Literature summary for 4.2.3.1 extracted from

Mas-Droux, C.; Biou, V.; Dumas, R.
Allosteric threonine synthase. Reorganization of the pyridoxal phosphate site upon asymmetric activation through S-adenosylmethionine binding to a novel site (2006), J. Biol. Chem., 281, 5188-5196.

Search for more literature for 4.2.3.1

Activating Compound

Activating Compound	Comment	Organism	Structure
S-adenosylmethionine	activates	Arabidopsis thaliana

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystallographic structure of Arabidopsis thaliana threonine synthase in complex with pyridoxal phosphate and with pyridoxal phosphate and S-adenosylmethionine	Arabidopsis thaliana
hanging drop method, 4°C, pH 6.5, resolution of 2.6 A	Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
O-phospho-L-homoserine + H2O	Arabidopsis thaliana	threonine synthesis in eukaryotes	L-threonine + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	Q9S7B5	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
O-phospho-L-homoserine + H2O = L-threonine + phosphate	reaction proceeds via phosphate removal and isomerization from primary to secondary alcohol	Arabidopsis thaliana	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
O-phospho-L-homoserine + H2O	threonine synthesis in eukaryotes	Arabidopsis thaliana	L-threonine + phosphate	-	?

Synonyms

Synonyms	Comment	Organism
threonine synthase	-	Arabidopsis thaliana

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Release 2023.1 (January 2023)