Amino acid analog incorporation into bacterial proteins

Cowie, Dean B.; Cohen, Georges N.; Bolton, Ellis T.; Robichon-Szulmajster, Huguette de

doi:10.1016/0006-3002(59)90230-6

Cited by 122 publications

(50 citation statements)

References 11 publications

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“…4-Fluorophenylalanine can effect a very high degree of replacement (75%) of the normal amino acid (26), and there is little, if any, discrimination against the analog during incorporation into the different classes of soluble protein found in E. coli cells (62). A similar random replacement.…”

Section: Phenylalanine Analogsmentioning

confidence: 99%

Toxic Amino Acids: Their Action as Antimetabolites

Fowden¹,

Lewis²,

Tristram³

1967

Advances in Enzymology - And Related Areas of Molecular Biology

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Section: Phenylalanine Analogsmentioning

confidence: 99%

Toxic Amino Acids: Their Action as Antimetabolites

Fowden¹,

Lewis²,

Tristram³

1967

Advances in Enzymology - And Related Areas of Molecular Biology

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“…[193,199] Typical substitutions include replacement of hydrogen with fluorine, methylene with oxygen or sulfur, and ring substitutions. For example, tryptophan has been replaced with tryptazan, [200] arginine with canavanine, [201] methionine with norleucine, [202] leucine with trifluoroleucine, [203] and the phenyl ring of phenylalanine with thioenyl or furyl rings. Most of the early work focused on studies of the effects of amino acid analogues on bacterial growth and protein synthesis and processing.…”

Section: The Use Of Auxotrophic Bacterial Strains To Incorporate Unnamentioning

confidence: 99%

Expanding the Genetic Code

2004

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Although chemists can synthesize virtually any small organic molecule, our ability to rationally manipulate the structures of proteins is quite limited, despite their involvement in virtually every life process. For most proteins, modifications are largely restricted to substitutions among the common 20 amino acids. Herein we describe recent advances that make it possible to add new building blocks to the genetic codes of both prokaryotic and eukaryotic organisms. Over 30 novel amino acids have been genetically encoded in response to unique triplet and quadruplet codons including fluorescent, photoreactive, and redox-active amino acids, glycosylated amino acids, and amino acids with keto, azido, acetylenic, and heavy-atom-containing side chains. By removing the limitations imposed by the existing 20 amino acid code, it should be possible to generate proteins and perhaps entire organisms with new or enhanced properties.

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“…In liquid media, /3-2-t inhibits growth of many bacterial species (7,10,26,35,37). In most bacteria, inhibition is due to blockage in the Phe biosynthetic pathway through feedback inhibition by Phe of the Phe-sensitive, 3-deoxy-D-arabinoheptulosonic acid 7-PO4 (DAHP) synthetase [EC 4.1.2.15] (18,25).…”

mentioning

confidence: 99%

Comparison of Liquid and Agar‐Solidified Defined Media Regarding the Physiological Mechanism by which β‐2‐Thienylalanine Inhibits Growth of Escherichia, Shigella, and Salmonella Cultures

Brown

Tannock

Elliott

et al. 1980

Microbiology and Immunology

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Growth comparisons were made, using Shigella, Escherichia, and Salmonella cultures, in liquid and agar-solidified defined media containing fl-2-thienylalanine (/3-24). The comparisons were performed to determine the nature of growth inhibition by 13-24 under different physical growth conditions.In a plate assay, with increasing 13-2-t mixed into the agar, inhibition of Escherichia and Shigella increased. However, Salmonella cultures were not inhibited even at the highest /-2-t concentrations used. With 13-2-t added to liquid cultures, however, dose-response growth relationships were exhibited by all three genera.The differences occurring in [3-24 inhibition between liquid and plate assay conditions were not due to composition of culture plates, time of challenge of cultures with 13-24, availability of oxygen and associated differences in ratios of volume of media to available surface area, selection of mutants in the plate assay, or to extractable substances from the agar.However, when fl-2-t diffusion into the liquid medium was delayed by using agar plug diffusion cultures, a physiological mechanism was demonstrable which largely protected Salmonella cultures, but not Escherichia and Shigella cultures, from growth inhibition.

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Amino acid analog incorporation into bacterial proteins

Cited by 122 publications

References 11 publications

Toxic Amino Acids: Their Action as Antimetabolites

Toxic Amino Acids: Their Action as Antimetabolites

Expanding the Genetic Code

Comparison of Liquid and Agar‐Solidified Defined Media Regarding the Physiological Mechanism by which β‐2‐Thienylalanine Inhibits Growth of Escherichia, Shigella, and Salmonella Cultures

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