Open AccessCloning and sequence analysis of thymidine kinase from the oral bacterium Streptococcus gordonii
Author(s) -
McNab Roderick
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb07973.x
Subject(s) - thymidine kinase , thymidine , biochemistry , biology , microbiology and biotechnology , escherichia coli , kinase , peptide sequence , nucleotide salvage , gene , nucleotide , dna , genetics , virus , herpes simplex virus
Thymidine kinase is an important enzyme in the pyrimidine nucleotide salvage pathway and catalyzes the formation of thymidylate from thymidine using ATP as a phosphate donor. The gene encoding thymidine kinase of the oral bacterium Streptococcus gordonii was cloned and the nucleptide sequence determined. The inferred amino acid sequence of thymidine kinase (191 amino acids) exhibited 43% identity with type H thymidine kinase from Escherichia coli . The S. gordonii thymidine kinase expressed in Escherichia coli KY895 ( tdk − ) was inhibited by thymidline triphosphate, a feature typical of type II thymidine kinases. Immediately 3′ to the tdk gene, and possibly co‐transcribed with it, was the gene encoding release factor 1 ( prfA ).