Corpus ID: 29636770

A defect in histidine biosynthesis causing an adenine deficiency.

  title={A defect in histidine biosynthesis causing an adenine deficiency.},
  author={Alexandra Shedlovsky and Boris Magasanik},
  journal={The Journal of biological chemistry},
In recent years, the role of purine nucleotides in the biosynthesis of histidine has been elucidated (2-5). The early steps of histidine biosynthesis comprise the purine nucleotide cycle shown schematically in Fig. 1. Adenosine triphosphate and 5-phosphoribosylpyrophosphate condense to form N-1-phosphoribosyl adenosine triphosphate; this compound is converted in several steps to Compound III in which the bond between N-l and C-2 of the purine ring has been cleaved; Compound III subsequently… Expand
Imidazole glycerol phosphate synthase: the glutamine amidotransferase in histidine biosynthesis.
Steady-state kinetic parameters for the holoenzyme indicate that glutamine is a more efficient substrate relative to ammonium ion by a factor of 10(3), and the mechanistic significance of this glutaminase activity compared to other trpG type glutamine amidotransferases is discussed. Expand
CHAPTER 8 – Regulation of Purine and Pyrimidine Metabolism
This chapter discusses the regulation of purine and pyrimidine metabolism, and the mechanisms by which exogenously supplied aglycones and nucleosides are rescued and returned to the nucleotide pools. Expand
Effect of α-methylhistidine on the control of histidine synthesis
It is proposed that the increase in the histidine biosynthetic enzymes results from the inhibition of the transfer of histidine to soluble RNA, and it must be the internal concentration of histidinyl-RNA, not of free histidine, that controls the degree of repression of these enzymes in the cell. Expand
Regulation of nitrogenase synthesis in histidine auxotrophs of Klebsiella pneumoniae with altered levels of adenylate nucleotides
Inhibition of phosphoribosyl phosphotransferase with 2-thiazolyl-DL-alanine restored nitrogenase activity and synthesis, indicating that the effect of the hisA mutation on nif expression was probably a consequence of lowered energy resources that occurred during anaerobic N starvation. Expand
Revisiting Purine-Histidine Cross-Pathway Regulation in Saccharomyces cerevisiae
5′-Phosphoribosyl-4-carboxamide-5-aminoimidazole (AICAR), a metabolic intermediate at the crossroads between these two pathways, is shown here to be critical for activation of the transcriptional response in the absence of adenine. Expand
The effect of the histidine analogue, 1,2,4-triazole-3-alanine (TRA), on growth and enzyme synthesis in histidine auxotrophs of Salmonella typhimurium has been studied and it fails to act as a feedback inhibitor of the first step in the formation of histidine. Expand
Metabolic Flux in Both the Purine Mononucleotide and Histidine Biosynthetic Pathways Can Influence Synthesis of the Hydroxymethyl Pyrimidine Moiety of Thiamine in Salmonella enterica
The molecular genetic characterization of purI mutants and their respective pseudorevertants resulted in the conclusion that <1% of the wild-type activity of the PurI enzyme was sufficient for thiamine but not for purine synthesis. Expand
Histidine starvation and adenosine 5'-triphosphate depletion in chemotaxis of Salmonella typhimurium
Results suggest that an adenosine 5'-triphosphate deficiency was responsible for the change in tumbling frequency, and that the change to smooth motility was prevented by 2-thiazolealanine, which inhibits phosphoribosyltransferase, thereby preventing adenine depletion during histidine starvation. Expand
Effect of histidine on purine nucleotide synthesis and utilization in Neurospora crassa
The effect of histidine on purine nucleotide pool utilization resulted in stimulated germination of ad8 and ad4 mutant conidia in adenine-deficient medium, and increased germination was correlated with increased net levels of nucleic acids in these strains. Expand
Combined, Functional Genomic-Biochemical Approach to Intermediary Metabolism: Interaction of Acivicin, a Glutamine Amidotransferase Inhibitor, with Escherichia coliK-12
This molecule prevented the growth of Escherichia coli in minimal medium unless the medium was supplemented with a purine or histidine, suggesting that the HisHF enzyme, a glutamine amidotransferase, was the target of acivicin action. Expand


MCELROY AND B. GLASS (Editors), Amino acid metabolism
  • 1955