No evidence of covalent modification of glutamine synthetase in the thermophilic phototropic bacterium Chloroflexus aurantiacus
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منابع مشابه
A cambialistic superoxide dismutase in the thermophilic photosynthetic bacterium Chloroflexus aurantiacus.
Superoxide dismutase from the thermophilic anoxygenic photosynthetic bacterium Chloroflexus aurantiacus was cloned, purified, and characterized. This protein is in the manganese- and iron-containing family of superoxide dismutases and is able to use both manganese and iron catalytically. This appears to be the only soluble superoxide dismutase in C. aurantiacus. Iron and manganese cofactors wer...
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Enolase catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate during both glycolysis and gluconeogenesis, and is required by all three domains of life. Here, we report the purification and biochemical and structural characterization of enolase from Chloroflexus aurantiacus, a thermophilic anoxygenic phototroph affiliated with the green non-sulfur bacteria. The protein was purifi...
متن کاملOxidative Modification of Glutamine Synthetase
The first step in the proteolytic degradation of bacterial glutamine synthetase is a mixed function oxidation of one of the 16 histidine residues in the glutamine synthetase subunit (Levine, R. L. (1983) J. Biol. Chem. 258, 11823-11827). A model system, consisting of oxygen, a metal ion, and ascorbic acid, mimics the bacterial system in mediating the oxidative modification of glutamine syntheta...
متن کاملBiosynthetic controls on the 13C contents of organic components in the photoautotrophic bacterium Chloroflexus aurantiacus.
To assess the effects related to known and proposed biosynthetic pathways on the (13)C content of lipids and storage products of the photoautotrophic bacterium Chloroflexus aurantiacus, the isotopic compositions of bulk cell material, alkyl and isoprenoid lipids, and storage products such as glycogen and polyhydroxyalkanoic acids have been investigated. The bulk cell material was 13 per thousan...
متن کاملMutations that alter the covalent modification of glutamine synthetase in Salmonella typhimurium.
glnD and glnE mutant strains of Salmonella typhimurium lack three of the four activities required for reversible covalent modification of glutamine synthetase (GS; EC 6.3.1.2). The glnD strains, which are unable to deadenylylate GS and therefore accumulate the adenylylated or less active form of the enzyme, were isolated as glutamine bradytrophs. They lack the activity of PIIA uridylyl-transfer...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 1983
ISSN: 0378-1097
DOI: 10.1016/0378-1097(83)90171-4