title: Characteristics of serine acetyltransferase from Escherichia coli deleting different lengths of amino acid residues from the C-terminus.
abstract: Some properties of serine acetyltransferases (SATs) from Escherichia coli, deleting 10-25 amino acid residues from the C-terminus (SATdeltaC10-deltaC25) were investigated. The specific activity depended only slightly on the length of the C-terminal region deleted. Although the sensitivity of SATdeltaC10 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. SATdeltaC10 was inactivated on cooling to 0 degrees C and dissociated into dimers or trimers in the same manner as the wild-type SAT, but Met-256-le mutant SAT as well as SATdeltaC14, SATdeltaC20, and SATdeltaC25 were stable. Since SATdeltaC10, SATdeltaC14, and SATdeltaC25 did not form a complex with O-acetylserine sulfhydrylase-A (OASS-A) in a way similar to SATdeltaC20, 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.
authors.affiliation: Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Mino
authors.forename: K
authors.initials: K
authors.lastname: Hiraoka
authors.forename: K
authors.initials: K
authors.lastname: Imamura
authors.forename: T
authors.initials: T
authors.lastname: Sakiyama
authors.forename: N
authors.initials: N
authors.lastname: Eisaki
authors.forename: A
authors.initials: A
authors.lastname: Matsuyama
authors.forename: K
authors.initials: K
authors.lastname: Nakanishi
mesh_terms: D000123:Acetyltransferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D017360:Arabidopsis / Q000201:enzymology; D019281:Dimerization; D004748:Entamoeba histolytica / Q000201:enzymology; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D012486:Salmonella typhimurium / Q000201:enzymology; D016415:Sequence Alignment; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid; D051050:Serine O-Acetyltransferase
chemical_list: D046911:Macromolecular Substances; D010446:Peptide Fragments; D011994:Recombinant Proteins; D000123:Acetyltransferases; D051050:Serine O-Acetyltransferase