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Literature summary for 5.4.3.2 extracted from

  • 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 (2000), Biochemistry, 39, 9561-9570.
    View publication on PubMed
Search for more literature for 5.4.3.2

Inhibitors

Inhibitors Comment Organism Structure
trans-4,5-dehydro-L-lysine competes with L-lysine for binding to the active site Clostridium subterminale

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
280000
-
-
 Clostridium subterminale

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-lysine Clostridium subterminale initial step in the catabolismus of L-lysine to acetyl-CoA and ammonia (3S)-3,6-diaminohexanoate
-
 ?

Organism

Organism UniProt Comment Textmining
Clostridium subterminale
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lysine initial step in the catabolismus of L-lysine to acetyl-CoA and ammonia Clostridium subterminale (3S)-3,6-diaminohexanoate
-
 ?

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Clostridium subterminale
S-adenosyl-L-methionine
-
 Clostridium subterminale