Zobrazeno 1 - 10
of 167
pro vyhledávání: '"Andrée Marquet"'
Autor:
Andrée Marquet, Danielle Fauque
Publikováno v:
European Women in Chemistry
Publikováno v:
International Journal of Peptide and Protein Research. 21:254-257
The synthesis of two glycosylated analogs of Substance P is described. The activity of the peptides was assayed on the isolated guinea-pig ileum and their degradation was studied using rat hypothalamus slices. While glycosylation noticeably enhances
Publikováno v:
International Journal of Peptide and Protein Research. 29:162-169
The general conditions for cyclization of peptides on polymer matrix by disulfide bridge formation are reported. This procedure is based on attack of 3-nitro-2-pyridinesulfenyl group (Npys) by a thiol function. It has been used for synthesis of five
Publikováno v:
International Journal of Peptide and Protein Research. 24:505-515
Pentapeptides Phe-Leu-X-Glu-Val where X is successively L-threo-gamma-fluoro-glutamyl, L-erythro-gamma-fluoro-glutamyl, L-threo-gamma-methyl-glutamyl or L-erythro-gamma-methyl-glutamyl have been synthesized and tested as substrates for the vitamin K-
Autor:
Dominique Florentin, Gérard Bolbach, Andrée Marquet, Tony A. Mattioli, Bernadette Tse Sum Bui
Publikováno v:
Biochemistry. 45:3824-3834
Biotin synthase, a member of the "radical SAM" family, catalyzes the final step of the biotin biosynthetic pathway, namely, the insertion of a sulfur atom into dethiobiotin. The as-isolated enzyme contains a [2Fe-2S](2+) cluster, but the active enzym
Publikováno v:
Biochemical Society Transactions. 33:820-823
Biotin synthase, a member of the ‘radical SAM’ (S-adenosylmethionine) family, converts DTB (dethiobiotin) into biotin. The active form of the Escherichia coli enzyme contains two (Fe-S) centres, a (4Fe-4S) and a (2Fe-2S). The (4Fe-4S)2+/+ mediate
Autor:
Andrée Marquet, Bernadette Tse Sum Bui, Volker Schünemann, Alfred X. Trautwein, Michel Rohmer, Patrick Wegner, Murielle Wolff, Myriam Seemann
Publikováno v:
Journal of Biological Inorganic Chemistry
Journal of Biological Inorganic Chemistry, 2005, 10, pp.131-137
Journal of Biological Inorganic Chemistry, Springer Verlag, 2005, 10, pp.131-137
Journal of Biological Inorganic Chemistry, 2005, 10, pp.131-137
Journal of Biological Inorganic Chemistry, Springer Verlag, 2005, 10, pp.131-137
The mevalonate-independent methylerythritol phosphate pathway is widespread in bacteria. It is also present in the chloroplasts of all phototrophic organisms. Whereas the first steps, are rather well known, GcpE and LytB, the enzymes catalyzing the l
Autor:
Olivier Ploux, Denis Lesage, Stéphane Mann, Dominique Florentin, Andrée Marquet, Thierry Drujon
Publikováno v:
Helvetica Chimica Acta. 86:3836-3850
The mechanism of action of amiclenomycin (1a), a naturally occuring inhibitor of diaminopelargonic acid aminotransferase, has been established. The enzyme catalyzes the formation of an aromatic adduct between the inhibitor and pyridoxal-5′-phosphat
Autor:
Andrée Marquet, Riidiger Benda, Volker Schünemann, Alfred X. Trautwein, Bernadette Tse Sum Bui, Dominique Florentin
Publikováno v:
Biochemistry. 42:8791-8798
Biotin synthase, the enzyme which catalyzes the last step of the biosynthesis of biotin, contains only (2Fe-2S)(2+) clusters when isolated under aerobic conditions. Previous results showed that reduction by dithionite or photoreduced deazaflavin conv
Autor:
Murielle Wolff, Manuel Rodríguez-Concepción, Yves Frapart, Albert Boronat, Ana Garcia Estrabot, Michel Rohmer, Andrée Marquet, Myriam Seemann, Bernadette Tse Sum Bui, Denis Tritsch
Publikováno v:
FEBS Letters. 541:115-120
The last enzyme (LytB) of the methylerythritol phosphate pathway for isoprenoid biosynthesis catalyzes the reduction of (E)-4-hydroxy-3-methylbut-2-enyl diphosphate into isopentenyl diphosphate and dimethylallyl diphosphate. This enzyme possesses a d