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Biochemical and cellular pharmacology of 1843U89, a novel benzoquinazoline inhibitor of thymidylate synthase.
1843U89, the benzoquinazoline which was transported most efficiently and which was the most potent inhibitor of the growth of human cells, exhibited the largest difference between binding to the MOLT-4 human and L1210 murine transporter. Expand
Cloning, sequencing, and enhanced expression of the dihydropteroate synthase gene of Escherichia coli MC4100
The Escherichia coli gene coding for dihydropteroate synthase (DHPS) has been cloned and sequenced and a temperature-sensitive mutant was isolated and found to express a DHPS with a lower specific activity and lower affinities for para-aminobenzoic acid and sulfathiazole. Expand
Inhibition of prolipoprotein signal peptidase by globomycin.
Globomycin inhibits the prolipoprotein-specific signal peptidase activity by binding to the enzyme in a noncompetitive manner (Ki = 36 nM). The Km of prolipoprotein signal peptidase for theExpand
Rapid assay and purification of a unique signal peptidase that processes the prolipoprotein from Escherichia coli B.
  • I. K. Dev, P. Ray
  • Chemistry, Medicine
  • The Journal of biological chemistry
  • 10 September 1984
A simple and accurate assay for prolipoprotein signal peptidase activity has been described that is based on the solubility of the signal peptide in 80% acetone. The unprocessed precursor and theExpand
Sources of one-carbon units in the folate pathway of Escherichia coli.
The anti-human immunodeficiency virus agent 3'-fluorothymidine induces DNA damage and apoptosis in human lymphoblastoid cells
It is demonstrated that FLT caused extensive DNA fragmentation in CEM cells that was not observed when these cells were treated with other, less toxic thymidine analogs, and this observation is offered as a possible explanation for the severe toxicity of FLT observed in vivo. Expand
Minimum substrate sequence for signal peptidase I of Escherichia coli.
Studies of the synthetic peptides showed that decreasing the length of the polypeptide chain of substrates decreased the substrate efficiency measured as kcat/Km, but in one case a decrease in thelength of a peptide corresponding to -7 to +3 positions of pro-MBP to a nonapeptide increased the substrate Efficiency by about 900-fold. Expand
Degradation of a signal peptide by protease IV and oligopeptidase A
The hypothesis that protease IV is the major signal peptide peptidase in membranes that initiates the degradation of the signal peptides by making endoproteolytic cuts is supported. Expand
Mode of binding of folate analogs to thymidylate synthase. Evidence for two asymmetric but interactive substrate binding sites.
The binding affinities of 5,10-methylene tetrahydropteroyltetraglutamate (folate substrate) and a group of close structural folate analog inhibitors are determined and it is concluded that the two subunits of thymidylate synthase bind folate substrates and analogs differently and that the asymmetric binding of the ligands is the major factor that determines the inhibition kinetics of each folATE analog inhibitor. Expand
Localization and purification of two enzymes from Escherichia coli capable of hydrolyzing a signal peptide.
The signal peptide generated during the maturation of prolipop protein by the purified prolipoprotein signal peptidase can be isolated in substrate amounts and is degraded predominantly from the carboxyl terminus by cell-free extracts of Escherichia coli. Expand