Výsledky vyhledávání - "Reiner Grabowski"

Bacterial l-serine dehydratases: a new family of enzymes containing iron-sulfur clusters

Autor: Antje E. M. Hofmeister, Reiner Grabowski, Wolfgang Buckel

Publikováno v: Trends in Biochemical Sciences. 18:297-300

Two families of enzymes are described which catalyse identical chemical reactions but differ in their prosthetic groups and hence in their mechanism of action. One family, the pyridoxal-5'-phosphate (PLP)-dependent L-threonine dehydratases, also use

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32ffd84d6c5d47b4962e65b8072130f4
https://doi.org/10.1016/0968-0004(93)90040-t

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The Saccharomyces cerevisiae SOP1 and SOP2 genes, which act in cation homeostasis, can be functionally substituted by the Drosophila lethal(2)giant larvae tumor suppressor gene

Autor: Dieter Strand, Florian Böhl, Bernard M. Mechler, Reiner Grabowski, Lennart Adler, Noreen Akhtar, Katrin Larsson, Ingrid Sjöström

Publikováno v: The Journal of biological chemistry. 273(50)

By complementation of a salt-sensitive mutant of Saccharomyces cerevisiae, we cloned the SOP1 gene, encoding a 114.5-kDa protein of 1033 amino acids. Cells deleted for SOP1 exhibited sensitivity to sodium stress, but showed no sensitivity to general

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52f1e3a1ab3ab0fb0ef30d8a47ac518f
https://pubmed.ncbi.nlm.nih.gov/9837945

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High-affinity binding of the yeast cis-Golgi t-SNARE, Sed5p, to wild-type and mutant Sly1p, a modulator of transport vesicle docking

Autor: Reiner Grabowski, Dieter Gallwitz

Publikováno v: FEBS letters. 411(2-3)

Docking of ER-derived vesicles to the cis-Golgi compartment in yeast requires vesicle and target membrane receptors (v-SNAREs and t-SNAREs) and the GTPase Ypt1p. The t-SNARE Sed5p is complexed with Sly1p in vivo. The mutant form Sly1-20p rescues Ypt1

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66e2ec3c1b49f7fc1d4db9f9a87ce767
https://pubmed.ncbi.nlm.nih.gov/9271199

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Purification and properties of an iron-sulfur-containing and pyridoxal-phosphate-independent L-serine dehydratase from Peptostreptococcus asaccharolyticus

Autor: Reiner Grabowski, Wolfgang Buckel

Publikováno v: European journal of biochemistry. 199(1)

L-Serine dehydratase with a specific activity of 15 nkat/mg protein was present in the anaerobic eubacterium Peptostreptococcus asaccharolyticus grown either on L-glutamate or L-serine. The enzyme was highly specific for L-serine with the lowest Km =

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12f4cc7b8f3c6d31a37a539239c3031d
https://pubmed.ncbi.nlm.nih.gov/2065681

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