Proceedings of the Korean Biophysical Society Conference (한국생물물리학회:학술대회논문집)

The Korean Biophysical Society (한국생물물리학회)
권호 표지

PYRANOSE OXIDASE HAVING A COVALENTLY BOUND FAD AS A COENZYME

  • Kwon, Jae-Youl (Laboratory of Biophysics, Department of Microbiology, College of Natural Sciences, and Research Center for Molecular Microbiology, Seoul National University) ;
  • Kang, Sa-Ouk (Laboratory of Biophysics, Department of Microbiology, College of Natural Sciences, and Research Center for Molecular Microbiology, Seoul National University)
  • Published : 1996.07.01
Download PDF
⟨ Previous Next ⟩

Abstract

Flavin-peptides were purified from pyranose oxidase (EC 1.1.3.10) after tryptic- chymotryptic and tryptic digestion. The spectral and chromatographic properties of these flavin peptides showed that the FAD of pyranose oxidase appears to be bound, by way of the 8${\alpha}$-methylene group, to the N-l position of the imidazole ring of the histidine. Automated sequence analysis showed that the amino acid sequence of the tryptic-chymotryptic flavin-peptide from pyranose oxidase is Ser-Thr-X-Trp and that of the tryptic flavin-peptide is Met-Ser-Thr-X-Trp. (omitted)

Keywords