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

BRENDA support

Literature summary for 5.4.3.2 extracted from

  • Zhang, Z.; Yang, M.; Peng, Q.; Wang, G.; Zheng, Q.; Zhang, J.; Song, F.
    Transcription of the lysine-2,3-aminomutase gene in the kam locus of Bacillus thuringiensis subsp. kurstaki HD73 is controlled by both sigma54 and sigmaK factors (2014), J. Bacteriol., 196, 2934-2943 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene kamA, DNA and amino acid sequence determination and analysis, sequence analysis of the kam locus, genetic organization, the kam locus forms two operons: yodT (yodT-yodS-yodR-yodQ-yodPkamR) and kamA (kamA-yokU-yozE). The transcriptional start sites (TSSs) of the kamA gene were determined using 5' rapid amplification of cDNA ends (RACE). A typical -12/-24 sigma54 binding site is identified in the promoter PkamA, which is located upstream of the kamA gene TSS. PkamA, which directs the transcription of the kamA operon, is controlled by the sigma54 factor and is activated through the sigma54-dependent transcriptional regulator KamR. The kamA operon is also controlled by sigmaK and regulated by the GerE protein in the late stage of sporulation Bacillus thuringiensis serovar kurstaki

Protein Variants

Protein Variants Comment Organism
additional information generation of kamR and kamA mutants by homologous recombination to examine the role of the kam locus. The results show that the sporulation rate in Bacillus thuringiensis mutant strain HD (DELTAkamR) is slightly decreased compared to that in wild-type strain HD73, whereas that in strain HD (DELTAkamA) it is similar to that in strain HD73. Other genes regulated by KamR are important for sporulation. Construction of yodT and kamA promoter fusions with lacZ Bacillus thuringiensis serovar kurstaki

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-lysine Bacillus thuringiensis serovar kurstaki
-
L-beta-lysine
-
r
L-lysine Bacillus thuringiensis serovar kurstaki HD73
-
L-beta-lysine
-
r

Organism

Organism UniProt Comment Textmining
Bacillus thuringiensis serovar kurstaki A0A0K0QCW0
-
-
Bacillus thuringiensis serovar kurstaki HD73 A0A0K0QCW0
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lysine
-
Bacillus thuringiensis serovar kurstaki L-beta-lysine
-
r
L-lysine
-
Bacillus thuringiensis serovar kurstaki HD73 L-beta-lysine
-
r

Synonyms

Synonyms Comment Organism
AblA
-
Bacillus thuringiensis serovar kurstaki
HD73_2540 locus name Bacillus thuringiensis serovar kurstaki
KAM
-
Bacillus thuringiensis serovar kurstaki
kamA
-
Bacillus thuringiensis serovar kurstaki
lysine-2,3-aminomutase
-
Bacillus thuringiensis serovar kurstaki

General Information

General Information Comment Organism
metabolism L-lysine is first converted to L-beta-lysine by a lysine-2,3-aminomutase in the lysine degradation pathway, and this intermediate is then acetylated to Nepsilon-acetyl-beta-lysine by the action of an acetyltransferase. The L-lysine degradation pathway in strain HD73, overview Bacillus thuringiensis serovar kurstaki
physiological function lysine 2,3-aminomutase catalyzes the interconversion of L-lysine and L-beta-lysine. Analysis of the transcription and regulation of the kam locus, including lysine-2,3-aminomutase-encoding genes, in Bacillus thuringiensis, overview. Transcription of the lysine-2,3-aminomutase gene in the kam locus of Bacillus thuringiensis subsp. kurstaki strain HD73 is controlled by both sigma54 and sigmaK factors Bacillus thuringiensis serovar kurstaki