Literature summary extracted from

Marks, G.T.; Harris, T.K.; Massiah, M.A.; Mildvan, A.S.; Harrison, D.H.
Mechanistic implications of methylglyoxal synthase complexed with phosphoglycolohydroxamic acid as observed by X-ray crystallography and NMR spectroscopy (2001), Biochemistry, 40, 6805-6818.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
4.2.3.3	sitting drop vapor diffusion method	Escherichia coli

Protein Variants

EC Number	Protein Variants	Comment	Organism
4.2.3.3	D71N	2500fold decrease in kcat	Escherichia coli

General Stability

EC Number	General Stability	Organism
4.2.3.3	D71N mutant enzyme rapidly becomes inactive in the absence of phosphate	Escherichia coli

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
4.2.3.3	phosphoglycolohydroxamic acid	tight binding inhibitor, neither a strictly competitive, non-competitive, nor uncompetitive mechanism	Escherichia coli

Organism

EC Number	Organism	UniProt	Comment	Textmining
4.2.3.3	Escherichia coli	-	-	-

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
4.2.3.3	glycerone phosphate = 2-oxopropanal + phosphate	mechanism	Escherichia coli	a

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4.2.3.3	dihydroxyacetone phosphate	converts dihydrocyacetone phosphate to a cis-enediolic intermediate, then catalyses the elimination of phosphate to form the enol of methylglyoxal	Escherichia coli	methylglyoxal + phosphate	-	?

Subunits

EC Number	Subunits	Comment	Organism
4.2.3.3	hexamer	homohexamer, crystallization experiments	Escherichia coli

Ki Value [mM]

EC Number	Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
4.2.3.3	0.000093	-	phosphoglycolohydroxamic acid	-	Escherichia coli

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Release 2023.1 (January 2023)