Characteristics of Serine Acetyltransferase from Escherichia coli Deleting Different Lengths of Amino Acid Residues from the C-Terminus

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Some properties of serine acetyltransferases (SATs) from Escherichia coli, deleting 10-25 amino acid residues from the C-terminus (SAT⊿C10-⊿C25) were investigated. The specific activity depended only slightly on the length of the C-terminal region deleted. Although the sensitivity of SAT⊿C10 to inhibition by L-cysteine was similar to that for the wild-type SAT, it became less with further increases in the length of the amino acid residues deleted. SAT⊿C10 was inactivated on cooling to 0℃ and dissociated into dimers or trimers in the same manner as the wild-type SAT, but Met-256-Ile mutant SAT as well as SAT⊿C14,SAT⊿C20,and SAT⊿C25 were stable. Since SAT⊿C10,SAT⊿C14,and SAT⊿C25 did not form a complex with O-acetylserine sulfhydrylase-A (OASS-A) in a way similar to SAT⊿C20,it was indicated that 10 amino acid residues or fewer from the C-terminus of the wild-type SAT are responsible for the complex formation with OASS-A. The C-terminal peptide of the 10 amino acid residues interacted competitively with OASS-A with respect to OAS although its affinity was much lower than that for the wild-type SAT.
社団法人日本農芸化学会の論文
2000-09-23