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| Content Provider | Springer Nature Link |
|---|---|
| Author | Rojo, Liliana García Carreño, Fernando Angeles Navarrete del Toro, Maria |
| Copyright Year | 2012 |
| Abstract | Aspartic proteinases in the gastric fluid of clawed lobsters Homarus americanus and Homarus gammarus were isolated to homogeneity by single-step pepstatin-A affinity chromatography; such enzymes have been previously identified as cathepsin D-like enzymes based on their deduced amino acid sequence. Here, we describe their biochemical characteristics; the properties of the lobster enzymes were compared with those of its homolog, bovine cathepsin D, and found to be unique in a number of ways. The lobster enzymes demonstrated hydrolytic activity against synthetic and natural substrates at a wider range of pH; they were more temperature-sensitive, showed no changes in the K M value at 4°C, 10°C, and 25°C, and had 20-fold higher k cat /K M values than bovine enzyme. The bovine enzyme was temperature-dependent. We propose that both properties arose from an increase in molecular flexibility required to compensate for the reduction of reaction rates at low habitat temperatures. This is supported by the fast denaturation rates induced by temperature. |
| Starting Page | 87 |
| Ending Page | 96 |
| Page Count | 10 |
| File Format | |
| ISSN | 14362228 |
| Journal | Marine Biotechnology |
| Volume Number | 15 |
| Issue Number | 1 |
| e-ISSN | 14362236 |
| Language | English |
| Publisher | Springer-Verlag |
| Publisher Date | 2012-05-31 |
| Publisher Place | New York |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Lobster Aspartic proteinase Cathepsin D Enzyme kinetics Freshwater & Marine Ecology Microbiology Zoology Engineering |
| Content Type | Text |
| Resource Type | Article |
| Subject | Aquatic Science Biotechnology |
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