Zobrazeno 1 - 10
of 138
pro vyhledávání: '"Nicolas Glansdorff"'
Autor:
Jan Massant, Nicolas Glansdorff
Publikováno v:
Archaea, Vol 1, Iss 6, Pp 365-373 (2005)
A somewhat neglected but essential aspect of the molecular physiology of hyperthermophiles is the protection of thermolabile metabolites and coenzymes. An example is carbamoyl phosphate (CP), a precursor of pyrimidines and arginine, which is an extre
Externí odkaz:
https://doaj.org/article/c70bd217cb8c4a1e90856a19c5ba43d7
A detailed overview of the current state of knowledge about this special group of organisms. • Serves as an essential volume for a variety of scientists, including microbiologists, biochemists, physiologists, biotechnology specialists, ecologists,
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:
Journal of Molecular Evolution. 77:70-80
Dihydroorotases are universal proteins catalyzing the third step of pyrimidine biosynthesis. These zinc metalloenzymes belong to the superfamily of cyclic amidohydrolases, comprising also other enzymes that are involved in degradation of either purin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15aabfb2ca591c509a0aff0c97d67a9c
https://doi.org/10.1007/s00239-013-9580-1
https://doi.org/10.1007/s00239-013-9580-1
Autor:
Nicolas Glansdorff, Jan Massant
Publikováno v:
Archaea, Vol 1, Iss 6, Pp 365-373 (2005)
A somewhat neglected but essential aspect of the molecular physiology of hyperthermophiles is the protection of thermolabile metabolites and coenzymes. An example is carbamoyl phosphate (CP), a precursor of pyrimidines and arginine, which is an extre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bde7f3ee2b1a6591a57a7874af88f54
https://doaj.org/article/c70bd217cb8c4a1e90856a19c5ba43d7
https://doaj.org/article/c70bd217cb8c4a1e90856a19c5ba43d7
Publikováno v:
Microbiology. 150:3908-3911
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4d3eb75d3e2a9fcc034fc8d1a0e10d7
https://doi.org/10.1099/mic.0.27640-0
https://doi.org/10.1099/mic.0.27640-0
Autor:
Ying Xu, Nicolas Glansdorff
Publikováno v:
Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology. 133:677-688
In this paper we critically review the 'classical' model for the emergence of the three domains (Archaea, Bacteria, Eucarya), which presents hyperthermophilic procaryotes as the ancestors of all life on this planet. We come to the conclusion that our
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1862abf2f264336ba3f8938b828add46
https://doi.org/10.1016/s1095-6433(02)00197-6
https://doi.org/10.1016/s1095-6433(02)00197-6
Publikováno v:
Molecular Microbiology. 45:1541-1555
Ss-Lrp, from Sulfolobus solfataricus, is an archaeal homologue of the global bacterial regulator Lrp (Leucine-responsive regulatory protein), which out of all genome-encoded proteins is most similar to Escherichia coli Lrp (E-value of 5.6 e-14). The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::797e6e03d216c9ca6ae5cc2fd1cd7f6c
https://doi.org/10.1046/j.1365-2958.2002.03136.x
https://doi.org/10.1046/j.1365-2958.2002.03136.x
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