2,5-dihydrophenylalanine as an inhibitor of microbial growth.

  title={2,5-dihydrophenylalanine as an inhibitor of microbial growth.},
  author={D. S. Genghof},
  journal={Canadian journal of microbiology},
  volume={16 6},
  • D. S. Genghof
  • Published 1970
  • Biology, Medicine
  • Canadian journal of microbiology
DL-2,5-Dihydrophenylalanine (DHPA) inhibited the growth of a variety of bacteria representing 10 different genera. Three yeasts were also sensitive to DHPA but only two of nine filamentous fungi we... 
Stoffwechselprodukte von Mikroorganismen
Summaryl-2,5-Dihydrophenylalanine has been isolated from cultures of two strains of Streptomyces. The antibiotic activity of this compound is antagonized by Phenylalanine andExpand
L-3-(2,5-dihydrophenyl)alanine, an antimetabolite of L-phenylalanine produced by a streptomycete.
An unclassified species of a Streptomycete, X-13,185, when grown in a medium containing glucose; asparagine; yeast extract; and yeast extract produced a substance inhibitory to the growth of Bacillus subtilis and Escherichia colt (Davis and Mingioli minimal agarx). Expand
Biosynthesis of the antibiotic 2,5-dihydrophenylalanine by Streptomyces arenae.
By preparing and feeding 5,6-dihydro[4-3H]prephenate it was shown that this compound is not an intermediate in the biosynthesis of DHPA and a reaction sequence is proposed for the conversion of prephenate to DHPA, involving an allylic rearrangement and a combined decarboxylation/dehydration. Expand
Incorporation of l-2,5-Dihydrophenylalanine into Cell Proteins of Escherichia coli and Sarcoma 180
  • M. J. Pine
  • Medicine, Biology
  • Antimicrobial Agents and Chemotherapy
  • 1975
The toxicities in steady-state and non-steady-state growth are closely related and it is proposed that single salient protein defects may determine the extent of growth rate reduction. Expand
Biosynthesis of Some Aromatic Antibiotics
Our laboratory has a long-standing interest in the shikimate pathway of aromatic biosynthesis (Floss, 1978) and in the metabolic conversions of trypto phan and related indoles (Floss, 1976). This ledExpand
1,4-Dihydro-l-phenylalanine-its synthesis and behavior in the phenylalanine ammonia-lyase reaction.
Kinetic measurements with phenylalanine ammonia-lyase showed that 1,4-dihydro-l-phenylalanines is no substrate but a moderately good competitive inhibitor of the enzymatic reaction, providing further evidence for the plausibility of the recently proposed mechanism of action of phenylAlanine ammonia -lyase. Expand
L-2,5-dihydrophenylalanine, an inducer of cathepsin-dependent apoptosis in human promyelocytic leukemia cells (HL-60).
Results indicated that DHPA was an inducer of cathepsin-dependent apoptosis in HL-60 cells, and this apoptosis was demonstrated by morphological changes and biochemical analysis. Expand
Dihydrophenylalanine: a prephenate-derived Photorhabdus luminescens antibiotic and intermediate in dihydrostilbene biosynthesis.
It is shown here that L-H(2)Phe is a secreted metabolite in Photorhabdus luminescens cultures and a precursor of a recently described 2,5-dihydrostilbene, illustrating the versatile metabolic rerouting of prephenate from aromatic amino acid synthesis to antibiotic synthesis. Expand
Antimetabolites from microorganisms.
The chapter reviews the techniques to demonstrate antimetabolite reversibility, and discusses biosynthesis, mechanism of action, and basis of selective activity of this group of compounds. Expand


The pathway of ergothioneine biosynthesis in mycobacteria, as judged by the use S(35)-sulfate and l-histidine-2-C(14) as tracers, appears similar to that found in Neurospora crassa and Claviceps purpurea, that is, from histidine to ergothionine via hercynine. Expand
The effect of amino acids on the microbial growth inhibition produced by thienylalanine.
The effects of thienylalanine on Streptococcus faecalis, Lactobacillus arabinosus 17-5, Escherichia coli, and Saccharomyces cerevisiae, and the effects of high concentrations of most of the known naturally occurring amino acids on the inhibitory action of thiamine on the last two organisms are reported. Expand
Inhibition studies with peptides of thienylalanine and phenylalanine.
An agar plate assay for biotin.