Unique primary structure of a thermostable multimetal β-galactosidase from Saccharopolyspora rectivirgula

Misa Inohara-Ochiai, Toru Nakayama, Masahiro Nakao, Tsuyoshi Fujita, Takashi Ueda, Toshihiko Ashikari, Tokuzo Nishino, Yuji Shibano

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

The gene of the monomeric multimetal β-galactosidase of Saccharopolyspora rectivirgula was cloned and sequenced. Although the enzyme could be assigned as a member of β-galactosidases belonging to the glycosyl hydrolase family 2, it has unusual structural features for β-galactosidase of this family; it contained a unique sequence which consists of approximately 200 amino acid residues with no similarity to known proteins. This 200-residue sequence exists as if it is inserted into a sequence homologous to the active-site domain of the Escherichia coli lacZ enzyme. Copyright (C) 1998 Elsevier Science B.V.

Original languageEnglish
Pages (from-to)77-83
Number of pages7
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1388
Issue number1
DOIs
Publication statusPublished - 1998 Oct 14

Keywords

  • Saccharopolyspora rectivirgula
  • β-Galactosidase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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