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Literature summary for 5.4.3.2 extracted from

  • Frey, P.A.; Reed, G.H.
    Pyridoxal-5'-phosphate as the catalyst for radical isomerization in reactions of PLP-dependent aminomutases (2011), Biochim. Biophys. Acta, 1814, 1548-1557.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
4,5-dehydro-(S)-lysine suicide inactivator Clostridium subterminale

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the activity is modestly increased by the addition of ferrous iron Clostridium subterminale

Organism

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

Oxidation Stability

Oxidation Stability Organism
the enzyme is extremely sensitive to oxidation by air and is active under anaerobic conditions Clostridium subterminale

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
LAM
-
Clostridium subterminale

Cofactor

Cofactor Comment Organism Structure
4Fe-4S-center
-
Clostridium subterminale
pyridoxal 5'-phosphate dependent on Clostridium subterminale