Literature summary for 5.4.3.2 extracted from

Lees, N.S.; Chen, D.; Walsby, C.J.; Behshad, E.; Frey, P.A.; Hoffman, B.M.
How an enzyme tames reactive intermediates: positioning of the active-site components of lysine 2,3-aminomutase during enzymatic turnover as determined by ENDOR spectroscopy (2006), J. Am. Chem. Soc., 128, 10145-10154.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Clostridium subterminale

Inhibitors

Inhibitors	Comment	Organism	Structure
4-thia-L-lysine	substrate analogue, generates a stable analogues of the alpha-Lys radical	Clostridium subterminale
trans-4,5-dehydro-L-lysine	substrate analogue, generates a stable analogues of the alpha-Lys radical	Clostridium subterminale

Organism

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

Purification (Commentary)

Purification (Comment)	Organism
recombinant protein, purification under anaerobic conditions	Clostridium subterminale

Reaction

Reaction	Comment	Organism	Reaction ID
L-lysine = (3S)-3,6-diaminohexanoate	the active site facilitates hydrogen atom transfer by enforcing van der Waals contact between radicals and their reacting partners thus minimizing side reactions of the highly active species	Clostridium subterminale	a

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Release 2023.1 (January 2023)