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Literature summary for 2.7.13.3 extracted from

  • Purcell, E.B.; McDonald, C.A.; Palfey, B.A.; Crosson, S.
    An analysis of the solution structure and signaling mechanism of LovK, a sensor histidine kinase integrating light and redox signals (2010), Biochemistry, 49, 6761-6770.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.13.3

Cloned(Commentary)

Cloned (Comment) Organism
gene CC_0285, recombinant expression of His-tagged wild-type enzyme, enzyme fragments, and mutant C70A enzyme in Escherichia coli strain Rosetta(DE3)pLysS Caulobacter vibrioides

Protein Variants

Protein Variants Comment Organism
C70A site-directed mutagenesis Caulobacter vibrioides

General Stability

General Stability Organism
photoexcitation destabilizes the LOV-HK linker sequence Caulobacter vibrioides

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + protein L-histidine Caulobacter vibrioides
-
 ADP + protein N-phospho-L-histidine
-
 ?

Organism

Organism UniProt Comment Textmining
Caulobacter vibrioides Q9ABE3
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type enzyme, enzyme fragments, and mutant C70A enzyme from Escherichia coli strain Rosetta(DE3)pLysS by nickel affinity chromatography, ultrafiltration, and gel filtration Caulobacter vibrioides

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + protein L-histidine
-
 Caulobacter vibrioides ADP + protein N-phospho-L-histidine
-
 ?
additional information measurement of the enzyme's ATPase activity Caulobacter vibrioides ?
-
 ?

Subunits

Subunits Comment Organism
More LovK trypsin peptide mapping Caulobacter vibrioides

Synonyms

Synonyms Comment Organism
CC_0285
-
 Caulobacter vibrioides
LovK
-
 Caulobacter vibrioides
sensor histidine kinase
-
 Caulobacter vibrioides

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at room temperature Caulobacter vibrioides

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
 assay at Caulobacter vibrioides

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Caulobacter vibrioides
FMN bound to the LovK histidine kinase Caulobacter vibrioides
additional information no FAD Caulobacter vibrioides

General Information

General Information Comment Organism
additional information effect of the nonconserved flanking sequence on the signaling lifetime of LovK, the effects of structure outside the LOV core on its signaling lifetime do not combine in a simple, additive way. Kinetics of recovery from the adduct state depend not only on the buffer environment but also on the structural context in which the LOV domain is contained. Full-length LovK (residues 1-368) has a long recovery, with a half-life of 2 h, the isolated LOV core (residues 25-138) recovers more quickly, with a half-life of 37 min. LovK (25-163), which contains the LOV core and the nonconserved linker sequence at its C-terminus, has a recovery half-life of 28 min. A construct containing the LOV core and the nonconserved N-terminal flanking sequence, LovK(1-138), has a half-life of only 2 min, but this N-terminal region has not a general rate enhancement effect. LovK(1-163), a construct with fully intact N- and C-termini (but missing the kinase domain), is slower to recover than either LovK(25-138), LovK(1-138), or LovK(25-163) Caulobacter vibrioides