Zobrazeno 1 - 10
of 50
pro vyhledávání: '"Christianne, Legrain"'
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:
PLoS ONE, Vol 7, Iss 11, p e50639 (2012)
Several aminopeptidases of the M42 family have been described as tetrahedral-shaped dodecameric (TET) aminopeptidases. A current hypothesis suggests that these enzymes are involved, along with the tricorn peptidase, in degrading peptides produced by
Externí odkaz:
https://doaj.org/article/aeba0cb89f344553a1f3d88e9b64f197
Autor:
Sonia Beeckmans, Virginie Durbecq, Christianne Legrain, Abdelaziz Kholti, Jan Massant, Patrick Verstreken, Pierre Cornelis, Nicolas Glansdorff
Publikováno v:
Journal of Biological Chemistry. 277:18517-18522
Two different approaches provided evidence for a physical interaction between the carbamate kinase-like carbamoyl-phosphate synthetase (CKase) and ornithine carbamoyltransferase (OTCase) from the hyperthermophilic archaeon Pyrococcus furiosus. Affini
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e82d21a9b3a2fb7cfd307e3ffca630d
https://doi.org/10.1074/jbc.m111481200
https://doi.org/10.1074/jbc.m111481200
Publikováno v:
Journal of Biological Chemistry. 276:25404-25410
In Bacillus stearothermophilus ornithine acetyltransferase is a bifunctional enzyme, catalyzing the first and the fifth steps of arginine biosynthesis; it follows a ping-pong kinetic mechanism. A single chain precursor protein is cleaved between the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1358a1a61e66c7e593a89fa68fee874d
https://doi.org/10.1074/jbc.m100392200
https://doi.org/10.1074/jbc.m100392200
Autor:
Frederic Marc, Nicolas Glansdorff, Yann Almeras, Pierre Weigel, Vehary Sakanyan, Christianne Legrain, Marie Santrot
Publikováno v:
European Journal of Biochemistry. 267:5217-5226
The argJ gene coding for N2-acetyl-L-ornithine: L-glutamate N-acetyltransferase, the key enzyme involved in the acetyl cycle of L-arginine biosynthesis, has been cloned from thermophilic procaryotes: the archaeon Methanoccocus jannaschii, and the bac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1f234389347625f253e61d241bc37fe7
https://doi.org/10.1046/j.1432-1327.2000.01593.x
https://doi.org/10.1046/j.1432-1327.2000.01593.x
Publikováno v:
Journal of Bacteriology. 182:1609-1615
In the arginine biosynthetic pathway of the vast majority of prokaryotes, the formation of ornithine is catalyzed by an enzyme transferring the acetyl group of N -α-acetylornithine to glutamate (ornithine acetyltransferase [OATase]) ( argJ encoded).
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::03a66c8ac1159725740e6e07119dd264
https://doi.org/10.1128/jb.182.6.1609-1615.2000
https://doi.org/10.1128/jb.182.6.1609-1615.2000
Autor:
Yuanfu Zhang, Ziyuan Liang, Ying Xu, Nicolas Glansdorff, Christianne Legrain, Mark Van de Casteele
Publikováno v:
Vrije Universiteit Brussel
The aspartate carbamoyltransferase (ATCase) genes of psychrophilic Vibrio strain 2693 were cloned by complementation in Escherichia coli and the enzyme was partly characterized. The genes constitute a pyrBl operon homologous to the cognate structure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab44d721cb3c7caf44709e6bebc6905e
https://doi.org/10.1099/00221287-144-5-1435
https://doi.org/10.1099/00221287-144-5-1435
Autor:
Catherine Tricot, Jozef Van Beeumen, Bernard Clantin, Martine Roovers, Nicolas Glansdorff, Vincent Villeret, Victor Stalon, Christianne Legrain
Publikováno v:
Proceedings of the National Academy of Sciences. 95:2801-2806
The Pyrococcus furiosus (PF) ornithine carbamoyltransferase (OTCase; EC 2.1.3.3 ) is an extremely heat-stable enzyme that maintains about 50% of its activity after heat treatment for 60 min at 100°C. To understand the molecular basis of thermostabil
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1ef3353bdb858a1bef8af8f86c3abf2
https://doi.org/10.1073/pnas.95.6.2801
https://doi.org/10.1073/pnas.95.6.2801
Publikováno v:
European Journal of Biochemistry. 247:1038-1045
The gene coding for ornithine carbamoyltransferase (OTCase, argF) in the hyperthermophilic archaea Pyrococcus furiosus was cloned by complementation of an OTCase mutant of Escherichia coli. The cloned P. furiosus argF gene also complemented a similar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01d013a991cbda701bc7bf3e909365c0
https://doi.org/10.1111/j.1432-1033.1997.01038.x
https://doi.org/10.1111/j.1432-1033.1997.01038.x
Publikováno v:
BMC Systems Biology
BMC Systems Biology, BioMed Central, 2013, 7, pp.99. ⟨10.1186/1752-0509-7-99⟩
BMC Systems Biology, 2013, 7, pp.99. ⟨10.1186/1752-0509-7-99⟩
B M C Systems Biology, 7
BMC Systems Biology, BioMed Central, 2013, 7, pp.99. ⟨10.1186/1752-0509-7-99⟩
BMC Systems Biology, 2013, 7, pp.99. ⟨10.1186/1752-0509-7-99⟩
B M C Systems Biology, 7
Enzymes belonging to mechanistically diverse superfamilies often display similar catalytic mechanisms. We previously observed such an association in the case of the cyclic amidohydrolase superfamily whose members play a role in related steps of purin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7faa5d92fa5f69a44f970d279135a9ed
https://hal.archives-ouvertes.fr/hal-01758866
https://hal.archives-ouvertes.fr/hal-01758866
