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Literature DB >> 4891805

Enzymes of tryptophan biosynthesis in Serratia marcescens.

Abstract

In Serratia marcescens, the tryptophan biosynthetic enzymes were formed coordinately. A number of tryptophan auxotrophs showed single biochemical lesions; several mutants showed pleiotropic effects. Sucrose density gradient centrifugation revealed an unique pattern of migration of the tryptophan biosynthetic enzymes. The repression response of the Serratia enzymes to exogenous tryptophan was fivefold more sensitive than that found in Escherichia coli. When this information is contrasted with the available information on the other Enterobacteriaceae, one is compelled to conclude that S. marcescens enjoys a rather marked evolutionary divergence from the other enteric organisms.

Entities: Chemical Species

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Year: 1969 PMID： 4891805 PMCID： PMC249911 DOI： 10.1128/jb.98.1.109-115.1969

Source DB: PubMed Journal: J Bacteriol ISSN： 0021-9193 Impact factor: 3.490

19 in total

1. The tryptophan synthetase system.

Authors: C YANOFSKY
Journal: Bacteriol Rev Date: 1960-06

2. A multifunctional enzyme complex in the tryptophan pathway of Salmonella typhimurium: comparison of polarity and pseudopolarity mutations.

Authors: R H Bauerle; P Margolin
Journal: Cold Spring Harb Symp Quant Biol Date: 1966

3. Characterization of mutants with single and multiple defects in the tryptophan biosynthetic pathway in Bacillus subtilis.

Authors: D D Whitt; B C Carlton
Journal: J Bacteriol Date: 1968-10 Impact factor: 3.490

6. Partial characterization of phosphoribosyl transferase, phosphoribosyl anthranilate isomerase, and indole glycerol phosphate synthase from Serratia marcescens.

Authors: J M Potts; G R Drapeau
Journal: J Bacteriol Date: 1972-08 Impact factor: 3.490

7. Pyrimidine biosynthesis in Serratia marcescens: a possible role for nonsequential enzyme interactions in mimicking coordinate gene expression.

Authors: J R Wild; W L Belser
Journal: Biochem Genet Date: 1977-02 Impact factor: 1.890

Enzymes of tryptophan biosynthesis in Serratia marcescens.

1. The tryptophan synthetase system.

2. A multifunctional enzyme complex in the tryptophan pathway of Salmonella typhimurium: comparison of polarity and pseudopolarity mutations.

3. Characterization of mutants with single and multiple defects in the tryptophan biosynthetic pathway in Bacillus subtilis.

4. Indole-3-glycerol phosphate synthetase of Escherichia coli, an enzyme of the tryptophan operon.

5. Regulation of the enzymes of the tryptophan pathway in Escherichia coli.

6. Association of the alpha and beta-2 subunits of the tryptophan synthetase of Escherichia coli.

7. The natural relationships of Aeromonas formicans.

8. Genetic control of the structure and activity of an enzyme aggregate in the tryptophan pathway of Neurospora crassa.

9. Tryptophan synthetic pathway and its regulation in Chromobacterium violaceum.

10. Enzymes of the tryptophan synthetic pathway in Pseudomonas putida.

1. Mapping of the tryptophan genes of Acinetobacter calcoaceticus by transformation.

2. Enzymes of the tryptophan pathway in Acinetobacter calco-aceticus.

Review 3. Gene rearrangements in the evolution of the tryptophan synthetic pathway.

4. Tryptophan operon regulation in interspecific hybrids of enteric bacteria.

5. Tryptophan biosynthetic pathway in the Enterobacteriaceae: some physical properties of the enzymes.

6. Partial characterization of phosphoribosyl transferase, phosphoribosyl anthranilate isomerase, and indole glycerol phosphate synthase from Serratia marcescens.

7. Pyrimidine biosynthesis in Serratia marcescens: a possible role for nonsequential enzyme interactions in mimicking coordinate gene expression.

8. Anthranilate synthase forms in plants and cultured cells of Nicotiana tabacum L.

9. Tryptophan biosynthetic enzymes of Staphylococcus aureus.

10. Regulation of a ligand-mediated association-dissociation system of anthranilate synthesis in Clostridium butyricum.