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
-
5\'-deoxyadenosyl
- epr
- pyridoxal
- l-beta-lysine
-
hyperfine
-
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
5.4.3.2 lysine 2,3-aminomutaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 5.4.3.2 - lysine 2,3-aminomutase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-Lys
(3R)-3,6-diaminohexanoic acid
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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
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-
?
L-Lys
(3S)-3,6-diaminohexanoic acid
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reaction with D-Lys is less than 1% of the reaction with L-Lys
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?
L-Lys
(3S)-3,6-diaminohexanoic acid
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reaction with D-Lys is less than 1% of the reaction with L-Lys
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?
L-Lys
(3S)-3,6-diaminohexanoic acid
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the radical intermediate has (S)-configuration, and stereochemistry is determined by the conformation of the lysine side chain in the active site
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-
?
L-Lys
?
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production of (3S)-3,6-diaminohexanoic acid for the biosynthesis of antibiotics
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-
?
L-Lys
?
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formation of (3S)-3,6-diaminohexanoic acid for biosynthesis of streptothricin F
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-
?
L-Lys
?
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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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initial step in the catabolismus of L-lysine to acetyl-CoA and ammonia
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?
L-lysine
(3S)-3,6-diaminohexanoate
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initial step in the catabolismus of L-lysine to acetyl-CoA and ammonia
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?
L-lysine
(3S)-3,6-diaminohexanoate
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initial step in the catabolismus of L-lysine to acetyl-CoA and ammonia
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?
L-lysine
(3S)-3,6-diaminohexanoate
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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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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
the enzyme functions by radical mechanism
-
-
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
-
-
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
-
-
r
L-lysine
(3S)-3,6-diaminohexanoate
the enzyme functions by radical mechanism
-
-
r
L-lysine
(3S)-3,6-diaminohexanoate
the enzyme functions by radical mechanism
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-
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
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highly specific for L-lysine
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-
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
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-
?
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
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-
?
additional information
?
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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
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?
additional information
?
-
substrate 13C ENDOR measurements
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-
?
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
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-
?
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
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-
?
additional information
?
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lysine 2,3-aminomutases functions as potential biocatalysts for the synthesis of beta-lysine in vivo and in vitro
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-
?
additional information
?
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lysine 2,3-aminomutases functions as potential biocatalysts for the synthesis of beta-lysine in vivo and in vitro
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?
