The Specificity of Enzymes Adding Amino Acids in the Synthesis of the Peptidoglycan Precursors of Corynebacterium poinsettiae and Corynebacterium insidiosum
| Autor: | Anne W. Wyke, H. R. Perkins |
|---|---|
| Rok vydání: | 1975 |
| Předmět: |
Peptide Biosynthesis
Glycine Corynebacterium Peptide Peptidoglycan Cell Fractionation Diaminopimelic Acid Tritium Microbiology chemistry.chemical_compound Glutamates Homoserine Nucleotide Carbon Radioisotopes Peptide Synthases Protein Precursors chemistry.chemical_classification Alanine Dipeptide Cell-Free System biology Lysine Succinates biology.organism_classification Aldehyde Oxidoreductases Amino acid Butyrates Enzyme chemistry Biochemistry Acetylation |
| Zdroj: | Journal of General Microbiology. 88:159-168 |
| ISSN: | 0022-1287 |
| DOI: | 10.1099/00221287-88-1-159 |
| Popis: | SUMMARY: A soluble extract from Corynebacterium poinsettiae able to synthesize the nucleotide precursor of its peptidoglycan was prepared. This extract contained all the enzymes necessary for the synthesis of the peptide side-chain. The specificity of these enzymes was determined and compared with the specificity of similar enzymes extracted from the closely related Corynebacterium insidiosum. In both organisms, addition of the third amino acid of the peptide side-chain was specific for the amino acid and nucleotide dipeptide involved in peptidoglycan synthesis in the parent organism. L-Diaminobutyric acid, which is found as the acetyl derivative in the precursor nucleotide and in the completed peptidoglycan of C. insidiosum, was added as the free amino acid and not as the acetylated compound. |
| Databáze: | OpenAIRE |
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