Isolation and characterization of two tryptophan biosynthetic enzymes, indoleglycerol phosphate synthase and phosphoribosyl anthranilate isomerase, from Bacillus subtilis
| Autor: | S O Hoch |
|---|---|
| Rok vydání: | 1979 |
| Předmět: |
Glycerol
Sucrose Carboxy-lyases Carboxy-Lyases Indole-3-Glycerol-Phosphate Synthase Isomerase Bacillus subtilis Microbiology ortho-Aminobenzoates Isomerases Molecular Biology Gel electrophoresis chemistry.chemical_classification ATP synthase biology Tryptophan biology.organism_classification Molecular biology Molecular Weight Kinetics Enzyme chemistry Biochemistry biology.protein Ribosemonophosphates Research Article |
| Zdroj: | Journal of Bacteriology. 139:362-368 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.139.2.362-368.1979 |
| Popis: | Two of the enzymes responsible for tryptophan biosynthesis in Bacillus subtilis have been extensively purified. These proteins are indole-3-glycerol phosphate synthase and N-(5'-phosphoribosyl) anthranilate isomerase. By comparison to the non-differentiating enteric bacteria in which these two enzymes are fused into a single polypeptide, the isolation of the indoleglycerol phosphate synthase and phosphoribosyl anthranilate isomerase from B. subtilis has demonstrated that the two proteins are separate species in this organism. The two enzymes were clearly separable by anion-exchange chromatography without any significant loss of activity. Molecular weights were determined for both enzymes by gel filtration and sodium dodecyl sulfate-slab gel electrophoresis, and indicated that the indoleglycerol phosphate synthase is the slightly larger of the two proteins. The minimum molecular weight for indoleglycerol phosphate synthase was 23,500, and that for phosphoribosyl anthranilate isomerase was 21,800. Both enzymes have been examined as to conditions necessary to achieve maximal activity of their individual functions and to maintain that activity. |
| Databáze: | OpenAIRE |
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