Literature summary for 6.3.2.4 extracted from

McDermott, A.E.; Creuzet, F.; Griffin, R.G.
Rotational resonance determination of the structure of an enzyme-inhibitor complex: phosphorylation of an (aminoalkyl)phosphinate inhibitor of D-alanyl-D-alanine ligase by ATP (1990), Biochemistry, 29, 5767-5775.

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Inhibitors

Inhibitors	Comment	Organism	Structure
[1(S)-aminoethyl][2-carboxy-2(R)-methyl-1-ethyl]phosphinic acid	ATP-dependent, slow-binding, enzyme-inhibitor half-life is 17 days at 37°C, mechanism of inactivation involves phosphorylation of the enzyme-bound inhibitor by ATP to form a phosphoryl-phosphinate adduct	Salmonella enterica subsp. enterica serovar Typhimurium

Organism

Organism	UniProt	Comment	Textmining
Salmonella enterica subsp. enterica serovar Typhimurium	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + D-Ala + D-Ala	-	Salmonella enterica subsp. enterica serovar Typhimurium	ADP + phosphate + D-Ala-D-Ala	-	?

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Release 2023.1 (January 2023)