作者: Xinxin Zhang , Dongsheng Wei , Mingchun Li , Yuyan Qi , Laijun Xing
DOI: 10.1007/S11033-008-9215-6
关键词: Biochemistry 、 Biology 、 Regioselectivity 、 Amino acid 、 Enzyme 、 Pichia pastoris 、 Fatty acid desaturase 、 Sequence alignment 、 Peptide sequence 、 Site-directed mutagenesis 、 Genetics 、 Molecular biology 、 General Medicine
摘要: ω3-fatty acid desaturase and Δ12-fatty of Pichia pastoris with distinguishable regioselectivity high degree sequence similarity were chosen for research. Chimeras constructed in which Histidine-rich boxes 1, 2 the carboxyl terminal region replaced corresponding desaturase. The replacement was found to result a change from ωy x + 3 by functionally characterizing these chimeric enzymes Saccharomyces cerevisae strain INVScI. Using site-directed mutagenesis, we further demonstrated that seven conserved amino acids within first two regions are responsible switch. Therefore, fatty desaturases may be better understood investigating evolutionary relationships different desaturases.