Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Marion Graupner"'
Publikováno v:
Journal of Bacteriology. 184:1952-1957
The Methanococcus jannaschii gene MJ0671 was cloned and overexpressed in Escherichia coli , and its gene product was tested for its ability to catalyze the pyridine nucleotide-dependent reduction of either 2,5-diamino-6-ribosylamino-4(3 H )-pyrimidin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3fb784dd9dcb1aec6e853309b669e6af
https://doi.org/10.1128/jb.184.7.1952-1957.2002
https://doi.org/10.1128/jb.184.7.1952-1957.2002
Autor:
Robert H. White, Marion Graupner
Publikováno v:
Biochemistry. 40:10859-10872
The biochemical route for the formation of the phosphodiester bond in coenzyme F(420), one of the methanogenic coenzymes, has been established in the methanoarchaea Methanosarcina thermophila and Methanococcus jannaschii. The first step in the format
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3b9832cd069810f95bbe0fe37c6803d
https://doi.org/10.1021/bi0107703
https://doi.org/10.1021/bi0107703
Publikováno v:
Journal of Bacteriology. 182:5013-5016
Two putativeMethanococcus jannaschiiisocitrate dehydrogenase genes, MJ1596 and MJ0720, were cloned and overexpressed inEscherichia coli, and their gene products were tested for the ability to catalyze the NAD- and NADP-dependent oxidative decarboxyla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f87048c839e1c70a7391dbb297bab366
https://doi.org/10.1128/jb.182.17.5013-5016.2000
https://doi.org/10.1128/jb.182.17.5013-5016.2000
Autor:
Andrea Hickel, Herfried Griengl, Dieter Lehner, Marion Graupner, Albin Hermetter, Otto Glatter
Publikováno v:
Enzyme and Microbial Technology. 21:361-366
The reasons for the deactivation of the hydroxynitrile lyase (Hnl) from the rubber tree ( Hevea brasiliensis ) at low pH values (below 4.0), and the influence of buffer salts as well as the possible stabilization of the enzyme by additives were inves
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7790a9ccd39220a4c5dc7af18d53bb35
https://doi.org/10.1016/s0141-0229(97)00010-0
https://doi.org/10.1016/s0141-0229(97)00010-0
Publikováno v:
Biochemistry. 42(32)
The protein product of the Methanococcus jannaschii MJ0768 gene has been expressed in Escherichia coli, purified to homogeneity, and shown to catalyze the GTP-dependent addition of two l-glutamates to the l-lactyl phosphodiester of 7,8-didemethyl-8-h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92e0e468b90da4c93d4b49227bc3d55c
https://pubmed.ncbi.nlm.nih.gov/12911320
https://pubmed.ncbi.nlm.nih.gov/12911320
Autor:
Robert H. White, Marion Graupner
Analyses of the F 420 s present in Methanococcus jannaschii have shown that these cells contain a series of γ-glutamyl-linked F 420 s capped with a single, terminal α-linked l -glutamate. The predominant form of F 420 was designated as α-F 420 -3
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aea1b7eb0ff57289ef1239c5089d8440
https://europepmc.org/articles/PMC165758/
https://europepmc.org/articles/PMC165758/
Publikováno v:
Biochemistry. 41(11)
The protein product of the Methanococcus jannaschii MJ1256 gene has been expressed in Escherichia coli, purified to homogeneity, and shown to be involved in coenzyme F(420) biosynthesis. The protein catalyzes the transfer of the 2-phospholactate moie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4945433cc3e14978e81e00f3a7db0ef9
https://pubmed.ncbi.nlm.nih.gov/11888293
https://pubmed.ncbi.nlm.nih.gov/11888293
Publikováno v:
Journal of bacteriology. 184(5)
The enzyme responsible for observed IMP cyclohydrolase activity in Methanococcus jannaschii was purified and sequenced: its genetic locus was found to correspond to gene MJ0626. The MJ0626 gene was cloned, and its protein product was expressed in Esc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e45d06b6b54407bd6619899a9240e951
https://pubmed.ncbi.nlm.nih.gov/11844782
https://pubmed.ncbi.nlm.nih.gov/11844782
Autor:
Robert H. White, Marion Graupner
The established pathway for proline biosynthesis in microorganisms is shown in the upper portion of Fig. Fig.1.1. The reaction sequence involves (i) the phosphorylation of the δ-carboxyl of l-glutamate to form l-glutamyl-5-P, (ii) the NADH-depend
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6717430de395e2c6b3170c4076deef4d
https://europepmc.org/articles/PMC95398/
https://europepmc.org/articles/PMC95398/
Autor:
Robert H. White, Marion Graupner
Publikováno v:
Biochimica et biophysica acta. 1548(1)
Reduction of 2-oxoacids to the corresponding (S)-2-hydroxyacids is an important transformation in biochemistry. To date all (S)-2-hydroxyacid dehydrogenases belonging to the L-lactate/L-malate dehydrogenase family have been found to transfer the pro-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::723ab77b96d28b26544dff34dd47601e
https://pubmed.ncbi.nlm.nih.gov/11451450
https://pubmed.ncbi.nlm.nih.gov/11451450