Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.4.3.2 extracted from

  • Frey, P.
    Travels with carbon-centered radicals. 5'-Deoxyadenosine and 5'-deoxyadenosine-5'-yl in radical enzymology (2014), Acc. Chem. Res., 47, 540-549 .
    View publication on PubMed
Search for more literature for 5.4.3.2

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ one [4Fe-4S] cluster, the iron-binding motif in LAM is CxxxCxxC Clostridium subterminale

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
285000
-
-
 Clostridium subterminale

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-lysine Clostridium subterminale
-
 L-beta-lysine
-
 r
L-lysine Clostridium subterminale SB4
-
 L-beta-lysine
-
 r

Organism

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

Reaction

Reaction Comment Organism Reaction ID
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 Clostridium subterminale
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lysine
-
 Clostridium subterminale L-beta-lysine
-
 r
L-lysine
-
 Clostridium subterminale SB4 L-beta-lysine
-
 r
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 Clostridium subterminale ?
-
 ?
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 Clostridium subterminale SB4 ?
-
 ?

Subunits

Subunits Comment Organism
oligomer x * 47000 Clostridium subterminale

Synonyms

Synonyms Comment Organism
LAM
-
 Clostridium subterminale

Cofactor

Cofactor Comment Organism Structure
additional information enzyme LAM does not require adenosylcobalamin. It contains pyridoxal-5'-phosphate and iron and is activated by a reducing agent and S-adenosyl-L-methionine Clostridium subterminale
pyridoxal 5'-phosphate dependent on Clostridium subterminale
S-adenosyl-L-methionine dependent on, activates. Reductive cleavage of S-adenosyl-L-methionine to the 5'-deoxyadenosyl radical by enzyme LAM, mechanism, overview. S-adenosyl-L-methionine dependence in the reduction of [4Fe-4S]2+ to [4Fe-4S]1+, S-adenosyl-L-methionine is in a direct interaction with the iron-sulfur cluster Clostridium subterminale
[4Fe-4S] cluster enzyme LAM contains one [4Fe-4S] cluster ligated by three cysteine residues. S-adenosyl-L-methionine dependence in the reduction of [4Fe-4S]2+ to [4Fe-4S]1+, S-adenosyl-L-methionine is in a direct interaction with the iron-sulfur cluster Clostridium subterminale

General Information

General Information Comment Organism
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 Clostridium subterminale
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 Clostridium subterminale