Common amino acid domain among endopolygalacturonases of ascomycete fungi
| Autor: | J. P. R. Keon, G. Waksman |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Glycoside Hydrolases
Molecular Sequence Data Applied Microbiology and Biotechnology Isozyme Ascomycota Species Specificity Sequence Homology Nucleic Acid Amino Acid Sequence Amino Acids Peptide sequence chemistry.chemical_classification Ecology biology Colletotrichum lindemuthianum Isoelectric focusing Immunochemistry Aspergillus niger Sclerotinia sclerotiorum Temperature Hydrogen-Ion Concentration biology.organism_classification Amino acid Molecular Weight Kinetics Polygalacturonase Isoelectric point Biochemistry chemistry Research Article Food Science Biotechnology |
| Zdroj: | Applied and Environmental Microbiology. 56:2522-2528 |
| ISSN: | 1098-5336 0099-2240 |
| DOI: | 10.1128/aem.56.8.2522-2528.1990 |
| Popis: | The endopolygalacturonase (EC 3.2.1.15) enzymes produced in vitro by three ascomycete fungi, Aspergillus niger, Sclerotinia sclerotiorum, and Colletotrichum lindemuthianum were studied by using thin-layer isoelectric focusing and activity stain overlay techniques. The polygalacturonases from A. niger and S. sclerotiorum consisted of numerous isoforms, whereas the endopolygalacturonase from C. lindemuthianum consisted of a single protein species. The most abundant endopolygalacturonase isoform produced by each of these organisms was purified and characterized. Biochemical parameters, including molecular weight, isoelectric point, kinetic parameters, temperature and pH optima, and thermal stability, were determined. Considerable differences in physical and chemical properties were demonstrated among these fungal polygalacturonases. Antibodies raised against individual proteins exhibited little cross-reaction, suggesting that these enzymes differ structurally as well as biochemically. In contrast, the analysis of the N-terminal amino acid sequences of the three proteins showed extensive homology, particularly in a region labeled domain 1 in which 84% of the amino acids were conserved. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|