Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.13.3 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

Application Comment Organism
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)

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

Inhibitors

Inhibitors Comment Organism Structure
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

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-
Mycobacterium tuberculosis H37Rv
-
-
-

Purification (Commentary)

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

Synonyms

Synonyms Comment Organism
histidine kinase
-
Mycobacterium tuberculosis
HK1
-
Mycobacterium tuberculosis
HK2
-
Mycobacterium tuberculosis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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
60
-
HK1 relatively stable up to 60°C, gets completely denatured at 90°C Mycobacterium tuberculosis