Hydroxamate formation by anthranilate synthetase of Escherichia coli K12

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Hydroxamate formation by anthranilate synthetase of Escherichia coli K12.

HO' H /H2 0 \ I dOOH chorismic acid anthranilic acid (Gibson and Gibson, 1964; Somerville, unpublished results). In Escherichia coli the catalytically active species is a protein complex formed by aggregation of the products of the E and D genes of the tryptophan operon (Ito and Yanofsky, 1966). Anthranilate synthetase is one of a class of amidotransferase enzymes where L-glutamine serves as th...

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Anthranilate Synthetase From Escherichia coli SJHI: Purification and Some Properties

Abstract: A procedure employed in the purification of anthranilate synhetase of Escherichia coli SJHI is described. The purified anthranilate synthetase appeared to be homogeneous when examined with poliacrylamide gel electrophoresis. Phenly-sepharose CL-4B and Blue dye sepharose were used for purification. A positive correlation was found between purification and ammonium sulfate especially us...

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Nucleotide sequence of the purM gene encoding 5'-phosphoribosyl-5-aminoimidazole synthetase of Escherichia coli K12.

5'-Phosphoribosyl-5-aminoimidazole synthetase (EC 6.3.3.1), encoded by the purM gene of Escherichia coli, catalyzes the synthesis of 5'-phosphoribosyl-5-aminoimidazole from 5'-phosphoribosylformylglycinamidine. The purM gene was subcloned from the Clarke and Carbon (Clarke, L., and Carbon, J. (1976) Cell 9, 91-99) plasmid pLC1-41 and the nucleotide sequence determined. The mature protein, as de...

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Nucleotide sequence and analysis of the purA gene encoding adenylosuccinate synthetase of Escherichia coli K12.

Adenylosuccinate synthetase (EC 6.3.4.4), encoded by the purA gene of Escherichia coli K12, catalyzes the synthesis of adenylosuccinate (SAMP) from IMP, the first committed step in AMP biosynthesis. The E. coli K12 purA gene and flanking DNA was cloned by miniMu-mediated transduction, and the nucleotide sequence was determined. The mature SAMP synthetase subunit, as deduced from the DNA sequenc...

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Anthranilate synthetase. Partial purification and some kinetic studies on the enzyme from Escherichia coli.

Anthranilate synthetase was purified by ammonium sulfate precipitation and gel filtration from extracts of an episomebearing Escherichia coli mutant grown under conditions of tryptophan pathway derepression. This purification represented an l&fold increase in specific activity over the activity of the derepressedmutant extract. Starch gel electrophoresis and ultracentrifugation revealed only sl...

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ژورنال

عنوان ژورنال: Biochemical and Biophysical Research Communications

سال: 1967

ISSN: 0006-291X

DOI: 10.1016/0006-291x(67)90331-2