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Literature summary for 2.7.13.3 extracted from

  • Shrivastava, R.; Ghosh, A.K.; Das, A.K.
    Probing the nucleotide binding and phosphorylation by the histidine kinase of a novel three-protein two-component system from Mycobacterium tuberculosis (2007), FEBS Lett., 581, 1903-1909.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.75
-
ATP HK1 Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required for HK1 activity Mycobacterium tuberculosis

Organism

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

Purification (Commentary)

Purification (Comment) Organism
by Ni-NTA affinity column, HK1 purified to homogeneity Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + histidine kinase HK2
-
Mycobacterium tuberculosis ADP + histidine kinase HK2 N-phospho-L-histidine
-
?
ATP + histidine kinase HK2
-
Mycobacterium tuberculosis H37Rv ADP + histidine kinase HK2 N-phospho-L-histidine
-
?
additional information neither HK1 nor HK2 is able to autophosphorylate itself, HK1 is an ATP binding protein, acts as a functional kinase and phosphorylates HK2 by interacting with it, transfer of a phosphoryl group from HK2 to the response regulator TcrA Mycobacterium tuberculosis ?
-
?
additional information neither HK1 nor HK2 is able to autophosphorylate itself, HK1 is an ATP binding protein, acts as a functional kinase and phosphorylates HK2 by interacting with it, transfer of a phosphoryl group from HK2 to the response regulator TcrA Mycobacterium tuberculosis H37Rv ?
-
?

Synonyms

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