Unique primary structure of a thermostable multimetal beta-galactosidase from Saccharopolyspora rectivirgula.
The gene of the monomeric multimetal beta-galactosidase of Saccharopolyspora rectivirgula was cloned and sequenced. Although the enzyme could be assigned as a member of beta-galactosidases belonging to the glycosyl hydrolase family 2, it has unusual structural features for beta-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.
Suntory Research Center, 1-1-1 Wakayamadai, Shimamoto-cho, Mishima-gun, Osaka 618-8503, Japan. misa_ochiai@suntory.co.jp
M
M
Inohara-Ochiai
T
T
Nakayama
M
M
Nakao
T
T
Fujita
T
T
Ueda
T
T
Ashikari
T
T
Nishino
Y
Y
Shibano
D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D008670:Metals / Q000378:metabolism; D008969:Molecular Sequence Data; D016930:Saccharopolyspora / Q000201:enzymology*; D001616:beta-Galactosidase / Q000235:genetics* / Q000378:metabolism
D008670:Metals; D001616:beta-Galactosidase