Sökning: L773:0264 6021 > (1980-1989) > (1989) > Naturvetenskap > New properties of B...
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000 | 03166naa a2200325 4500 | |
001 | oai:lup.lub.lu.se:68640c32-f9f3-447e-b006-a0653f22d0b1 | |
003 | SwePub | |
008 | 170718s1989 | |||||||||||000 ||eng| | |
024 | 7 | a https://lup.lub.lu.se/record/68640c32-f9f3-447e-b006-a0653f22d0b12 URI |
024 | 7 | a https://doi.org/10.1042/bj26004912 DOI |
040 | a (SwePub)lu | |
041 | a engb eng | |
042 | 9 SwePub | |
072 | 7 | a art2 swepub-publicationtype |
072 | 7 | a ref2 swepub-contenttype |
100 | 1 | a Hederstedt, Larsu Lund University,Lunds universitet,Molekylär cellbiologi,Biologiska institutionen,Naturvetenskapliga fakulteten,Molecular Cell Biology,Department of Biology,Faculty of Science4 aut0 (Swepub:lu)mikb-lhe |
245 | 1 0 | a New properties of Bacillus subtilis succinate dehydrogenase altered at the active site |
264 | 1 | b Portland Press Ltd.c 1989 |
520 | a Mammalian and Escherichia coli succinate dehydrogenase (SDH) and E. coli fumarate reductase apparentlycontain an essential cysteine residue at the active site, as shown by substrate-protectable inactivation withthiol-specific reagents. Bacillus subtilis SDH was found to be resistant to this type of reagent and containsan alanine residue at the amino acid position equivalent to the only invariant cysteine in the flavoproteinsubunit of E. coli succinate oxidoreductases. Substitution of this alanine, at position 252 in the flavoprotein subunit of B. subtilis SDH, by cysteine resulted in an enzyme sensitive to thiol-specific reagents and protectable by substrate. Other biochemical properties of the redesigned SDH were similar to those of the wild-type enzyme. It is concluded that the invariant cysteine in the flavoprotein of E. coli succinate oxidoreductases corresponds to the active site thiol. However, this cysteine is most likely not essential for succinate oxidation and seemingly lacks an assignable specific function. An invariant arginine in juxtaposition to Ala-252 in the flavoprotein of B. subtilis SDH, and to the invariant cysteine in the E. coli homologous enzymes, is probably essential for substrate binding. | |
650 | 7 | a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe |
650 | 7 | a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng |
650 | 7 | a NATURVETENSKAPx Biologix Mikrobiologi0 (SwePub)106062 hsv//swe |
650 | 7 | a NATURAL SCIENCESx Biological Sciencesx Microbiology0 (SwePub)106062 hsv//eng |
700 | 1 | a Hedén, Lars-Olofu Lund University,Lunds universitet,Molekylär cellbiologi,Biologiska institutionen,Naturvetenskapliga fakulteten,Molecular Cell Biology,Department of Biology,Faculty of Science4 aut0 (Swepub:lu)mikb-loh |
710 | 2 | a Molekylär cellbiologib Biologiska institutionen4 org |
773 | 0 | t Biochemical Journald : Portland Press Ltd.g 260:2, s. 491-497q 260:2<491-497x 0264-6021x 1470-8728 |
856 | 4 | u http://dx.doi.org/10.1042/bj2600491y FULLTEXT |
856 | 4 | u https://europepmc.org/articles/pmc1138695?pdf=render |
856 | 4 8 | u https://lup.lub.lu.se/record/68640c32-f9f3-447e-b006-a0653f22d0b1 |
856 | 4 8 | u https://doi.org/10.1042/bj2600491 |
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