Literature summary for 2.5.1.7 extracted from

Steinbach, A.; Scheidig, A.J.; Klein, C.D.
The unusual binding mode of cnicin to the antibacterial target enzyme MurA revealed by X-ray crystallography (2008), J. Med. Chem., 51, 5143-5147.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with inhibitor cnicin and substrate UDP-N-acetylglucosamine, at 2.0 A resolution. The enzyme catalyzes the formation of a covalent adduct between cnicin and UDP-N-acetylglucosamine via an anti-Michael 1,3-addition of UDP-N-acetylglucosamine to an alpha,beta-unsaturated carbonyl function in cnicin thus forming a noncovalent suicide inhibitor	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
cnicin	sesquiterpene lactone. The enzyme catalyzes the formation of a covalent adduct between cnicin and substrate UDP-N-acetylglucosamine via an anti-Michael 1,3-addition of UDP-N-acetylglucosamine to an alpha,beta-unsaturated carbonyl function in cnicin thus forming a noncovalent suicide inhibitor	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A749	-	-

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Release 2023.1 (January 2023)