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Literature summary for 5.4.3.2 extracted from

  • 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 (2015), J. Am. Chem. Soc., 137, 7111-7121 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.4.3.2

Cloned(Commentary)

Cloned (Comment) Organism
gene kamA, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS Clostridium subterminale

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ [4Fe-4S] cluster Clostridium subterminale

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-lysine Clostridium subterminale
-
 (3S)-3,6-diaminohexanoate
-
 ?
L-lysine Clostridium subterminale SB4
-
 (3S)-3,6-diaminohexanoate
-
 ?

Organism

Organism UniProt Comment Textmining
Clostridium subterminale Q9XBQ8
-
-
Clostridium subterminale SB4 Q9XBQ8
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography, ultrafiltration, and dialysis Clostridium subterminale

Reaction

Reaction Comment Organism Reaction ID
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 Clostridium subterminale
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lysine
-
 Clostridium subterminale (3S)-3,6-diaminohexanoate
-
 ?
L-lysine
-
 Clostridium subterminale SB4 (3S)-3,6-diaminohexanoate
-
 ?
additional information substrate 13C ENDOR measurements Clostridium subterminale ?
-
 ?
additional information substrate 13C ENDOR measurements Clostridium subterminale SB4 ?
-
 ?

Synonyms

Synonyms Comment Organism
kamA
-
 Clostridium subterminale
LAM
-
 Clostridium subterminale

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Clostridium subterminale

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Clostridium subterminale

Cofactor

Cofactor Comment Organism Structure
additional information S-3',4'-anhydroadenosyl-L-methionine, anSAM, development of the S-adenosyl-L-methionine surrogate, the compound is a true cofactor for lysine 2,3-aminomutase. Specific activity is 0.1 IU/mg Clostridium subterminale
pyridoxal 5'-phosphate
-
 Clostridium subterminale
S-adenosyl-L-methionine SAM, natural cofactor, lysine 2,3-aminomutase (LAM) is a radical S-adenosyl-L-methionine (SAM) enzyme. Enzyme 2,3-LAM utilizes radical-generating machinery comprising SAM anchored to the unique Fe2+ of a [4Fe-4S] cluster via a classical five-membered N,O chelate ring. Specific activity is 35-40 IU/mg Clostridium subterminale
[4Fe-4S] cluster
-
 Clostridium subterminale

General Information

General Information Comment Organism
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 Clostridium subterminale
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 Clostridium subterminale
physiological function lysine 2,3-aminomutase (LAM) utilizes the radical-SAM machinery to isomerize L-alpha-lysine to L-beta-lysine Clostridium subterminale