Comparative specificities of trehalases from various species
| Autor: | F C Baumann, E Bar-Guilloux, D Robic, J Labat-Robert |
|---|---|
| Rok vydání: | 1978 |
| Předmět: |
Physiology
Stereochemistry Swine Alpha (ethology) Substrate (chemistry) Pseudomonas fluorescens General Medicine Primary alcohol Biology biology.organism_classification Biochemistry Substrate Specificity carbohydrates (lipids) Coleoptera Residue (chemistry) Species Specificity Substrate specificity Animals Humans Trehalase Beta (finance) Molecular Biology |
| Zdroj: | Comparative biochemistry and physiology. B, Comparative biochemistry. 61(1) |
| ISSN: | 0305-0491 |
| Popis: | 1. Using derivatives or non-symmetrical analogs of alpha,alpha-trehalose, we studied the catalytic specificities of trehalases from various species: Pseudomonas fluorescens, Melolontha vulgaris, porcine and human kidneys. 2. alpha,Beta-trehalose, beta,beta-trehalose, 6,6'dideoxy alpha,alpha-trehalose, alpha-D-xylopyranosyl alpha-D-xylopyranoside were shown to be neither substrates nor inhibitors. 3. 6'deoxy alpha,alpha-trehalose, alpha-D-glucopyranosyl alpha-D-xylopyranoside, alpha-D-allopyranosyl alpha-D-glucopyranoside and alpha-D-galactosyl alpha-D-glucopyranoside, which all possess an intact alpha-D-glucopyranosyl residue, were split by all these trehalases. 4. alpha-D-glucopyranosyl alpha-D-mannopyranoside, alpha,alpha-trehalosamine are competitive inhibitors. 5. These results show the importance of the primary alcohol group at C-6, of the equatorial configuration of the OH groups at C-2, C-3 and C-4 and of the modification of the structure at C-2 of the substrate for the catalytic activity. |
| Databáze: | OpenAIRE |
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