Staphylococcus aureus.
1. As a result of the mutation of Staphylococcus aureus by pyrithiamine, deletion of the enzyme thiaminokinase in the system occurs. Some properties of thiaminokinase including the effects of pH, pyrophosphate donor nucleotides and metal ions on the enzyme in the parent S. aureus have been studied. Cell-free extract from mutant strain has been studied under similar conditions and thiaminokinase activity was found to be absent. Addition of thiamine (10mug./ml.) to the medium containing pyrithiamine (required for the growth of the mutant strain) did not give rise to thiaminokinase activity in the mutant bacteria. 2. The parent and the mutant strains of S. aureus have been studied for the fermentative production of acetylmethylcarbinol (3-hydroxybutan-2-one) and the mutant strain did not produce acetylmethylcarbinol under the conditions used.
D002474:Cell-Free System; D005285:Fermentation; D006863:Hydrogen-Ion Concentration; D008670:Metals / Q000494:pharmacology; D009154:Mutation / Q000187:drug effects*; D010770:Phosphotransferases / Q000037:antagonists & inhibitors*; D013210:Staphylococcus / Q000201:enzymology*; D013831:Thiamine / Q000378:metabolism; D013835:Thiamine Pyrophosphate / Q000494:pharmacology
D008670:Metals; D010770:Phosphotransferases; D013835:Thiamine Pyrophosphate; D013831:Thiamine