Abstract
The α-L-arabinofuranosidase from Geobacillus stearothermophilus T-6 (AbfA T-6) belongs to the retaining family 51 glycoside hydrolases. The conserved Glu175 was proposed to be the acid-base catalytic residue. AbfA T-6 exhibits residual activity towards aryl β-D-xylopyranosides. This phenomenon was used to examine the catalytic properties of the putative acid-base mutant E175A. Data from kinetic experiments, pH profiles, azide rescue, and the identification of the xylopyranosyl azide product provide firm support to the assignment of Glu175 as the acid-base catalyst of AbfA T-6.
| Original language | English |
|---|---|
| Pages (from-to) | 163-167 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 514 |
| Issue number | 2-3 |
| DOIs | |
| State | Published - 13 Mar 2002 |
Bibliographical note
Funding Information:This study was supported by The Israel Science Foundation (Grant no. 676/00 to G.S. and Y.S.), and by The United States–Israel Binational Science Foundation (BSF) (Grant no. 96-178 to Y.S.), Jerusalem, Israel. Additional support was provided by the Fund for the Promotion of Research at the Technion, and by the Otto Meyerhof Center for Biotechnology, established by the Minerva Foundation (Munich, Germany). V.B. acknowledges the financial support by the Center of Absorption in Science, the Ministry of Immigration Absorption and the Ministry of Science and Arts, Israel (Kamea Program).
Keywords
- Acid-base catalyst
- Aryl β-D-xylopyranoside
- Glycoside hydrolase family 51
- α-L-Arabinofuranosidase
- β-D-Xylopyranosyl azide