A short C-terminal region of alpha-synuclein protects a (R/S)-non-specific esterase from Archaeglobus fulgidus.
We show that alpha-synuclein could assist the molecular activity of a ketoprofen-(R/S) nonspecific esterase from Archaeglobus Fulgidus. Specifically, several synthetic peptides from alpha-synuclein, each having random coil conformation in far-UV spectra, could protect the enzyme activity against stress conditions such as heat and organic solvents.
Kim
Seungbum
S
Department of Biological and Molecular Engineering, College of Engineering, Ajou University, Suwon, South Korea.
Kang
Mira
M
Ryu
Yeonwoo
Y
Kim
T Doohun
TD
D000595:Amino Acid Sequence; D001105:Archaea / Q000187:drug effects / Q000201:enzymology; D043182:Carboxylesterase / Q000037:antagonists & inhibitors* / Q000378:metabolism; D004121:Dimethyl Sulfoxide / Q000494:pharmacology; D004795:Enzyme Stability / Q000187:drug effects; D006358:Hot Temperature; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism*; D012997:Solvents; D051844:alpha-Synuclein / Q000378:metabolism*
D010446:Peptide Fragments; D012997:Solvents; D051844:alpha-Synuclein; D043182:Carboxylesterase; D004121:Dimethyl Sulfoxide