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.
|Number of pages
|Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
|Published - 1998 Oct 14
- Saccharopolyspora rectivirgula