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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Reaction
Reaction on EC 5.4.3.2 - lysine 2,3-aminomutase
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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
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L-lysine = (3S)-3,6-diaminohexanoate
only the migrating (3-pro-R) hydrogen of alpha-Lys is involved in the intermolecular exchange
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L-lysine = (3S)-3,6-diaminohexanoate
lysine radicals participate in the rearrangement mechanism
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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
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L-lysine = (3S)-3,6-diaminohexanoate
mechanism of radical rearrangement in the reaction
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L-lysine = (3S)-3,6-diaminohexanoate
substantially or completely intermolecular hydrogen transfer
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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
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L-lysine = (3S)-3,6-diaminohexanoate
structure of a substrate radical intermediate in the reaction
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L-lysine = (3S)-3,6-diaminohexanoate
formation of substrate radicals as intermediates
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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
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L-lysine = (3S)-3,6-diaminohexanoate
LAM catalytic cycle and reaction intermediate analysis for lysine 2,3-aminomutase
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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
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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
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L-lysine = (3S)-3,6-diaminohexanoate
substantially or completely intermolecular hydrogen transfer
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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
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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
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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
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