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4.4.1.14: 1-aminocyclopropane-1-carboxylate synthase

This is an abbreviated version!
For detailed information about 1-aminocyclopropane-1-carboxylate synthase, go to the full flat file.

Word Map on EC 4.4.1.14

Reaction

S-adenosyl-L-methionine
=
1-aminocyclopropane-1-carboxylate
 +
methylthioadenosine

Synonyms

1-aminocyclopropane carboxylic acid synthase, 1-aminocyclopropane-1-carboxylate synthase, 1-aminocyclopropane-1-carboxylate synthase 4, 1-aminocyclopropane-1-carboxylate synthase 6, 1-aminocyclopropane-1-carboxylate synthetase, 1-aminocyclopropane-1-carboxylic acid synthase, 1-aminocyclopropanecarboxylate synthase, ACACS2 gene, ACC synthase, ACS, ACS-1, ACS1, ACS2, ACS3, ACS4, ACS5, ACS6, ACS7, ACS9, aminocyclopropane-1-carboxylate synthase, aminocyclopropane-2-carboxylic acid synthase, aminocyclopropanecarboxylate synthase, aminocyclopropanecarboxylic acid synthase, ASC, AtACS4 gene, Ca-ACS1, CyACS1, DC-ACS1, DC-ACS2, GhACS1, LE-ACS1A, LE-ACS2, LE-ACS3, LE-ACS4, LE-ACS6, LeACS2, MA-ACS4, MdACS1, MdACS3, MdACS5B, OsACS1, PgACS1, PgACS2, PgACS3a, PgACS3b, PgACS4, PmACS2, PmACS3, PmACS4, Pp-ACS1, S-adenosyl-L-methionine methylethioadenosine-lyase, S-adenosyl-L-methionine methylthioadenosine-lyase, S-adenosyl-L-methionine methylthioadenosine-lyase (1-aminocyclopropane-1-carboxylate-forming), synthase, 1-aminocyclopropanecarboxylate, type 2 1-aminocyclopropane-1-carboxylate synthase, type-2 ACC synthase

ECTree

     4 Lyases
         4.4 Carbon-sulfur lyases
             4.4.1 Carbon-sulfur lyases (only sub-subclass identified to date)
                4.4.1.14 1-aminocyclopropane-1-carboxylate synthase

Crystallization

Crystallization on EC 4.4.1.14 - 1-aminocyclopropane-1-carboxylate synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure at 2.4 A resolution
-
crystal structure of ACC synthase in complex with the substrate analogue [2-(aminooxy)ethyl](5'deoxyadenosin-5'-yl)(methyl)sulfonium at 2.01 A resolution, crystals are obtained with the sitting drop method, 0.001 ml of protein solution, consisting of 20 mg/ml ACC synthase, 10 mM [2-(aminooxy)ethyl](5'deoxyadenosin-5'-yl)(methyl)sulfonium, 50 mM HEPES, pH 7.9, 0.01 mM pyridoxal 5'-phosphate, 1 mM dithiothreitol, is mixed with 0.001 ml of precipitating solution containing 30% 2-methyl-2-4-pentanediol and 50 mM MES, pH 6.5
-
recombinant enzyme, cocrystals of the enzyme-L-vinylglycine complex are obtained by sitting drop method. The crystals belong to space group C2 with cell constants a = 103.3 A, b = 59.4 A, c = 79.0 A, beta = 124.2°. The crystal structure of the covalent adduct of the inactivated enzyme is determined at 2.25 A resolution
-
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
in silico three-dimensional modelling. The overall structure of the modelled binding site for pyridoxal 5'-phosphate and aminoethylvinylglycine in ACS1 is very similar to the known structure for the binding site in apple and tomato ACC synthase. The structures show good conservation of the catalytic residues
in complex with pyridoxal 5'-phosphate and aminoethoxyvinylglycine
-
vapor diffusion method, well buffer consists of 20 mM sodium cacodylate, pH 6.0, 200 mM Li2SO4 and 19-23% polyethylene glycol 3350, crystal structure of ACC synthase complexed with pyridoxal 5'-phosphate and aminoethoxyvinylglycine at 2.7 A resolution
-