Literature summary for 4.4.1.14 extracted from

Schaerer, M.A.; Eliot, A.C.; Gruetter, M.G.; Capitani, G.
Structural basis for reduced activity of 1-aminocyclopropane-1-carboxylate synthase affected by a mutation linked to andromonoecy (2011), FEBS Lett., 585, 111-114.

Crystallization (Commentary)

Crystallization (Comment)	Organism
to 1.35 A resolution. The internal aldimine Schiff base linking the C4' atom of the pyridoxal 5'-phosphate cofactor and the side chain nitrogen of K273 in the N'-pyridoxyl-lysine-5'-monophosphate adduct coexists with a small portion, about 20%, of free K273. Modeling of the mutation A46V, corresponding to A57V in Cucumis melo, which results in andromonoecious plants. The mutation changes the structure of the neighbouring active site residues only marginally. The mutation may cause an improper orientation of SAM in the active site	Malus domestica

Crystallization (Comment)

Organism

to 1.35 A resolution. The internal aldimine Schiff base linking the C4' atom of the pyridoxal 5'-phosphate cofactor and the side chain nitrogen of K273 in the N'-pyridoxyl-lysine-5'-monophosphate adduct coexists with a small portion, about 20%, of free K273. Modeling of the mutation A46V, corresponding to A57V in Cucumis melo, which results in andromonoecious plants. The mutation changes the structure of the neighbouring active site residues only marginally. The mutation may cause an improper orientation of SAM in the active site

Malus domestica

Protein Variants

Protein Variants	Comment	Organism
A46V	modeling of the mutation, corresponding to A57V in Cucumis melo, which results in andromonoecious plants. The mutation changes the structure of the neighbouring active site residues only marginally. The mutation may cause an improper orientation of SAM in the active site	Malus domestica

Organism

Organism	UniProt	Comment	Textmining
Malus domestica	P37821	-	-

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	the internal aldimine Schiff base linking the C4' atom of the pyridoxal 5'-phosphate cofactor and the side chain nitrogen of K273 in the N'-pyridoxyl-lysine-5'-monophosphate adduct coexists with a small portion, about 20%, of free K273	Malus domestica

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Release 2023.1 (January 2023)