|
|||||
|
|
Role of glutamate-52 in the mechanism of L-lactate dehydrogenase from Bacillus stearothermophilus |
|
| Authors: | Nevin Gül-Karagüler Richard B. Sessions J. John Holbrook |
| Affiliation: | (1) Present address: Fen-Edebiyat Fakultesi, Moleküler Biyoloji ve Genetik Bölümü, Istanbul Teknik Universitesi, Istanbul, Turkey;(2) Department of Biochemistry, School of Medical Sciences, University Walk, Bristol, BS8 1TD, UK |
| Abstract: | A single residue of the NAD(H)-dependent lactate dehydrogenase (LDH) from Bacillus stearothermophilus has been changed in order to decrease substrate inhibition. The conserved aspartic acid residue at position 52 was replaced by glutamate using site-directed mutagenesis. The effect on substrate inhibition was measured. In the glutamate-52 mutant substrate inhibition is decreased twofold. |
| Keywords: | lactate dehydrogenase substrate inhibition site-directed mutagenesis |
| 本文献已被 SpringerLink 等数据库收录！ | |