Zobrazeno 1 - 10
of 43
pro vyhledávání: '"Sabine Eberhardt"'
Autor:
Stefanie Püttmer, Johannes Kaiser, Nicholas Schramek, Sabine Eberhardt, Adelbert Bacher, Michael Schuster
Publikováno v:
European Journal of Biochemistry. 269:5264-5270
GTP cyclohydrolase II catalyzes the hydrolytic release of formate and pyrophosphate from GTP producing 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, the first committed intermediate in the biosynthesis of riboflavin. The enzyme was show
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::23ac688565a726c1f771a1d71e0bf8f6
https://doi.org/10.1046/j.1432-1033.2002.03239.x
https://doi.org/10.1046/j.1432-1033.2002.03239.x
Autor:
Sabine Eberhardt, Nora Zingler, Adelbert Bacher, Mark Cushman, Gerald Richter, Kristina Kemter
Publikováno v:
European Journal of Biochemistry. 268:4315-4323
Riboflavin synthase of Escherichia coli is a homotrimer of 23.4 kDa subunits catalyzing the formation of the carbocyclic ring of the vitamin, riboflavin, by dismutation of 6,7-dimethyl-8-ribityllumazine. Intramolecular sequence similarity suggested t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ac97f9a35ee40859a9a9f66e1ec8954d
https://doi.org/10.1046/j.1432-1327.2001.02351.x
https://doi.org/10.1046/j.1432-1327.2001.02351.x
Autor:
Boris Illarionov, Kristina Kemter, Adelbert Bacher, Mark Cushman, Sabine Eberhardt, Gerald Richter
Publikováno v:
Journal of Biological Chemistry. 276:11524-11530
Conserved amino acid residues of riboflavin synthase from Escherichia coli were modified by site-directed mutagenesis. Replacement or deletion of phenylalanine 2 afforded catalytically inactive proteins. S41A and H102Q mutants had substantially reduc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0d40fa37797446baf98f67480b8831d3
https://doi.org/10.1074/jbc.m008931200
https://doi.org/10.1074/jbc.m008931200
Autor:
Markus Fischer, Rudolf Ladenstein, Gudrun Tibbelin, Adelbert Bacher, Winfried Meining, Sabine Eberhardt
Publikováno v:
Journal of Structural Biology. 121:53-60
Riboflavin synthase is a trimer of identical 23-kDa subunits. The primary structure is characterized by considerable similarity of the C-terminal and N-terminal parts. Recombinant riboflavin synthase of Escherichia coli and Bacillus subtilis was crys
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afb042c20e81dd57eb3d1bb0bf6dd834
https://doi.org/10.1006/jsbi.1997.3935
https://doi.org/10.1006/jsbi.1997.3935
Publikováno v:
European Journal of Biochemistry. 242:712-719
The gene coding for riboflavin synthase of Escherichia coli has been cloned by marker rescue on a 6-kb fragment that has been sequenced. The riboflavin synthase gene is identical to the ribC locus and codes for a protein of 213 amino acids with a mis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ffa0900f460a1f9446eaed41c9cd46ac
https://doi.org/10.1111/j.1432-1033.1996.0712r.x
https://doi.org/10.1111/j.1432-1033.1996.0712r.x
Autor:
Chan Yong Lee, Markus Fischer, Kristina Kemter, Boris Illarionov, Ryu-Ryun Kim, Young-Eun Woo, Sabine Eberhardt, Adelbert Bacher, Mark Cushman, Wolfgang Eisenreich
Publikováno v:
Journal of biochemistry and molecular biology. 40(2)
Riboflavin synthase from Escherichia coli is a homotrimer of 23.4 kDa subunits and catalyzes the formation of one molecule each of riboflavin and 5-amino-6-ribitylamino- 2,4(1H,3H)-pyrimidinedione by the transfer of a 4-carbon moiety between two mole
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e507641a2a2435ee4d2373fe11bf9f8
https://pubmed.ncbi.nlm.nih.gov/17394775
https://pubmed.ncbi.nlm.nih.gov/17394775
Publikováno v:
Journal of molecular biology. 331(5)
Riboflavin synthase of Escherichia coli is a homotrimer with a molecular mass of 70 kDa. The enzyme catalyzes the dismutation of 6,7-dimethyl-8-(1'-D-ribityl)-lumazine, affording riboflavin and 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione. The N
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f23b4934b6d5ce5713bccf971e78ce23
https://pubmed.ncbi.nlm.nih.gov/12927541
https://pubmed.ncbi.nlm.nih.gov/12927541
Autor:
Johannes, Kaiser, Nicholas, Schramek, Sabine, Eberhardt, Stefanie, Püttmer, Michael, Schuster, Adelbert, Bacher
Publikováno v:
European journal of biochemistry. 269(21)
GTP cyclohydrolase II catalyzes the hydrolytic release of formate and pyrophosphate from GTP producing 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, the first committed intermediate in the biosynthesis of riboflavin. The enzyme was show
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4938370c50c88ef2a63d5895126a9cab
https://pubmed.ncbi.nlm.nih.gov/12392559
https://pubmed.ncbi.nlm.nih.gov/12392559
Autor:
Sabine Eberhardt, Tammo Diercks, Holger Lüttgen, Murray Coles, Horst Kessler, Vincent Truffault, Kerstin Abelmann, Adelbert Bacher
Publikováno v:
Journal of molecular biology. 309(4)
The structure of the amino-terminal domain of Escherichia coli riboflavin synthase (RiSy) has been determined by NMR spectroscopy with riboflavin as a bound ligand. RiSy is functional as a 75 kDa homotrimer, each subunit of which consists of two doma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a64aedd3f2ceaaab0a01c083a21dbcd
https://pubmed.ncbi.nlm.nih.gov/11399071
https://pubmed.ncbi.nlm.nih.gov/11399071
Autor:
Stefan Herz, Wolfgang Eisenreich, Markus Fischer, Boris Illarionov, Gerald Richter, Adelbert Bacher, Sabine Eberhardt, Klaus Kis
The biosynthesis of one riboflavin molecule requires one molecule of GTP and two molecules of ribulose 5-phosphate. The imidazole ring of GTP is hydrolytically opened, yielding a 4,5-diaminopyrimidine that is converted to 5-amino-6-ribitylamino-2,4(1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2fdf1f31aac8b7ebae1618bb0fd32122
https://doi.org/10.1016/s0083-6729(01)61001-x
https://doi.org/10.1016/s0083-6729(01)61001-x
