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Literature summary extracted from

  • Shrivastava, R.; Das, A.K.
    Temperature and urea induced conformational changes of the histidine kinases from Mycobacterium tuberculosis (2007), Int. J. Biol. Macromol., 41, 154-161.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.7.13.3 additional information great effect of temperature on the dynamics of the HAMP linker domain, which is a key feature in signal transduction Mycobacterium tuberculosis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.13.3 into pQE30 and overexpressed in Escherichia coli M15 Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.13.3 additional information thermal transition of HK1 is a two-state process and that of HK2 is a three-state process. Urea denaturation of HK1 and HK2 is a three-state and two-state process, respectively Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
2.7.13.3 Mycobacterium tuberculosis
-
-
-
2.7.13.3 Mycobacterium tuberculosis H37Rv
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.13.3 by Ni-NTA column and gel filtration Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
2.7.13.3 histidine kinase
-
Mycobacterium tuberculosis
2.7.13.3 HK1
-
Mycobacterium tuberculosis
2.7.13.3 HK2
-
Mycobacterium tuberculosis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.13.3 40
-
HK2 is stable up to 40°C and reaches an intermediate state at 60°C. On raising the temperature to 100°C, the second stage of denaturation is observed Mycobacterium tuberculosis
2.7.13.3 60
-
HK1 relatively stable up to 60°C, gets completely denatured at 90°C Mycobacterium tuberculosis