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L-lysine = (3S)-3,6-diaminohexanoate
L-lysine = (3S)-3,6-diaminohexanoate
mechanism
-
L-lysine = (3S)-3,6-diaminohexanoate
mechanism
-
L-lysine = (3S)-3,6-diaminohexanoate
reaction proceeds by a substrate radical rearrangement mechanism, in which the external aldimine formed between pyridoxal phosphate and Lys is initially converted into a lysyl-radical intermediate by hydrogen abstraction from C3
-
L-lysine = (3S)-3,6-diaminohexanoate
only the migrating (3-pro-R) hydrogen of alpha-Lys is involved in the intermolecular exchange
-
L-lysine = (3S)-3,6-diaminohexanoate
lysine radicals participate in the rearrangement mechanism
-
L-lysine = (3S)-3,6-diaminohexanoate
evidence for participation of pyridoxal 5'-phosphate in a radical rearrangement, formation of an aldimine linkage between the pyridoxal 5'-phosphate and the beta-nitrogen of (3S)-3,6-diaminohexanoic acid
-
L-lysine = (3S)-3,6-diaminohexanoate
mechanism of radical rearrangement in the reaction
-
L-lysine = (3S)-3,6-diaminohexanoate
substantially or completely intermolecular hydrogen transfer
-
L-lysine = (3S)-3,6-diaminohexanoate
activation of the enzyme may involve a transformation of S-adenosylmethionine into a form that promotes the generation of an adenosyl-5' free radical, which abstracts hydrogen from Lys to form 5'-deoxyadenosine as an intermediate
-
L-lysine = (3S)-3,6-diaminohexanoate
structure of a substrate radical intermediate in the reaction
-
L-lysine = (3S)-3,6-diaminohexanoate
formation of substrate radicals as intermediates
-
L-lysine = (3S)-3,6-diaminohexanoate
the active site facilitates hydrogen atom transfer by enforcing van der Waals contact between radicals and their reacting partners thus minimizing side reactions of the highly active species
-
L-lysine = (3S)-3,6-diaminohexanoate
LAM catalytic cycle and reaction intermediate analysis for lysine 2,3-aminomutase
-
L-lysine = (3S)-3,6-diaminohexanoate
lysine 2,3-aminomutase (LAM) is a radical S-adenosyl-L-methionine (SAM) enzyme, catalysis is initiated by reductive cleavage of the S-adenosyl-L-methionine S-C5' bond, which creates the highly reactive 5'-deoxyadenosyl radical, the same radical generated by homolytic Co-C bond cleavage in B12 radical enzymes. The S-adenosyl-L-methionine surrogate S-3',4'-anhydroadenosyl-L-methionine can replace S-adenosyl-L-methionine as a cofactor in the isomerization of L-alpha-lysine to L-beta-lysine by 2,3-LAM, via the stable allylic anhydroadenosyl radical. The holoenzyme coordinates a pyridoxal 5'-phosphate cofactor through formation of an internal aldimine with Lys337. As L-alpha-lysine binds, pyridoxal 5'-phosphate forms an external aldimine linkage to the alpha-amine group of the substrate. Reductive cleavage of S-adenosyl-L-methionine leads to formation of 5'-dA radical. Electron transfer from the [4Fe4S]1+ cluster initiates radical S-adenosyl-L-methionine reactions by reductive cleavage of the S-C5' bond to create the highly reactive 5'-deoxyadenosyl radical
L-lysine = (3S)-3,6-diaminohexanoate
lysine 2,3-aminomutase catalyzes S-adenosylmethionine and pyridoxal 5'-phosphate-dependent interconversion of L-lysine and L-beta-lysine, the reaction follows the pattern of adenosylcobalamin-dependent rearrangements, with hydrogen transfer from lysine through the adenosyl-C5' of S-adenosyl-L-methionine to beta-lysine. S-Adenosyl-L-methionine is cleaved to form 5'-deoxyadenosine-5'-yl followed by abstraction of C3(H) from pyridoxal-5'-phosphate-alpha-lysine aldimine to form PLP-R-lysine-3-yl. Pyridoxal 5'-phosphate-alpha-lysine-3-yl isomerizes to pyridoxal-beta-lysine-2-yl, and a hydrogen abstraction from 5'-deoxyadenosine regenerates 5'-deoxyadenosine-5'-yl and releases beta-lysine, 4 radicals in the reaction. Identification of radical intermediates. Reaction mechanism, detailed overview
L-lysine = (3S)-3,6-diaminohexanoate
activation of the enzyme may involve a transformation of S-adenosylmethionine into a form that promotes the generation of an adenosyl-5' free radical, which abstracts hydrogen from Lys to form 5'-deoxyadenosine as an intermediate
-
-
L-lysine = (3S)-3,6-diaminohexanoate
evidence for participation of pyridoxal 5'-phosphate in a radical rearrangement, formation of an aldimine linkage between the pyridoxal 5'-phosphate and the beta-nitrogen of (3S)-3,6-diaminohexanoic acid
-
-
L-lysine = (3S)-3,6-diaminohexanoate
substantially or completely intermolecular hydrogen transfer
-
-
L-lysine = (3S)-3,6-diaminohexanoate
mechanism
-
-
L-lysine = (3S)-3,6-diaminohexanoate
the active site facilitates hydrogen atom transfer by enforcing van der Waals contact between radicals and their reacting partners thus minimizing side reactions of the highly active species
-
-
L-lysine = (3S)-3,6-diaminohexanoate
lysine 2,3-aminomutase catalyzes S-adenosylmethionine and pyridoxal 5'-phosphate-dependent interconversion of L-lysine and L-beta-lysine, the reaction follows the pattern of adenosylcobalamin-dependent rearrangements, with hydrogen transfer from lysine through the adenosyl-C5' of S-adenosyl-L-methionine to beta-lysine. S-Adenosyl-L-methionine is cleaved to form 5'-deoxyadenosine-5'-yl followed by abstraction of C3(H) from pyridoxal-5'-phosphate-alpha-lysine aldimine to form PLP-R-lysine-3-yl. Pyridoxal 5'-phosphate-alpha-lysine-3-yl isomerizes to pyridoxal-beta-lysine-2-yl, and a hydrogen abstraction from 5'-deoxyadenosine regenerates 5'-deoxyadenosine-5'-yl and releases beta-lysine, 4 radicals in the reaction. Identification of radical intermediates. Reaction mechanism, detailed overview
-
-
L-lysine = (3S)-3,6-diaminohexanoate
lysine 2,3-aminomutase (LAM) is a radical S-adenosyl-L-methionine (SAM) enzyme, catalysis is initiated by reductive cleavage of the S-adenosyl-L-methionine S-C5' bond, which creates the highly reactive 5'-deoxyadenosyl radical, the same radical generated by homolytic Co-C bond cleavage in B12 radical enzymes. The S-adenosyl-L-methionine surrogate S-3',4'-anhydroadenosyl-L-methionine can replace S-adenosyl-L-methionine as a cofactor in the isomerization of L-alpha-lysine to L-beta-lysine by 2,3-LAM, via the stable allylic anhydroadenosyl radical. The holoenzyme coordinates a pyridoxal 5'-phosphate cofactor through formation of an internal aldimine with Lys337. As L-alpha-lysine binds, pyridoxal 5'-phosphate forms an external aldimine linkage to the alpha-amine group of the substrate. Reductive cleavage of S-adenosyl-L-methionine leads to formation of 5'-dA radical. Electron transfer from the [4Fe4S]1+ cluster initiates radical S-adenosyl-L-methionine reactions by reductive cleavage of the S-C5' bond to create the highly reactive 5'-deoxyadenosyl radical
-
-
L-lysine = (3S)-3,6-diaminohexanoate
-
-
-
-
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(S)-lysine
(S)-beta-lysine
alpha-lysine
beta-lysine
-
-
-
-
?
L-2-aminobutyrate
L-3-aminobutyrate
L-Lys
(3R)-3,6-diaminohexanoic acid
-
hydrogen transfer is not rate-limiting in reaction. The radical intermediate has (R)-configuration, and stereochemistry is determined by the conformation of the lysine side chain in the active site
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
L-lysine
(3S)-3,6-diaminohexanoate
L-lysine
(3S)-3,6-diaminohexanoic acid
S-adenosylmethionine
5'-deoxyadenosylmethionine
-
-
-
r
additional information
?
-
(S)-lysine
(S)-beta-lysine
-
-
-
-
r
(S)-lysine
(S)-beta-lysine
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-
-
-
r
L-2-aminobutyrate
L-3-aminobutyrate
-
very low activity
-
-
?
L-2-aminobutyrate
L-3-aminobutyrate
-
very low activity
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-
?
L-alanine
beta-alanine
-
very low activity
-
-
?
L-alanine
beta-alanine
-
very low activity
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-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
r
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
r
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
reaction with D-Lys is less than 1% of the reaction with L-Lys
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
r
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
reaction with D-Lys is less than 1% of the reaction with L-Lys
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
r
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
(2S)-alpha-Lys
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
the radical intermediate has (S)-configuration, and stereochemistry is determined by the conformation of the lysine side chain in the active site
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
(2S)-alpha-Lys
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
-
-
-
?
L-Lys
?
-
production of (3S)-3,6-diaminohexanoic acid for the biosynthesis of antibiotics
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-
?
L-Lys
?
-
formation of (3S)-3,6-diaminohexanoic acid for biosynthesis of streptothricin F
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-
?
L-Lys
?
-
formation of (3S)-3,6-diaminohexanoic acid for biosynthesis of streptothricin F
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?
L-lysine
(3S)-3,6-diaminohexanoate
-
-
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?
L-lysine
(3S)-3,6-diaminohexanoate
-
-
-
?
L-lysine
(3S)-3,6-diaminohexanoate
-
-
-
?
L-lysine
(3S)-3,6-diaminohexanoate
-
initial step in the catabolismus of L-lysine to acetyl-CoA and ammonia
-
?
L-lysine
(3S)-3,6-diaminohexanoate
-
initial step in the catabolismus of L-lysine to acetyl-CoA and ammonia
-
?
L-lysine
(3S)-3,6-diaminohexanoate
-
initial step in the catabolismus of L-lysine to acetyl-CoA and ammonia
-
?
L-lysine
(3S)-3,6-diaminohexanoate
-
-
-
?
L-lysine
(3S)-3,6-diaminohexanoate
-
-
-
-
?
L-lysine
(3S)-3,6-diaminohexanoate
-
-
-
-
?
L-lysine
(3S)-3,6-diaminohexanoate
-
lysyl modification at lysine 34 in native and recombinant bacterial elongation factor-P proteins, no activity with bacterial elongation factor-P mutant K34A
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?
L-lysine
(3S)-3,6-diaminohexanoate
-
-
-
-
?
L-lysine
(3S)-3,6-diaminohexanoate
-
lysyl modification at lysine 34 in native and recombinant bacterial elongation factor-P proteins, no activity with bacterial elongation factor-P mutant K34A
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?
L-lysine
(3S)-3,6-diaminohexanoate
-
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r
L-lysine
(3S)-3,6-diaminohexanoate
the enzyme functions by radical mechanism
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r
L-lysine
(3S)-3,6-diaminohexanoate
-
-
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r
L-lysine
(3S)-3,6-diaminohexanoate
the enzyme functions by radical mechanism
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r
L-lysine
(3S)-3,6-diaminohexanoate
conversion of alpha-lysine to beta-lysine is confirmed by NMR analysis in strain FDF1
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r
L-lysine
(3S)-3,6-diaminohexanoate
the enzyme functions by radical mechanism
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r
L-lysine
(3S)-3,6-diaminohexanoate
conversion of alpha-lysine to beta-lysine is confirmed by NMR analysis in strain FDF1
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r
L-lysine
(3S)-3,6-diaminohexanoate
the enzyme functions by radical mechanism
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r
L-lysine
(3S)-3,6-diaminohexanoate
-
-
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r
L-lysine
(3S)-3,6-diaminohexanoate
the enzyme functions by radical mechanism
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r
L-lysine
(3S)-3,6-diaminohexanoate
-
-
-
r
L-lysine
(3S)-3,6-diaminohexanoate
the enzyme functions by radical mechanism
-
-
r
L-lysine
(3S)-3,6-diaminohexanoic acid
-
-
-
-
?
L-lysine
(3S)-3,6-diaminohexanoic acid
-
-
-
r
L-lysine
(3S)-3,6-diaminohexanoic acid
-
highly specific for L-lysine
-
-
r
L-lysine
(3S)-3,6-diaminohexanoic acid
-
highly specific for L-lysine
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r
L-lysine
(3S)-3,6-diaminohexanoic acid
-
-
-
-
?
L-lysine
L-beta-lysine
-
-
-
r
L-lysine
L-beta-lysine
-
-
-
r
L-lysine
L-beta-lysine
-
-
-
r
L-lysine
L-beta-lysine
-
-
-
r
additional information
?
-
-
the equilibrium constants for reaction favor the beta-isomers. The value of the equilibrium constant is independent of pH between pH 6 and pH 11. It is temperature-dependent and ranges from 10.9 at 4°C to 6.8 at 65°C. Reaction is enthalpy-driven
-
-
?
additional information
?
-
-
the enzyme does not display detectable activity toward D-lysine, L-glutamate, L-glutamine, L-threonine, L-homoserine, L-tyrosine, L-phenylalanine, L-valine, L-leucine, L-isoleucine, L-histidine, L-tryptophan, L-ornithine, or L-arginine
-
-
?
additional information
?
-
lysine 2,3-aminomutase (LAM) catalyzes S-adenosylmethionine and pyridoxal-5'-phosphate dependent interconversion of L-lysine and L-beta-lysine. Reaction of trans-4,5-dehydro-L-lysine with the enzyme and S-adenosyl-L-methionine leads to the 4,5-dehydro-radical. Reductive cleavage of S-adenosyl-L-methionine to the 5'-deoxyadenosyl radical by enzyme LAM, mechanism, overview
-
-
?
additional information
?
-
substrate 13C ENDOR measurements
-
-
?
additional information
?
-
-
the enzyme does not display detectable activity toward D-lysine, L-glutamate, L-glutamine, L-threonine, L-homoserine, L-tyrosine, L-phenylalanine, L-valine, L-leucine, L-isoleucine, L-histidine, L-tryptophan, L-ornithine, or L-arginine
-
-
?
additional information
?
-
-
the equilibrium constants for reaction favor the beta-isomers. The value of the equilibrium constant is independent of pH between pH 6 and pH 11. It is temperature-dependent and ranges from 10.9 at 4°C to 6.8 at 65°C. Reaction is enthalpy-driven
-
-
?
additional information
?
-
lysine 2,3-aminomutase (LAM) catalyzes S-adenosylmethionine and pyridoxal-5'-phosphate dependent interconversion of L-lysine and L-beta-lysine. Reaction of trans-4,5-dehydro-L-lysine with the enzyme and S-adenosyl-L-methionine leads to the 4,5-dehydro-radical. Reductive cleavage of S-adenosyl-L-methionine to the 5'-deoxyadenosyl radical by enzyme LAM, mechanism, overview
-
-
?
additional information
?
-
substrate 13C ENDOR measurements
-
-
?
additional information
?
-
-
substrate 13C ENDOR measurements
-
-
?
additional information
?
-
-
a [4Fe-4S]+ cluster reduces a bound S-adenosylmethionine (SAM) molecule, cleaving it into methionine and a 5'-deoxyadenosyl radical. This step initiates the varied chemistry catalyzed by each of the so-called radical SAM enzymes. The strongly oxidizing 5'-deoxyadenosyl radical is quenched by abstracting a H-atom from a target species. Reaction intermediate analysis for lysine 2,3-aminomutase with 4-thia-L-lysine, 13C ENDOR measurements. A close proximity of 5'-dAH to the substrate/product radical is maintained throughout the reaction cycle is thought to minimize the potential for unwanted side reactions of the reactive intermediates and help to recycle S-adenosylmethionine for the next turnover. The pyridoxal 5'-phosphate cofactor plays an important role in stabilizing this species by delocalizing the unpaired electron onto the Pi-system of its pyridine ring yielding N3-(5'-phosphopyridoxylidene)-beta-lysin-2-yl
-
-
?
additional information
?
-
lysine 2,3-aminomutases functions as potential biocatalysts for the synthesis of beta-lysine in vivo and in vitro
-
-
?
additional information
?
-
lysine 2,3-aminomutases functions as potential biocatalysts for the synthesis of beta-lysine in vivo and in vitro
-
-
?
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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
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
-
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
-
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
-
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
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
-
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
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
-
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
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
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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
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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
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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
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physiological function
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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
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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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additional information
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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Chirpich, T.P.; Zappia, V.; Costilow, R.N.; Barker, H.A.
Lysine 2,3-aminomutase. Purification and properties of a pyridoxal phosphate and S-adenosylmethionine-activated enzyme
J. Biol. Chem.
245
1778-1789
1970
Clostridium sp., Clostridium sp. SB4
brenda
Zappia, V.; Barker, H.A.
Studies on lysine-2,3-aminomutase. Subunit structure and sulfhydryl groups
Biochim. Biophys. Acta
207
505-513
1970
Clostridium sp., Clostridium sp. SB4
brenda
Chirpich, T.P.; Barker, H.A.
Lysine-2,3-aminomutase (Clostridium)
Methods Enzymol.
17B
215-222
1971
Clostridium sp., Clostridium sp. SB4
-
brenda
Barker, H.A.; Kahn, J.M.; Hedrick, L.
Pathway of lysine degradation in Fusobacterium nucleatum
J. Bacteriol.
152
201-207
1982
Fusobacterium nucleatum
brenda
Aberhart, D.J.; Gould, S.J.; Lin, H.J.; Thiruvengadam, T.K.; Weiller, B.H.
Stereochemistry of lysine 2,3-aminomutase isolated from Clostridium subterminale strain SB4
J. Am. Chem. Soc.
105
5461-5470
1983
Clostridium subterminale, Clostridium subterminale SB4
-
brenda
Thiruvengadam, T.K.; Gould, S.J.; Aberhart, D.J.; Lin, H.J.
Biosynthesis of Streptothricin F. 5. Formation of beta-lysine by Streptomyces L-1689-23
J. Am. Chem. Soc.
105
5470-5476
1983
Streptomyces sp., Streptomyces sp. L-1689-23
-
brenda
Petrovich, R.M.; Ruzicka, F.J.; Reed, G.H.; Frey, P.A.
Metal cofactors of lysine-2,3-aminomutase
J. Biol. Chem.
266
7656-7660
1991
Clostridium sp., Clostridium sp. SB4
brenda
Song, K.B.; Frey, P.A.
Molecular properties of lysine-2,3-aminomutase
J. Biol. Chem.
266
7651-7655
1991
Clostridium subterminale, Clostridium subterminale SB4
brenda
Aberhart, D.J.
Studies of the mechanism of lysine 2,3-aminomutase
J. Chem. Soc. Perkin Trans. I
1988
343-350
1988
Clostridium subterminale, Clostridium subterminale SB4
-
brenda
Aberhart, D.J.; Cotting, J.A.
Mechanistic studies on lysine 2,3-aminomutase: carbon-13-deuterium crossover experiments
J. Chem. Soc. Perkin Trans. I
1988
2119-2122
1988
Clostridium subterminale
-
brenda
Frey, P.A.; Reed, G.H.
Lysine 2,3-aminomutase and the mechanism of the interconversion of lysine and beta-lysine
Adv. Enzymol. Relat. Areas Mol. Biol.
66
1-39
1993
Clostridium sp.
brenda
Frey, P.A.; Moss, M.; Petrovich, R.; Baraniak, J.
The roles of S-adenosylmethionine and pyridoxal phosphate in the lysine 2,3-aminomutase reaction
Ann. N. Y. Acad. Sci.
585
368-378
1990
Clostridium sp.
brenda
Frey, P.A.; Ballinger, M.D.; Reed, G.H.
S-Adenosylmethionine: a "poor man's coenzyme B12" in the reaction of lysine 2,3-aminomutase
Biochem. Soc. Trans.
26
304-310
1998
Clostridium sp.
brenda
Lieder, K.W.; Booker, S.; Ruzicka, F.J.; Beinert, H.; Reed, G.H.; Frey, P.A.
S-Adenosylmethionine-dependent reduction of lysine 2,3-aminomutase and observation of the catalytically functional iron-sulfur centers by electron paramagnetic resonance
Biochemistry
37
2578-2585
1998
Clostridium subterminale
brenda
Frey, P.A.
Lysine 2,3-aminomutase: is adenosylmethionine a poor man's adenosylcobalamin?
FASEB J.
7
662-670
1993
Clostridium subterminale
brenda
Moss, M.L.; Frey, P.A.
Activation of lysine 2,3-aminomutase by S-adenosylmethionine
J. Biol. Chem.
265
18112-18115
1990
Clostridium sp., Clostridium sp. SB4
brenda
Baraniak, J.; Moss, M.L.; Frey, P.A.
Lysine 2,3-aminomutase. Support for a mechanism of hydrogen transfer involving S-adenosylmethionine
J. Biol. Chem.
264
1357-1360
1989
Clostridium sp., Clostridium sp. SB4
brenda
Ballinger, M.D.; Frey, P.A.; Reed, G.H.; LoBrutto, R.
Pulsed electron paramagnetic resonance studies of the lysine 2,3-aminomutase substrate radical: evidence for participation of pyridoxal 5'-phosphate in a radical rearrangement
Biochemistry
34
10086-10093
1995
Clostridium sp., Clostridium sp. SB4
brenda
Ballinger, M.D.; Frey, P.A.; Reed, G.H.
Structure of a substrate radical intermediate in the reaction of lysine 2,3-aminomutase
Biochemistry
31
10782-10789
1992
Clostridium sp.
brenda
Ballinger, M.D.; Reed, G.H.; Frey, P.A.
An organic radical in the lysine 2,3-aminomutase reaction
Biochemistry
31
949-953
1992
Clostridium sp.
brenda
Chen, D.; Ruzicka, F.J.; Frey, P.A.
A novel lysine 2,3-aminomutase encoded by the yodO gene of Bacillus subtilis: characterization and the observation of organic radical intermediates
Biochem. J.
348
539-549
2000
Bacillus subtilis
brenda
Cosper, N.J.; Booker, S.J.; Ruzicka, F.; Frey, P.A.; Scott, R.A.
Direct FeS cluster involvement in generation of a radical in lysine 2,3-aminomutase
Biochemistry
39
15668-15673
2000
Clostridium subterminale
brenda
Wu, W.; Booker, S.; Lieder, K.W.; Bandarian, V.; Reed, G.H.; Frey, P.A.
Lysine 2,3-aminomutase and trans-4,5-dehydrolysine: characterization of an allylic analogue of a substrate-based radical in the catalytic mechanism
Biochemistry
39
9561-9570
2000
Clostridium subterminale
brenda
Chen, D.; Walsby, C.; Hoffman, B.M.; Frey, P.A.
Coordination and mechanism of reversible cleavage of S-adenosylmethionine by the [4Fe-4S] center in lysine 2,3-aminomutase
J. Am. Chem. Soc.
125
11788-11789
2003
Clostridium subterminale
brenda
Pfluger, K.; Baumann, S.; Gottschalk, G.; Lin, W.; Santos, H.; Muller, V.
Lysine-2,3-aminomutase and beta-lysine acetyltransferase genes of methanogenic archaea are salt induced and are essential for the biosynthesis of Nepsilon-acetyl-beta-lysine and growth at high salinity
Appl. Environ. Microbiol.
69
6047-6055
2003
Methanococcus maripaludis (Q6LYX4), Methanococcus maripaludis, Methanosarcina mazei (Q8PYC9), Methanosarcina mazei, Methanosarcina mazei DSM 3647 (Q8PYC9), Methanococcus maripaludis DSM 2067 (Q6LYX4)
brenda
Lepore, B.W.; Ruzicka, F.J.; Frey, P.A.; Ringe, D.
The X-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale
Proc. Natl. Acad. Sci. USA
102
13819-13824
2005
Clostridium subterminale (Q9XBQ8), Clostridium subterminale
brenda
Brazeau, B.J.; Gort, S.J.; Jessen, H.J.; Andrew, A.J.; Liao, H.H.
Enzymatic activation of lysine 2,3-aminomutase from Porphyromonas gingivalis
Appl. Environ. Microbiol.
72
6402-6404
2006
Porphyromonas gingivalis
brenda
Behshad, E.; Ruzicka, F.J.; Mansoorabadi, S.O.; Chen, D.; Reed, G.H.; Frey, P.A.
Enantiomeric free radicals and enzymatic control of stereochemistry in a radical mechanism: the case of lysine 2,3-aminomutases
Biochemistry
45
12639-12646
2006
Clostridium subterminale, Escherichia coli
brenda
Chen, D.; Frey, P.A.; Lepore, B.W.; Ringe, D.; Ruzicka, F.J.
Identification of structural and catalytic classes of highly conserved amino acid residues in lysine 2,3-aminomutase
Biochemistry
45
12647-12653
2006
Clostridium subterminale (Q9XBQ8), Clostridium subterminale SB4 (Q9XBQ8), Clostridium subterminale SB4
brenda
Hinckley, G.T.; Frey, P.A.
Cofactor dependence of reduction potentials for [4Fe-4S]2+/1+ in lysine 2,3-aminomutase
Biochemistry
45
3219-3225
2006
Clostridium subterminale, Clostridium subterminale SB4
brenda
Wang, S.C.; Frey, P.A.
Binding energy in the one-electron reductive cleavage of S-adenosylmethionine in lysine 2,3-aminomutase, a radical SAM enzyme
Biochemistry
46
12889-12895
2007
Clostridium subterminale, Clostridium subterminale SB4
brenda
Chen, D.; Tanem, J.; Frey, P.A.
Basis for the equilibrium constant in the interconversion of L-lysine and L-beta-lysine by lysine 2,3-aminomutase
Biochim. Biophys. Acta
1774
297-302
2007
Clostridium subterminale, Clostridium subterminale SB4
brenda
Lees, N.S.; Chen, D.; Walsby, C.J.; Behshad, E.; Frey, P.A.; Hoffman, B.M.
How an enzyme tames reactive intermediates: positioning of the active-site components of lysine 2,3-aminomutase during enzymatic turnover as determined by ENDOR spectroscopy
J. Am. Chem. Soc.
128
10145-10154
2006
Clostridium subterminale, Clostridium subterminale SB4
brenda
Frey, P.A.; Hegeman, A.D.; Ruzicka, F.J.
The radical SAM superfamily
Crit. Rev. Biochem. Mol. Biol.
43
63-88
2008
Clostridium subterminale (Q9XBQ8)
brenda
Saum, R.; Mingote, A.; Santos, H.; Mueller, V.
A novel limb in the osmoregulatory network of Methanosarcina mazei Goe1: N(epsilon)-acetyl-beta-lysine can be substituted by glutamate and alanine
Environ. Microbiol.
11
1056-1065
2009
Methanosarcina mazei Go1
brenda
Frey, P.A.; Reed, G.H.
Pyridoxal-5'-phosphate as the catalyst for radical isomerization in reactions of PLP-dependent aminomutases
Biochim. Biophys. Acta
1814
1548-1557
2011
Clostridium subterminale, Clostridium subterminale SB4
brenda
Ruzicka, F.J.; Frey, P.A.
Kinetic and spectroscopic evidence of negative cooperativity in the action of lysine 2,3-aminomutase
J. Phys. Chem. B
114
16118-16124
2010
Clostridium subterminale, Clostridium subterminale SB4
brenda
Park, J.H.; Johansson, H.E.; Aoki, H.; Huang, B.X.; Kim, H.Y.; Ganoza, M.C.; Park, M.H.
Post-translational modification by beta-lysylation is required for activity of Escherichia coli elongation factor P (EF-P)
J. Biol. Chem.
287
2579-2590
2012
Escherichia coli, Escherichia coli K-16
brenda
Hung, C.C.; Lai, M.C.
The phylogenetic analysis and putative function of lysine 2,3-aminomutase from methanoarchaea infers the potential biocatalysts for the synthesis of beta-lysine
J. Microbiol. Immunol. Infect.
46
1-10
2013
Methanocalculus chunghsingensis (G3F9W8), Methanocalculus chunghsingensis, Methanohalophilus portucalensis (G3F9X2), Methanohalophilus portucalensis, Methanosarcina mazei (Q8PYC9), Methanosarcina mazei DSM 3647 (Q8PYC9), Methanohalophilus portucalensis FDF1 (G3F9X2), Methanocalculus chunghsingensis K1F9705b (G3F9W8)
brenda
Stich, T.A.; Myers, W.K.; Britt, R.D.
Paramagnetic intermediates generated by radical S-adenosylmethionine (SAM) enzymes
Acc. Chem. Res.
47
2235-2243
2014
Escherichia coli
brenda
Frey, P.
Travels with carbon-centered radicals. 5'-Deoxyadenosine and 5'-deoxyadenosine-5'-yl in radical enzymology
Acc. Chem. Res.
47
540-549
2014
Clostridium subterminale (Q9XBQ8), Clostridium subterminale SB4 (Q9XBQ8)
brenda
Horitani, M.; Byer, A.S.; Shisler, K.A.; Chandra, T.; Broderick, J.B.; Hoffman, B.M.
Why nature uses radical SAM enzymes so widely electron nuclear double resonance studies of lysine 2,3-aminomutase show the 5-dAdo? Free radical is never free
J. Am. Chem. Soc.
137
7111-7121
2015
Clostridium subterminale (Q9XBQ8), Clostridium subterminale SB4 (Q9XBQ8), Clostridium subterminale SB4
brenda
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
J. Bacteriol.
196
2934-2943
2014
Bacillus thuringiensis serovar kurstaki (A0A0K0QCW0), Bacillus thuringiensis serovar kurstaki, Bacillus thuringiensis serovar kurstaki HD73 (A0A0K0QCW0)
brenda