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Literature summary for 4.3.1.19 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

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
seed
-
Arabidopsis thaliana
-
seedling
-
Arabidopsis thaliana
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
OMR1
-
Arabidopsis thaliana
Threonine deaminase
-
Arabidopsis thaliana