Characteristics of serine acetyltransferase from Escherichia coli deleting different lengths of amino acid residues from the C-terminus

• Published in: Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2000-09, Vol.64 (9), p.1874-1880
• Main Authors: Mino, K. (Okayama Univ. (Japan)), Hiraoka, K, Imamura, K, Sakiyama, T, Eisaki, N, Matsuyama, A, Nakanishi, K
• Format: Article
• Language: English
• Subjects: Acetyltransferases - chemistry; Acetyltransferases - genetics; Acetyltransferases - metabolism; Amino Acid Sequence; AMINO ACIDS; Analytical, structural and metabolic biochemistry; Animals; Arabidopsis - enzymology; Biological and medical sciences; C-terminal region; cold inactivation; CYSTEINE; cysteine synthetase; Dimerization; Entamoeba histolytica - enzymology; Enzymes and enzyme inhibitors; ENZYMIC ACTIVITY; ESCHERICHIA COLI; Escherichia coli - enzymology; Fundamental and applied biological sciences. Psychology; Kinetics; LIGASES; Macromolecular Substances; Molecular Sequence Data; NUCLEOTIDE SEQUENCE; O-acetylserine sulfhydrylase; Peptide Fragments - chemistry; Recombinant Proteins - chemistry; Recombinant Proteins - isolation & purification; Recombinant Proteins - metabolism; Salmonella typhimurium - enzymology; Sequence Alignment; Sequence Deletion; Sequence Homology, Amino Acid; SERINE; serine acetyltransferase; Serine O-Acetyltransferase; TRANSFERASES
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1271/bbb.64.1874

Some properties of serine acetyltransferases (SATs) from Escherichia coli, deleting 10-25 amino acid residues from the C-terminus (SATΔC10-ΔC25) were investigated. The specific activity depended only slightly on the length of the C-terminal region deleted. Although the sensitivity of SATΔC10 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. SATΔC10 was inactivated on cooling to 0°C and dissociated into dimers or trimers in the same manner as the wild-type SAT, but Met-256-Ile mutant SAT as well as SATΔC14, SATΔC20, and SATΔC25 were stable. Since SATΔC10, SATΔC14, and SATΔC25 did not form a complex with O-acetylserine sulfhydrylase-A (OASS-A) in a way similar to SATΔC20, 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.