Undecaprenyl pyrophosphate synthetase from Lactobacillus plantarum: A dimeric protein

摘要: a++Undecaprenyl pyrophosphate synthetase has been purified from Lactobacillus plantarum. It catalyzes the formation of a C55 polyprenyl having isoprene residues with cis stereochemistry. The enzyme was shown to be an acidic protein (pI = 5.1), which can partially by preparative gel electrophoresis and Blue-agarose column chromatography. Km's for its substrates t,t-farnesyl isopentenyl were determined 0.13 1.92 microM, respectively. molecular weight estimated sieve chromatography gradient centrifugation 56,000 +/- 4000. Analysis sodium dodecyl sulfate-polyacrylamide indicated that composed dimer 30,000-Da subunits. inactivated arginine-specific reagents phenylglyoxal, butanedione and, cyclohexanedione, but this inactivation not prevented either substrates.