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Literature summary extracted from

  • Joshi, V.; Laubengayer, K.M.; Schauer, N.; Fernie, A.R.; Jander, G.
    Two Arabidopsis threonine aldolases are nonredundant and compete with threonine deaminase for a common substrate pool (2006), Plant Cell, 18, 3564-3575.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.3.1.19 additional information threonine aldolase mutations increase substrate availability for threonine deaminase Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.3.1.19 L-threonine Arabidopsis thaliana
-
 2-oxobutanoate + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.3.1.19 Arabidopsis thaliana
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.3.1.19 seed
-
 Arabidopsis thaliana
-
4.3.1.19 seedling
-
 Arabidopsis thaliana
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.1.19 L-threonine
-
 Arabidopsis thaliana 2-oxobutanoate + NH3
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.3.1.19 OMR1
-
 Arabidopsis thaliana
4.3.1.19 Threonine deaminase
-
 Arabidopsis thaliana