Zobrazeno 1 - 10
of 63
pro vyhledávání: '"André, Piérard"'
Publikováno v:
Microbiology (Reading, England). 141(5)
SUMMARYThe biosynthesis of carbamoyl phosphate (CP), a metabolic precursor of arginine and the pyrimidines was investigated in the hyperthermophilic archaeon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7bd6b7016228d380649c9b851d78628d
https://pubmed.ncbi.nlm.nih.gov/33820113
https://pubmed.ncbi.nlm.nih.gov/33820113
Publikováno v:
Current Genetics. 38:78-86
The Lys14 regulatory protein of Saccharomyces cerevisiae activates the expression of the LYS genes involved in the lysine biosynthetic pathway. Studies with a fused Lys14-green fluorescent protein reveal that Lys14p is localised to the nucleus, even
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2bbc618b072b8e90578fa9a2196adb96
https://doi.org/10.1007/s002940000134
https://doi.org/10.1007/s002940000134
Autor:
Catherine Tricot, Daniel Charlier, Vincent Villeret, Sylviane N. Delannay, Victor Stalon, André Piérard
Publikováno v:
Journal of Molecular Biology. 286:1217-1228
Escherichia coli carbamoylphosphate synthetase (CPSase) is a key enzyme in the pyrimidine nucleotides and arginine biosynthetic pathways. The enzyme harbors a complex regulation, being activated by ornithine and inosine 5'-monophosphate (IMP), and in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::66e58921f0e555f2890f8c0b8a17a354
https://doi.org/10.1006/jmbi.1999.2561
https://doi.org/10.1006/jmbi.1999.2561
Autor:
Nicolas Glansdorff, Martine Roovers, Daniel Charlier, André Piérard, Daniel Gigot, Nadine Huysveld
Publikováno v:
Journal of Molecular Biology. 250:383-391
By measuring the protection against Dam methylase modification of a GATC sequence located 106 bp upstream of the startpoint of promoter P1 in the control region of the carAB operon (encoding carbamoylphosphate synthetase) we have obtained evidence fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8177cb188048011d7cfaf07127d145e2
https://doi.org/10.1006/jmbi.1995.0384
https://doi.org/10.1006/jmbi.1995.0384
Autor:
M. Van de Casteele, Pingguo Chen, C Legrain, K. Van Lierde, Nicolas Glansdorff, L. Desmarez, André Piérard
Publikováno v:
Biocatalysis. 11:165-179
Aspartate carbamoyltransferase genes from the extreme thermophilic eubacteria Ta. maritima and T. aquaticus were cloned by complementation in E. coli.Sequencing of the Ta. maritima pyrB gene, the aberrant behaviour of the enzyme product in E. coli, a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2649104fa7fd06b018f38536f1676cef
https://doi.org/10.3109/10242429409034386
https://doi.org/10.3109/10242429409034386
Autor:
A. Boyen, Raymond Cunin, André Piérard, Françoise Van Vliet, Daniel Charlier, Nicolas Glansdorff, Yoshikazu Nakamura, Martine Roovers
Publikováno v:
Journal of Molecular Biology. 226:367-386
The 12 genes which in E. coli K-12 constitute the arginine regulon are organized in nine transcriptional units all of which contain in their 5′ non-coding region two 18 bp partially conserved imperfect palindromes (ARG boxes) which are the target s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5bf2f468ad447d425db2f6f65d81abad
https://doi.org/10.1016/0022-2836(92)90953-h
https://doi.org/10.1016/0022-2836(92)90953-h
Autor:
Vehary Sakanyan, Nicolas Glansdorff, Anahit Kochikyan, Christianne Legrain, Igor Mett, André Piérard, Daniel Charlier
Publikováno v:
Scopus-Elsevier
Summary: The expression of Bacillus stearothermophilus genes complementing arginine auxotrophs of Escherichia coli was studied. The activity responsible for the formation of ornithine in B. stearothermophilus was identified as a repressible ornithine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::edd764cb9036682ebfa4e45d642190d3
https://doi.org/10.1099/00221287-138-1-125
https://doi.org/10.1099/00221287-138-1-125
Autor:
S. Marcq, Victor Stalon, Otto Dideberg, André Piérard, Catherine Tricot, Paulette Charlier, A. Diaz-Ruano
Publikováno v:
Journal of Molecular Biology. 220:9-12
The catabolic ornithine carbamoyltransferase (EC 2.1.3.3) from Pseudomonas aeruginosa, that shows allosteric behaviour, and a mutant version of this enzyme has been crystallized in several different crystal forms. All of these have been characterized
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cf5d2d4abc03e4fbfb04b6120902044d
https://doi.org/10.1016/0022-2836(91)90375-g
https://doi.org/10.1016/0022-2836(91)90375-g
Publikováno v:
Journal of General Microbiology. 136:1177-1183
Summary: The pathway of arginine biosynthesis was investigated in two thermophilic eubacteria, Thermus aquaticus and Thermotoga maritima, and in two thermophilic archaeobacteria, Sulfolobus solfataricus and Pyrococcus furiosus. In the first three org
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6881137573698c88bd7788fe31825e29
https://doi.org/10.1099/00221287-136-7-1177
https://doi.org/10.1099/00221287-136-7-1177
Publikováno v:
Molecular microbiology. 43(6)
Transcription of lysine genes in Saccharomyces cerevisiae is dependent on Lys14p and on alpha-aminoadipate semialdehyde (alphaAASA), an intermediate of the pathway. The two-thirds C-terminal end of Lys14p is sufficient to ensure the activation functi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42d070352062c84204eb376f591cd464
https://pubmed.ncbi.nlm.nih.gov/11952910
https://pubmed.ncbi.nlm.nih.gov/11952910