Cloning and characterization of a novel gene encoding L-ribose isomerase from Acinetobacter sp. strain DL-28 in Escherichia coli.
The gene encoding a novel L-ribose isomerase (L-RI) from Acinetobacter sp. was cloned into Escherichia coli and nucleotide sequence was determined. The gene corresponded to an open reading frame of 747 bp that codes for a deduced protein of 249 amino acids, which showed no amino acid sequence similarity with any other sugar isomerases. After expression of the gene in E. coli using pUC118 the recombinant L-RI was purified to homogeneity using different chromatographic methods. The overall enzymatic properties of the purified recombinant L-RI were the same as those of the authentic L-RI. To our knowledge, this is the first time report concerning the L-RI gene.
Mizanur
R M
RM
Department of Biochemistry and Food Science, Faculty of Agriculture, Kagawa University, Ikenobe 2393, Miki-cho, 761-0795, Kagawa, Japan.
Takata
G
G
Izumori
K
K
D000150:Acinetobacter / Q000201:enzymology / Q000235:genetics*; D019747:Aldose-Ketose Isomerases / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D005798:Genes, Bacterial; D008969:Molecular Sequence Data
D019747:Aldose-Ketose Isomerases; C022546:ribose isomerase