Thiazole Synthase from Escherichia coli
نویسندگان
چکیده
منابع مشابه
Inhibition by phenylalanine of thiazole biosynthesis in Escherichia coli.
Phenylalanine inhibited thiazole biosynthesis in a thiamine-regulatory mutant of Escherichia coli, and the inhibition was overcome by tyrosine.
متن کاملEffect of glycine on thiazole biosynthesis in Escherichia coli.
Glycine was found to replace thiamine thiazole for the growth of the thiazoleless mutant of Escherichia coli; it also stimulated the production of thiamine thiazole by washed cell suspensions of the mutant.
متن کاملStructure of dihydrouridine synthase C (DusC) from Escherichia coli.
Dihydrouridine (D) is one of the most widely conserved tRNA modifications. Dihydrouridine synthase (Dus) is responsible for introducing D modifications into RNA by the reduction of uridine. Recently, a unique substrate-recognition mechanism using a small adapter molecule has been proposed for Thermus thermophilus Dus (TthDusC). To acquire insight regarding its substrate-recognition mechanism, t...
متن کاملPhylogenetic analysis of Escherichia coli strains isolated from human samples
Escherichia coli (E. coli) is a normal inhabitant of the gastrointestinal tract of vertebrates, including humans. Phylogenetic analysis has shown that E. coli is composed of four main phylogenetic groups (A, B1, B2 and D). Group A and B1 are generally associated with commensals, whereas group B2 is associated with extra-intestinal pathotypes. Most enteropathogenic isolates, however, are assigne...
متن کاملIdentification of phosphate binding residues of Escherichia coli ATP synthase.
Four positively-charged residues, namely betaLys-155, betaArg-182, betaArg-246, and alphaArg-376 have been identified as Pi binding residues in Escherichia coli ATP synthase. They form a triangular Pi binding site in catalytic site betaE where substrate Pi initially binds for ATP synthesis in oxidative phosphorylation. Positive electrostatic charge in the vicinity of betaArg-246 is shown to be ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2007
ISSN: 0021-9258
DOI: 10.1074/jbc.m700782200