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

Koshiki Mino, Kenji Hiraoka, Koreyoshi Imamura, Takaharu Sakiyama, Naoki Eisaki, Asahi Matsuyama, Kazuhiro Nakanishi

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

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, SAT/ΔC14, 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.

Original languageEnglish
Pages (from-to)1874-1880
Number of pages7
JournalBioscience, Biotechnology and Biochemistry
Volume64
Issue number9
Publication statusPublished - 2000

Fingerprint

Serine O-Acetyltransferase
serine O-acetyltransferase
Escherichia coli
Amino acids
Amino Acids
amino acids
Cysteine Synthase
Dimers
Peptides
Cooling
Cysteine
cysteine
cooling
peptides
mutants

Keywords

  • C-terminal region
  • Cold inactivation
  • Cysteine synthetase
  • O-acetylserine sulfhydrylase
  • Serine acetyltransferase

ASJC Scopus subject areas

  • Food Science
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biotechnology
  • Chemistry (miscellaneous)
  • Applied Microbiology and Biotechnology
  • Bioengineering

Cite this

Characteristics of Serine Acetyltransferase from Escherichia coli Deleting Different Lengths of Amino Acid Residues from the C-Terminus. / Mino, Koshiki; Hiraoka, Kenji; Imamura, Koreyoshi; Sakiyama, Takaharu; Eisaki, Naoki; Matsuyama, Asahi; Nakanishi, Kazuhiro.

In: Bioscience, Biotechnology and Biochemistry, Vol. 64, No. 9, 2000, p. 1874-1880.

Research output: Contribution to journalArticle

Mino, Koshiki ; Hiraoka, Kenji ; Imamura, Koreyoshi ; Sakiyama, Takaharu ; Eisaki, Naoki ; Matsuyama, Asahi ; Nakanishi, Kazuhiro. / Characteristics of Serine Acetyltransferase from Escherichia coli Deleting Different Lengths of Amino Acid Residues from the C-Terminus. In: Bioscience, Biotechnology and Biochemistry. 2000 ; Vol. 64, No. 9. pp. 1874-1880.
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