TY - JOUR
T1 - Role of glutamate-52 in the mechanism of L-lactate dehydrogenase from Bacillus stearothermophilus
AU - Gül-Karagüler, Nevin
AU - Sessions, Richard B.
AU - Holbrook, J. John
PY - 2001
Y1 - 2001
N2 - 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.
AB - 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.
KW - Lactate dehydrogenase
KW - Site-directed mutagenesis
KW - Substrate inhibition
UR - https://www.scopus.com/pages/publications/0035120153
U2 - 10.1023/A:1005687723905
DO - 10.1023/A:1005687723905
M3 - Article
AN - SCOPUS:0035120153
SN - 0141-5492
VL - 23
SP - 395
EP - 399
JO - Biotechnology Letters
JF - Biotechnology Letters
IS - 5
ER -