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

BRENDA support

Literature summary for 5.4.3.2 extracted from

  • Behshad, E.; Ruzicka, F.J.; Mansoorabadi, S.O.; Chen, D.; Reed, G.H.; Frey, P.A.
    Enantiomeric free radicals and enzymatic control of stereochemistry in a radical mechanism: the case of lysine 2,3-aminomutases (2006), Biochemistry, 45, 12639-12646.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Clostridium subterminale
-
-
-
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Lys the radical intermediate has (S)-configuration, and stereochemistry is determined by the conformation of the lysine side chain in the active site Clostridium subterminale (3S)-3,6-diaminohexanoic acid
-
?
L-Lys hydrogen transfer is not rate-limiting in reaction. The radical intermediate has (R)-configuration, and stereochemistry is determined by the conformation of the lysine side chain in the active site Escherichia coli (3R)-3,6-diaminohexanoic acid
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.083
-
L-Lys pH 8.0, 37°C Escherichia coli
83
-
L-Lys pH 8.0, 37°C Clostridium subterminale