Molecular cloning and expression of an isomalto-dextranase gene from Arthrobacter globiformis T6.
The gene encoding an extracellular isomalto-dextranase, designated imd, was isolated from the chromosomal DNA of Arthrobacter globiformis T6 and cloned and expressed in Escherichia coli. A single open reading frame consisting of 1,926 base pairs that encoded a polypeptide composed of a signal peptide of 39 amino acids and a mature protein of 602 amino acids (M(r), 65,900) was found. The primary structure had no significant homology with the structures of any other reported carbohydrases, including two other dextranases. Transformed E. coli cells carrying the 2.3-kb fragment overproduced isomalto-dextranase into the periplasmic space under control of the promoter of the imd gene itself.
Iwai
A
A
Department of Bioscience and Chemistry, Hokkaido University, Sapporo, Japan.
Ito
H
H
Mizuno
T
T
Mori
H
H
Matsui
H
H
Honma
M
M
Okada
G
G
Chiba
S
S
D000595:Amino Acid Sequence; D001173:Arthrobacter / Q000201:enzymology / Q000235:genetics*; D001483:Base Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D005798:Genes, Bacterial / Q000235:genetics*; D006026:Glycoside Hydrolases / Q000096:biosynthesis / Q000235:genetics* / Q000378:metabolism; D007534:Isomaltose / Q000378:metabolism*; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000096:biosynthesis
D011994:Recombinant Proteins; D007534:Isomaltose; D006026:Glycoside Hydrolases; C091051:glucan 1,6-alpha-isomaltosidase