5.4.3.2: lysine 2,3-aminomutase
This is an abbreviated version!
For detailed information about lysine 2,3-aminomutase, go to the full flat file.
Word Map on EC 5.4.3.2
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5.4.3.2
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s-adenosylmethionine
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5\'-deoxyadenosyl
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epr
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pyridoxal
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l-beta-lysine
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hyperfine
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adenosylcobalamin-dependent
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formate-lyase
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subterminale
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aldimine
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pyridoxal-5'-phosphate
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adenosylcobalamin
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5'-deoxyadenosine
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cxxxcxxc
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homolytic
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deoxyadenosyl
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aminomutases
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synthesis
- 5.4.3.2
- s-adenosylmethionine
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5\'-deoxyadenosyl
- epr
- pyridoxal
- l-beta-lysine
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hyperfine
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adenosylcobalamin-dependent
- formate-lyase
- subterminale
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aldimine
- pyridoxal-5'-phosphate
- adenosylcobalamin
- 5'-deoxyadenosine
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cxxxcxxc
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homolytic
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deoxyadenosyl
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aminomutases
- synthesis
Reaction
Synonyms
AblA, Aminomutase, lysine 2,3-, HD73_2540, KAM, kamA, L-Lysine-2,3-aminomutase, LAM, lysine 2,3-aminomutase, lysine-2,3-aminomutase, Mutase, lysine 2,3-amino-, YjeK
ECTree
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General Information
General Information on EC 5.4.3.2 - lysine 2,3-aminomutase
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evolution
malfunction
metabolism
physiological function
additional information
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
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
evolution
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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
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evolution
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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
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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
malfunction
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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
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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
metabolism
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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
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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
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
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
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
physiological function
the enzyme is involved in the biosynthesis of Nepsilon-acetyl-beta-lysine, that is accumulated in the cells to respond to an osmotic upshock
physiological function
the enzyme is involved in the biosynthesis of Nepsilon-acetyl-beta-lysine, that is accumulated in the cells to respond to an osmotic upshock
physiological function
lysine 2,3-aminomutase (LAM) utilizes the radical-SAM machinery to isomerize L-alpha-lysine to L-beta-lysine
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
physiological function
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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
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physiological function
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the enzyme is involved in the biosynthesis of Nepsilon-acetyl-beta-lysine, that is accumulated in the cells to respond to an osmotic upshock
-
physiological function
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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
-
physiological function
-
the enzyme is involved in the biosynthesis of Nepsilon-acetyl-beta-lysine, that is accumulated in the cells to respond to an osmotic upshock
-
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
-
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
-
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
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physiological function
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lysine 2,3-aminomutase (LAM) utilizes the radical-SAM machinery to isomerize L-alpha-lysine to L-beta-lysine
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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
additional information
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
additional information
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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
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additional information
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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
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