Zobrazeno 1 - 10
of 55
pro vyhledávání: '"F. Foor"'
Autor:
P. J. Barker, Gilberto A Hintermann, A. L. Demain, Xinfa Xiao, F. Foor, Jacqueline Piret, A. Häusler
Publikováno v:
Antimicrobial Agents and Chemotherapy. 37:84-88
A 26-mer DNA probe was designed from N-terminal sequence data for the cephalosporin 7 alpha-hydroxylase (CH) of Streptomyces clavuligerus NRRL 3585 and used to screen a DNA library from this organism. The library was constructed in the lambda GEM-11
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed2dfdf5ee3e6950a4a67891ca9a4802
https://doi.org/10.1128/aac.37.1.84
https://doi.org/10.1128/aac.37.1.84
Autor:
Robert J. Limhardt, C. P. Bahl, G. Bell, R. Picktet, H. M. Goodman, W. J. Rutter, S. Chang, J. H. Meade, S. N. Cohen, C. Colby, D. W. Denney, C. A. Colson, P. E. Cornelis, C. S. Digneffe, C. Walon, R. Crea, R. Curtiss, D. H. Dean, D. M. Ellis, J. T. Fayerman, M. A. Richardson, F. Foor, N. R. Morin, G. P. Roberts, D. V. Goeddel, H. L. Heyneker, J. Shine, P. H. Seeburg, D. H. Hamer, J. Gerin, W. H. Hanisch, P. M. Fernandes, C. L. Hershberger, A. K. Radue, P. R. Rostek, Paul R. Rostek, K. Itakura, M. Kikuchi, T. Hayakawa, M. Kida, M. W. Konrard, L. S. Lin, D. F. Mark, H. S. Kung, O. Kurahashi, T. Tsuchida, H. Kawashima, H. Enei, S. Nakamoris, M. E. Malin, M. D. Jones, J. A. Mabe, W. M. Nakatsukasa, J. R. Miller, S. Kovacevic, N. E. Beerman, R. H. Olsen, G. V. Paddok, A. D. Riggs, A. Ullrich, J. Chirgwin, R. Picket, H. E. Schnepf, H. R. Whiteley, H. Shizuya, B. E. Uhlin, K. Nordstrom, S. Molin, P. Gustaffson, C. B. Ward, R. D. Bruner
Publikováno v:
Applied Biochemistry and Biotechnology. 11:333-348
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a65d73f5896f57e6f42bf06722274f9a
https://doi.org/10.1007/bf02798445
https://doi.org/10.1007/bf02798445
Publikováno v:
Journal of Biological Chemistry. 250:3545-3551
An enzyme that uses GTP as substrate for the formation in stoichiometric quantities of formate, inorganic pyrophosphate, and 2,5-diamino-6-hydroxy-4-(ribosylamino)pyrimidine-5'-phosphate has been purified 2200-fold from extracts of Escherichia coli B
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::de38a486f61f3f29ce6b930cebc65223
https://doi.org/10.1016/s0021-9258(19)41549-4
https://doi.org/10.1016/s0021-9258(19)41549-4
Publikováno v:
Journal of Bacteriology. 150:221-230
We isolated mutants of Klebsiella aerogenes with insertions of transposon Tn5 linked to the structural gene for glutamine synthetase, glnA. We found that K. aerogenes, like Escherichia coli and Salmonella typhimurium, contains a regulatory gene, glnG
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3ab4c4232c099340bbb0bb63cba091a
https://doi.org/10.1128/jb.150.1.221-230.1982
https://doi.org/10.1128/jb.150.1.221-230.1982
Autor:
F, Foor, G M, Brown
Publikováno v:
The Journal of biological chemistry. 250(9)
An enzyme that uses GTP as substrate for the formation in stoichiometric quantities of formate, inorganic pyrophosphate, and 2,5-diamino-6-hydroxy-4-(ribosylamino)pyrimidine-5'-phosphate has been purified 2200-fold from extracts of Escherichia coli B
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e997cd42dd70d41fabf5ed4cfeadf9d3
https://pubmed.ncbi.nlm.nih.gov/235552
https://pubmed.ncbi.nlm.nih.gov/235552
Publikováno v:
Journal of bacteriology. 134(2)
A lambda phage (lambdaNK55) carrying the translocatable element Tn10, conferring tetracycline resistance (Tetr), has been utilized to isolate glutamine auxotrophs of Escherichia coli K-12. Such strains lack uridylyltransferase as a result of an inser
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02c5d0e20d39c408e4dd56a7a86f0510
https://pubmed.ncbi.nlm.nih.gov/26660
https://pubmed.ncbi.nlm.nih.gov/26660
Publikováno v:
Journal of bacteriology. 129(2)
The glutamine synthetase (GS) from Klebsiella aerogenes is similar to that from Escherichia coli in several respects: (i) it is repressed by high levels of ammonia in the growth medium; (ii) its biosynthetic activity is greatly reduced by adenylylati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::49820ef95f04e56b618e1214050c8a95
https://pubmed.ncbi.nlm.nih.gov/14104
https://pubmed.ncbi.nlm.nih.gov/14104
A mutation of Klebsiella aerogenes causing production of an altered PII regulatory protein which stimulates overadenylylation of glutamine synthetase and also prevents its derepression was combined with mutations abolishing the activity of adenylyltr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f61ae3d6163f6042bac82f2f603b1f35
https://europepmc.org/articles/PMC217020/
https://europepmc.org/articles/PMC217020/
Autor:
F, Foor, G M, Brown
Publikováno v:
Methods in enzymology. 66
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b43baf3d5a5d183b392687e20f43d1ec
https://pubmed.ncbi.nlm.nih.gov/6990194
https://pubmed.ncbi.nlm.nih.gov/6990194
Glutamine synthetase of Klebsiella aerogenes: properties of glnD mutants lacking uridylyltransferase
The glnD mutation of Klebsiella aerogenes is cotransducible by phage P1 with pan (requirement for pantothenate) and leads to a loss of uridylytransferase and uridylyl-removing enzyme, components of the glutamine synthetase adenylylation system. This
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7c127e99a5f229140612b0f176feb2c
https://europepmc.org/articles/PMC222287/
https://europepmc.org/articles/PMC222287/