Purification and characterization of dihydrofolate reductase from Mycobacterium phlei.
The dihydrofolate reductase from Mycobacterium phlei was purified and characterized; it has an Mr of 15 000 and a pI of 4.8. It is competitively inhibited by both methotrexate and trimethoprim, although the affinity is less than for other bacterial dihydrofolate reductases.
D005493:Folic Acid Antagonists; D006863:Hydrogen-Ion Concentration; D008727:Methotrexate / Q000494:pharmacology; D009161:Mycobacterium / Q000201:enzymology*; D009168:Mycobacterium phlei / Q000201:enzymology*; D013762:Tetrahydrofolate Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism*; D014295:Trimethoprim / Q000494:pharmacology
D005493:Folic Acid Antagonists; D014295:Trimethoprim; D013762:Tetrahydrofolate Dehydrogenase; D008727:Methotrexate