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Literature summary for 2.7.1.189 extracted from

  • Xavier, K.B.; Bassler, B.L.
    Regulation of uptake and processing of the quorum-sensing autoinducer AI-2 in Escherichia coli (2005), J. Bacteriol., 187, 238-248.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.1.189

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + autoinducer-2 Escherichia coli i.e. AI-2 ADP + phosphorylated autoinducer-2
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 MG1655, gene lsrK
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + autoinducer-2 i.e. AI-2 Escherichia coli ADP + phosphorylated autoinducer-2
-
 ?

Synonyms

Synonyms Comment Organism
AI-2 kinase
-
 Escherichia coli
lsrK
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli

Expression

Organism Comment Expression
Escherichia coli glycerol-3-phosphate inhibits lsr operon transcription activation by cAMP-catabolite activator protein, CAP. Dihydroxyacetone phosphate represses lsr transcription by a cAMP-CAP-independent mechanism involving LsrR, the lsr operon repressor, dihydroxyacetone phosphate causes repression by an LsrR-dependent and catabolite repression-independent route down
Escherichia coli cAMP-catabolite activator protein (CAP)-dependent activation of the lsr transcription. A cAMP-CAP-independent mechanism of lsr activation involves LsrR, the lsr operon repressor up

General Information

General Information Comment Organism
malfunction unlike the wild-type, the lsrK mutant does not activate transcription of the lsr operon in response to AI-2. The lsrK mutant fails to activate lsr expression because it cannot produce phospho-AI-2, which is the lsr operon inducer. Specifically, in an lsrK mutant, any AI-2 internalized by a secondary transporter does not get phosphorylated, and cannot be sequestered. In an lsrR/lsrK double mutant extracellular AI-2 accumulates to wild-type levels Escherichia coli
physiological function the enzyme is repsonsible for the regulation of uptake and processing of the quorum-sensing autoinducer AI-2 in Escherichia coli, overview. Enzyme LsrK and the Lsr transporter are required for AI-2 internalization and processing in Escherichia coli Escherichia coli