Ja. Brannigan et al., Nucleotide sequence, heterologous expression and novel purification of DNAligase from Bacillus stearothermophilus, BBA-PROT ST, 1432(2), 1999, pp. 413-418
Citations number
25
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
The gene for DNA ligase (EC 6.5.1.2) from thermophilic bacterium Bacillus s
tearothermophilus NCA1503 has been cloned and the complete nucleotide seque
nce determined. The ligase gene encodes a protein 670 amino acids in length
. The gene was overexpressed in Escherichia coli and the enzyme has been pu
rified to homogeneity. Preliminary characterisation confirms that it is a t
hermostable, NAD(+)-dependent DNA ligase. (C) 1999 Elsevier Science B.V. Al
l rights reserved.