| Autor: |
Høj, Peter Bordier, Slade, Amanda M., Wettenhall, Richard E.H., Fincher, Geoffrey B. |
| Zdroj: |
FEBS Letters; January 1988, Vol. 230 Issue: 1 p67-71, 5p |
| Abstrakt: |
A (1 → 3)-β-glucan 3-glucanohydrolase (EC 3.2.1.39) has been purified approx. 190-fold from extracts of germinating barley. The enzyme has an apparent Mr32 000, a p Iof 8.6, and a pH optimum of 5.6. Analysis of hydrolysis products released from the (1 → 3)-β-glucan, laminarin, shows that the enzyme is an endohydrolase. Sequence analysis of the 46 NH 2-terminal amino acids of the (1 → 3)-β-glucanase reveals 54% positional identity with barley (1 → 3,1 → 4)-β-glucanases (EC 3.2.1.73) and suggests a common evolutionary origin for these two classes of β-glucan endohydrolases. The barley (1 → 3)-β-glucanase also exhibits significant similarity with a (1 → 3)-β-glucanase from tobacco. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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