Literature summary for 4.3.3.7 extracted from

Dobson, R.C.; Griffin, M.D.; Jameson, G.B.; Gerrard, J.A.
The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance (2005), Acta Crystallogr. Sect. D, 61, 1116-1124.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging-drop vapour-diffusion method, crystal struture of native and (S)-lysine-bound dihydropicolinate synthase are presented to 1.9 A and 2.0 A resolution, respectively	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
(S)-Lys	partial mixed inhibition with respect to pyruvate and partial non-competitive inhibition with resoect to L-aspartate 4-semialdehyde	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A6L2	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.32	-	(S)-Lys	with respect to L-aspartate 4-semialdehyde	Escherichia coli
3.9	-	(S)-Lys	with respect to pyruvate	Escherichia coli

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Release 2023.1 (January 2023)