EC Number   |
General Information |
Reference |
|---|
    5.4.3.2 | evolution |
lysine 2,3-aminomutase (LAM) is a member of the radical S-adenosyl-L-methionine (SAM) enzyme superfamily whose reactions are initiated by radical-generating machinery comprising SAM anchored to the unique Fe of a [4Fe-4S] cluster via a classical five-membered N,O chelate ring formed by the methionine |
-, 748031 |
| 5.4.3.2 | evolution |
the iron-binding motif in LAM, CxxxCxxC, found in four other SAM-dependent enzymes, is the founding motif for the radical SAM superfamily. This superfamily provides the chemical context from which the much more structurally complex adenosylcobalamin evolved |
-, 746571 |
| 5.4.3.2 | malfunction |
DELTAabl mutants of Methanococcus maripaludis no longer produced Nepsilon-acetyl-beta-lysine and are incapable of growth at high salt concentrations, indicating that the abl operon is essential for Nepsilon-acetyl-beta-lysine synthesis |
-, 657591 |
| 5.4.3.2 | 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 |
-, 748088 |
| 5.4.3.2 | more |
S-adenosyl-L-methionine is an evolutionary predecessor to adenosylcobalamin. The 5'-deoxyadenosyl of S-adenosyl-L-methionine mediates hydrogen transfer by enzyme LAM exactly as in adenosylcobalamin mediated hydrogen transfer in B12-dependent isomerizations. Active site structure analysis, structure comparisons, overview |
-, 746571 |
| 5.4.3.2 | more |
substitution of SAM with S-3',4'-anhydroadenosyl-L-methionine leads to generation of a stable allylic analogue of 5'-dA. radical. Deuterium labeling at positions 2', 3', and 5' dramatically alters the continuous-wave (CW) EPR spectrum |
-, 748031 |
| 5.4.3.2 | physiological function |
class II lysyl-tRNA synthetase and lysine-2,3-aminomutase are implicated in the modification of bacterial elongation factor P, EF-P, to convert a specific lysine to a hypothetical beta-lysyl-lysine. Both enzymes, YjeA and YjeK, are required forbeta-lysylation of EF-P. beta-Lysyl-EF-P stimulated N-formyl-methionyl-puromycin synthesis 4fold over the preparations containing unmodified EF-P and/or beta-lysyl-EF-P. The mutant K34A lacking the modification site lysine is inactive. YjeA canbeta-lysylate EF-P in vitro or in cells independently of YjeK. In contrast, YjeK alone or supplementation with D-beta-lysine cannot lysylate EF-P |
-, 727911 |
| 5.4.3.2 | physiological function |
lysine 2,3-aminomutase (LAM) utilizes the radical-SAM machinery to isomerize L-alpha-lysine to L-beta-lysine |
-, 748031 |
| 5.4.3.2 | 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 |
-, 748088 |
| 5.4.3.2 | physiological function |
the enzyme is involved in biosynthesis of beta-lysine, in methanoarchaea, beta-lysine acts as a precursor for osmolyte Nepsilon-acetyl-beta-lysine in response to abiotic salt and osmotic stress |
-, 728109 |
