f Thymidine Kinase of Bacteria: Activity of the Enzyme in Actinomycetes and Related Organisms
- Authors: HAJIME SAITO, HARUAKI TOMIOKA
- Microbiology, July 1984 130: 1863-1870, doi: 10.1099/00221287-130-7-1863
- Subject: Systematics
- Published Online:
Various micro-organisms were studied for their thymidine kinase (adenosine 5'-triphosphate: thymidine 5'-phosphotransferase, EC 22.214.171.124) (TK) activity. The sonicated cell extract of Escherichia coli K12 had a TK activity of 35-66 pmol thymidine monophosphate formed min-1 (mg protein)-l. The cell extracts of Salmonella typhimurium and Klebsiella pneumoniae showed a markedly higher (5- to 11-fold) TK activity. Somewhat lower but significant TK activity was detected in the cell extracts of Staphylococcus aureus, Streptococcus pyogenes, Bacillus subtilis and Proteus mzrabilis. In contrast, weak TK activity, if any, was detected in the cell extracts of Pseudomonas aeruginosa. This was also the case with respect to the cell extracts of various actinomycetes (such as Nocardia and Streptomyces) and related organisms (such as Corynebacterium, Mycobacteriurn and Rhodococcus).
© Society for General Microbiology 1984 | Published by the Society for General Microbiology
Full text loading...
Author and Article Information
/content/journal/micro/10.1099/00221287-130-7-1863dcterms_title,dcterms_subject,pub_serialTitlepub_serialIdent:journal/micro AND -contentType:BlogPost64
/content/journal/micro/10.1099/00221287-130-7-1863dcterms_title,dcterms_subject-pub_serialIdent:journal/micro AND -contentType:BlogPost64
Figure data loading....