Purification and Characterization of Serine Acetyltransferase from Escherichia coli Partially Truncated at the C-Terminal Region

概要

論文の詳細を見る
Incubation of serine acetyltransferase (SAT) from Escherichia coli at 25℃ in the absence of protease inhibitors yielded a truncated SAT. The truncated SAT was much less sensitive to feedback inhibition than the wild-type SAT. Analyses of the N-and C-terminal amino acid sequences found that the truncated SAT designated as SAT⊿C20 was a resultant form of the wild-type SAT cleaved between Ser 253 and Met 254,deleting 20 amino acid residues form the C-terminus. Based on these findings, we constructed a plasmid containing an altered cysE gene encoding the truncated SAT. SAT⊿C20 was produced using the cells of E. coli JM70 transformed with the plasmid and purified to be homogeneous on an SDS-polyacrylamide gel. Properties of the purified SAT⊿C20 were investigated in comparison with those of the wild-type SAT and Met-256-Ile mutant SAT, which was isolated by Denk and Bock but not purified (J. Gen. Microbiol., 133,515-525 (1987)). SAT⊿C20 was composed of four identical subunits like the wild-type SAT and Met-256-Ile mutant SAT. Specific activity, optimum pH for reaction, thermal stability, and stability to reagents for SAT⊿C20 were similar to those for the wild-type SAT and Met-256-Ile mutant SAT. However, SAT⊿C20 did not form a complex with O-acetylserine sulfhydrylase-A (OASS-A), a counterpart of the cysteine synthetase and did not reduce OASS activity in contrast to the wild-type SAT and Met-256-Ile mutant SAT.
社団法人日本農芸化学会の論文
1999-01-23

Purification and Characterization of Serine Acetyltransferase from Escherichia coli Partially Truncated at the C-Terminal Region

スポンサーリンク

概要

著者

関連論文

スポンサーリンク