Purification and properties of aromatic amino acid aminotransferase from Klebsiella aerogenes
| Autor: | B Magasanik, C G Paris |
|---|---|
| Rok vydání: | 1981 |
| Předmět: |
Phenylalanine
Enterobacter aerogenes medicine.disease_cause Microbiology chemistry.chemical_compound Aromatic amino acids medicine Amino Acids Molecular Biology Gene Escherichia coli Transaminases chemistry.chemical_classification Aromatic-amino-acid aminotransferase biology Temperature Tryptophan Hydrogen-Ion Concentration biology.organism_classification Molecular Weight Kinetics Klebsiella pneumoniae Enzyme chemistry Biochemistry Research Article |
| Zdroj: | Journal of Bacteriology. 145:266-271 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.145.1.266-271.1981 |
| Popis: | We describe the complete purification of aromatic aminotransferase I, the enzyme responsible for the ability of Klebsiella aerogenes to use tryptophan and phenylalanine as sole sources of nitrogen, as well as the partial purification of aromatic aminotransferase IV. An examination of the properties of these enzymes revealed that aminotransferase I had much greater affinity for the aromatic amino acids than aminotransferase IV, explaining the essential role of aminotransferase I in the utilization of exogenously supplied aromatic amino acids. The properties of aminotransferase IV suggest that this enzyme is actually an aspartate aminotransferase (EC 2.6.1.1), corresponding to the product of the aspC gene of Escherichia coli. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|