Literature summary for 4.2.3.1 extracted from

Farrington, G.K.; Kumar, A.; Shames, S.L.; Ewaskiewicz, J.I.; Ash, D.A.; Wedler, F.C.
Threonine synthase of Escherichia coli: inhibition by classical and slow-binding analogues of homoserine phosphate (1993), Arch. Biochem. Biophys., 307, 165-174.

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Inhibitors

Inhibitors	Comment	Organism	Structure
L-2-amino-3[(phosphonomethyl)thio]propionic acid	Ki: 0.00011 mM, "slow, tight" inhibition kinetics	Escherichia coli
L-threo-3-hydroxyhomoserine	Ki: 0.006 mM	Escherichia coli
phosphonovaleric acid	Ki: 0.031 mM	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
O-phospho-L-homoserine + H2O = L-threonine + phosphate	inhibitor studies concerning mechanism, model of stepwise catalytic mechanism	Escherichia coli	a

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	enzyme assay at	Escherichia coli

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.006	-	L-threo-3-hydroxyhomoserine	-	Escherichia coli
0.031	-	phosphonovaleric acid	-	Escherichia coli

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Release 2023.1 (January 2023)