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Analysis of feedback-resistant anthranilate synthases from Saccharomyces cerevisiae
scientific article
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instance of
scholarly article
1 reference
stated in
PubMed
PubMed ID
8432699
retrieved
1 December 2016
title
Analysis of feedback-resistant anthranilate synthases from Saccharomyces cerevisiae
(English)
1 reference
stated in
PubMed
PubMed ID
8432699
retrieved
1 December 2016
main subject
Saccharomyces cerevisiae
0 references
Anthranilate synthase TRP2 YER090W
1 reference
stated in
GOA release 2020-03-11
author
Gerhard H Braus
series ordinal
3
object named as
G H Braus
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author name string
R Graf
series ordinal
1
0 references
B Mehmann
series ordinal
2
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language of work or name
English
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publication date
February 1993
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published in
Journal of Bacteriology
1 reference
stated in
PubMed
PubMed ID
8432699
retrieved
1 December 2016
volume
175
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page(s)
1061-8
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issue
4
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cites work
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PubMed Central
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Nucleotide sequence of Saccharomyces cerevisiae genes TRP2 and TRP3 encoding bifunctional anthranilate synthase: indole-3-glycerol phosphate synthase
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Purification and characterization of the indole-3-glycerolphosphate synthase/anthranilate synthase complex of Saccharomyces cerevisiae
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PubMed Central
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Aromatic amino acid biosynthesis in the yeast Saccharomyces cerevisiae: a model system for the regulation of a eukaryotic biosynthetic pathway
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Tryptophan biosynthesis in Saccharomyces cerevisiae: control of the flux through the pathway
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DNA sequencing with chain-terminating inhibitors
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Identification and characterization of genes for a second anthranilate synthase in Pseudomonas aeruginosa: interchangeability of the two anthranilate synthases and evolutionary implications
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PubMed Central
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Nucleotide sequence of Escherichia coli pabB indicates a common evolutionary origin of p-aminobenzoate synthetase and anthranilate synthetase
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The presence of a defective LEU2 gene on 2 mu DNA recombinant plasmids of Saccharomyces cerevisiae is responsible for curing and high copy number.
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Anthranilate synthetase
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PubMed Central
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Two single-base-pair substitutions causing desensitization to tryptophan feedback inhibition of anthranilate synthase and enhanced expression of tryptophan genes of Brevibacterium lactofermentum
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A single point mutation results in a constitutively activated and feedback-resistant chorismate mutase of Saccharomyces cerevisiae
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Identification of amino acid residues involved in feedback regulation of the anthranilate synthase complex from Salmonella typhimurium. Evidence for an amino-terminal regulatory site
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Permeabilization of microorganisms by Triton X-100
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Different amino acid substitutions at the same position in the nucleotide-binding site of aspartate transcarbamoylase have diverse effects on the allosteric properties of the enzyme.
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2 June 2018
Free tryptophan pool and tryptophan biosynthetic enzymes in Saccharomyces cerevisiae
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/8432699
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
21 β-Galactosidase gene fusions for analyzing gene expression in Escherichia coli and yeast
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/8432699
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Expression of an artificial yeast TRP-gene cluster in yeast and Escherichia coli
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/8432699
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Tryptophan accumulation in Saccharomyces cerevisiae under the influence of an artificial yeast TRP gene cluster
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/8432699
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Yeast allosteric chorismate mutase is locked in the activated state by a single amino acid substitution
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/8432699
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1128/JB.175.4.1061-1068.1993
0 references
PMCID
193020
0 references
PubMed ID
8432699
1 reference
stated in
PubMed
PubMed ID
8432699
retrieved
1 December 2016
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