Complementation of a trpE deletion in Escherichia coli by Spirochaeta aurantia DNA encoding anthranilate synthetase component I activity

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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HO' H /H2 0 \ I dOOH chorismic acid anthranilic acid (Gibson and Gibson, 1964; Somerville, unpublished results).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, an enzyme specified by the tryptophan operon of Escherichia coli: purification and characterization of component I.

A procedure employed in the purification of anthranilate synthetase component I of Escherichia coli is described. The purified component appears homogeneous by starch gel electrophoresis and by sedimentation analysis. A molecular weight of 60,000 was estimated by gel filtration of Sephadex G-100. This value is consistent with the molecular weight estimated from the sedimentation and diffusion c...

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Spirochaeta aurantia has diacetyl chloramphenicol esterase activity.

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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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Chemotaxis mutants of Spirochaeta aurantia.

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ژورنال

عنوان ژورنال: Journal of Bacteriology

سال: 1987

ISSN: 0021-9193,1098-5530

DOI: 10.1128/jb.169.8.3764-3769.1987