Purification, Subunit Structure and Partial Amino-Acid Sequence of Anthranilate-5-phosphoribosylpyrophosphate Phosphoribosyltransferase from the Enteric Bacterium Serratia marcescens
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1976.tb10628.x/fullpdf
Reference22 articles.
1. Tryptophan biosynthetic pathway in the Enterobacteriaceae: some physical properties of the enzymes
2. Anthranilate Synthetase, an Enzyme Specified by the Tryptophan Operon of Escherichia coli : Comparative Studies on the Complex and the Subunits
3. A Multifunctional Enzyme Complex in the Tryptophan Pathway of Salmonella typhimurium: Comparison of Polarity and Pseudopolarity Mutations
4. Tryptophan biosynthetic pathway in the Enterobacteriaceae: some physical properties of the enzymes
5. On the Composition of Anthranilate Synthetase-Anthranilate 5-Phosphoribosylpyrophosphate Phosphoribosyltransferase from Salmonella typhimurium
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1. Anthranilate phosphoribosyltransferase from the hyperthermophilic archaeonThermococcus kodakarensisshows maximum activity with zinc and forms a unique dimeric structure;FEBS Open Bio;2017-07-24
2. Multifunctional Tryptophan-synthesizing Enzyme;Journal of Biological Chemistry;1997-04
3. Anthranilate phosphoribosyltransferase;Enzyme Handbook 12;1996
4. Anthranilate synthase in microorganisms and plants;Phytochemistry;1995-05
5. Structural Features of the Phosphoribosyl-Transferases and Their Relationship to the Human Deficiency Disorders of Purine and Pyrimidine Metabolis;Critical Reviews in Biochemistry;1981-01
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