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1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2
1-butene + cyanide + dehydroascorbate + CO2 + H2O
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2 + HCO3-
1-butene + cyanide + dehydroascorbate + CO2 + H2O
1-amino-2-methylcyclopropane-1-carboxylate + L-ascorbate + O2
?
1-aminocyclopropane-1-carboxylate + 5,6-O-isopropylidine L-ascorbate + O2
ethylene + cyanide + 5,6-O-isopropylidine L-dehydroascorbate + CO2 + H2O
-
better cosubstrate than L-ascorbate
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
1-aminocyclopropane-1-carboxylate + ascorbate + O2 + H+
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + D-ascorbate + O2
ethylene + cyanide + D-dehydroascorbate + CO2 + H2O
-
better cosubstrate than L-ascorbate
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
1-aminocyclopropane-1-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
alpha-aminoisobutyric acid + L-ascorbate + O2
ammonia + acetone + dehydroascorbate + CO2 + H2O
-
-
-
-
?
D-alanine + L-ascorbate + O2
?
-
-
-
-
?
D-alpha-aminobutyric acid + L-ascorbate + O2
ammonia + acetone + dehydroascorbate + CO2 + H2O
-
-
-
-
?
L-alanine + L-ascorbate + O2
?
-
-
-
-
?
L-alpha-aminobutyric acid + L-ascorbate + O2
ammonia + acetone + dehydroascorbate + CO2 + H2O
-
-
-
-
?
N-hydroxy-alpha-aminoisobutyric acid + L-ascorbate + O2
ammonia + acetone + dehydroascorbate + CO2 + H2O
-
-
-
-
?
O2 + 1-aminocyclopropyl-1-carboxylic acid + ascorbate
?
-
assay at pH 7.2, 25°C
-
-
?
additional information
?
-
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2
1-butene + cyanide + dehydroascorbate + CO2 + H2O
-
stereoselectivity
-
-
?
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2
1-butene + cyanide + dehydroascorbate + CO2 + H2O
-
i.e. allo-coronamic acid
-
-
?
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2
1-butene + cyanide + dehydroascorbate + CO2 + H2O
-
stereoselectivity
-
-
?
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2
1-butene + cyanide + dehydroascorbate + CO2 + H2O
-
i.e. allo-coronamic acid
-
-
?
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2
1-butene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2
1-butene + cyanide + dehydroascorbate + CO2 + H2O
-
prefers mixture of 1R,2S- and 1S,2R-amino-2-ethylcyclopropane-1-carboxylate, less effective with racemic mixture of 1R,2R- and 1S,2S-diastereomers
-
-
?
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2
1-butene + cyanide + dehydroascorbate + CO2 + H2O
Vicia sp.
-
stereoselectivity
-
-
?
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2
1-butene + cyanide + dehydroascorbate + CO2 + H2O
Vicia sp.
-
i.e. allo-coronamic acid
-
-
?
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2
1-butene + cyanide + dehydroascorbate + CO2 + H2O
-
stereoselectivity
-
-
?
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2
1-butene + cyanide + dehydroascorbate + CO2 + H2O
-
i.e. allo-coronamic acid
-
-
?
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2 + HCO3-
1-butene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2 + HCO3-
1-butene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2 + HCO3-
1-butene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
1-amino-2-methylcyclopropane-1-carboxylate + L-ascorbate + O2
?
-
stereoselectivity
-
-
?
1-amino-2-methylcyclopropane-1-carboxylate + L-ascorbate + O2
?
-
prefers mixture of 1R,2S-amino-2-methylcyclopropane-1-carboxylate
-
-
?
1-amino-2-methylcyclopropane-1-carboxylate + L-ascorbate + O2
?
-
stereoselectivity
-
-
?
1-amino-2-methylcyclopropane-1-carboxylate + L-ascorbate + O2
?
-
prefers mixture of 1R,2S-amino-2-methylcyclopropane-1-carboxylate
-
-
?
1-amino-2-methylcyclopropane-1-carboxylate + L-ascorbate + O2
?
-
-
-
-
?
1-amino-2-methylcyclopropane-1-carboxylate + L-ascorbate + O2
?
Vicia sp.
-
stereoselectivity
-
-
?
1-amino-2-methylcyclopropane-1-carboxylate + L-ascorbate + O2
?
Vicia sp.
-
prefers mixture of 1R,2S-amino-2-methylcyclopropane-1-carboxylate
-
-
?
1-amino-2-methylcyclopropane-1-carboxylate + L-ascorbate + O2
?
-
stereoselectivity
-
-
?
1-amino-2-methylcyclopropane-1-carboxylate + L-ascorbate + O2
?
-
prefers mixture of 1R,2S-amino-2-methylcyclopropane-1-carboxylate
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
ethylene regulates fruit ripening by regulating the expression of specific genes, especially in climacteric fruits
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
absolutely dependent on CO2
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
biosynthesis of plant signalling molecule ethylene
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
absolutely dependent on CO2
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
absolutely dependent on CO2
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
biosynthesis of plant signalling molecule ethylene
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
rate-limiting, one of two key enzymes in the pathway of ethylene biosynthesis are those catalyzing the conversion of S-adenosylmethyonine to 1-aminocyclopropane-1-carboxylic acid, ACC, exogenous ethylene accelerates rimpening, endogenous induces it, enzyme expression depends on the developmental stage of the fruit and ethylene
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
last step in ethylene biosynthesis
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
catalyses the final step in ethylene biosynthesis
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
the enzyme is regulated by jasmonates
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
biosynthesis of plant signalling molecule ethylene
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
biosynthesis of plant signalling molecule ethylene
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
catalyses the final step in ethylene biosynthesis
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
kinetics and mechanism of O2 activation, the rate-determining step is the formation of an FeIV=O species, which acts as the reactive intermediate in substrate oxidation, the FeIV=O species is linked to a rate-limiting proton or hydrogen atom transfer step, overview
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
last step in the ethylene biosynthetic pathway
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
Vicia sp.
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
biosynthesis of plant signalling molecule ethylene
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
absolutely dependent on CO2
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
stereoselectivity
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
specific for the substrates
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
absolutely dependent on CO2
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
absolutely dependent on CO2
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
stereoselectivity
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
stereoselectivity
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
absolutely dependent on ascorbate
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
N-hydroxyl-1-aminocyclopropane-1-carboxylate is no intermediate
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
absolutely dependent on CO2
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
specific for 1-aminocyclopropane-1-carboxylate
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
absolutely dependent on ascorbate
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
specific for the substrates
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
Vicia sp.
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
stereoselectivity
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
1-aminocyclopropane-1-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
additional information
?
-
-
2-oxoglutarate is not required for activity
-
-
?
additional information
?
-
-
the enzyme becomes inactivated by fragmentation and apparently has intrinsic protease and transpeptidase activity
-
-
?
additional information
?
-
ACC oxidase amino acids Cys28, Thr157, Lys158, Arg175, Gln188, Lys199, Arg244, Ser246, Lys230, Lys292, Glu294, Glu297, Arg299, Phe300 and Glu301 are important residues affecting enzyme activity. alpha-Aminoisobutryric acid is an alternative substrate for enzyme ACCO producing acetone, ammonia and CO2
-
-
?
additional information
?
-
-
ACC oxidase amino acids Cys28, Thr157, Lys158, Arg175, Gln188, Lys199, Arg244, Ser246, Lys230, Lys292, Glu294, Glu297, Arg299, Phe300 and Glu301 are important residues affecting enzyme activity. alpha-Aminoisobutryric acid is an alternative substrate for enzyme ACCO producing acetone, ammonia and CO2
-
-
?
additional information
?
-
-
ascorbate is not required for O2 activation or product formation
-
-
?
additional information
?
-
-
L-galactono-gamma-lactone is no cosubstrate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
1-aminocyclopropane-1-carboxylate + ascorbate + O2 + H+
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
1-aminocyclopropane-1-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
ethylene regulates fruit ripening by regulating the expression of specific genes, especially in climacteric fruits
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
absolutely dependent on CO2
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
biosynthesis of plant signalling molecule ethylene
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
absolutely dependent on CO2
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
absolutely dependent on CO2
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
biosynthesis of plant signalling molecule ethylene
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
rate-limiting, one of two key enzymes in the pathway of ethylene biosynthesis are those catalyzing the conversion of S-adenosylmethyonine to 1-aminocyclopropane-1-carboxylic acid, ACC, exogenous ethylene accelerates rimpening, endogenous induces it, enzyme expression depends on the developmental stage of the fruit and ethylene
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
last step in ethylene biosynthesis
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
catalyses the final step in ethylene biosynthesis
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
the enzyme is regulated by jasmonates
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
biosynthesis of plant signalling molecule ethylene
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
biosynthesis of plant signalling molecule ethylene
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
catalyses the final step in ethylene biosynthesis
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
last step in the ethylene biosynthetic pathway
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
Vicia sp.
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
biosynthesis of plant signalling molecule ethylene
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
1-aminocyclopropane-1-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
?
1-aminocyclopropane-1-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
-
-
-
-
?
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114
1-amino-2-ethylcyclopropane-1-carboxylate
-
-
0.012 - 2.3
1-aminocyclopropane-1-carboxylate
0.08939 - 0.401
1-aminocyclopropane-1-carboxylic acid
1
5,6-O-isopropylidine L-ascorbate
-
recombinant enzyme, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C
14.7
alpha-aminoisobutyrate
-
recombinant enzyme, pH 7.0, 30°C
1.7
D-ascorbate
-
recombinant enzyme, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C
0.028
O2
-
recombinant isozyme ACO1, in presence of 0.5 mM L-ascorbate and 20 mM CO2/HCO3-, pH 7.2, 25°C
additional information
additional information
-
0.012
1-aminocyclopropane-1-carboxylate
recombinant isozyme ACO1, in presence of 3mM L-ascorbate, pH 7.2, 29°C
0.013
1-aminocyclopropane-1-carboxylate
recombinant isozyme ACO1, in presence of 3mM L-ascorbate, pH 7.2, 29°C
0.029
1-aminocyclopropane-1-carboxylate
recombinant isozyme ACO1, in presence of 3mM L-ascorbate and 10 mM HCO3-, pH 7.2, 29°C
0.03
1-aminocyclopropane-1-carboxylate
recombinant isozyme ACO1, in presence of 3mM L-ascorbate, pH 7.2, 29°C
0.03
1-aminocyclopropane-1-carboxylate
recombinant isozyme ACO1, in presence of 3mM L-ascorbate and 10 mM HCO3-, pH 7.2, 29°C
0.031
1-aminocyclopropane-1-carboxylate
-
mutant enzyme E301L, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.031
1-aminocyclopropane-1-carboxylate
-
mutant enzyme R299L, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.031
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant E301L, pH 7.2, 20°C
0.031
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant R299L, pH 7.2, 20°C
0.032
1-aminocyclopropane-1-carboxylate
-
recombinant enzyme, in presence of 5mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C
0.036
1-aminocyclopropane-1-carboxylate
-
mutant enzyme F300Y, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.036
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant F300Y, pH 7.2, 20°C
0.042
1-aminocyclopropane-1-carboxylate
-
recombinant mutant H177E, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C
0.046
1-aminocyclopropane-1-carboxylate
-
mutant enzyme K158R, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.046
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant K158R, pH 7.2, 20°C
0.047
1-aminocyclopropane-1-carboxylate
-
mutant enzyme R299K, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.047
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant R299K, pH 7.2, 20°C
0.051
1-aminocyclopropane-1-carboxylate
-
wild type enzyme, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.051
1-aminocyclopropane-1-carboxylate
recombinant His-tagged wild-type enzyme, pH 7.2, 20°C
0.057
1-aminocyclopropane-1-carboxylate
-
pH 6.7, 30°C
0.06
1-aminocyclopropane-1-carboxylate
-
pH 7.5, 30°C
0.06
1-aminocyclopropane-1-carboxylate
-
mutant enzyme K158Q, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.06
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant K158Q, pH 7.2, 20°C
0.062
1-aminocyclopropane-1-carboxylate
-
mutant enzyme C28A, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.062
1-aminocyclopropane-1-carboxylate
-
mutant enzyme Y251F, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.062
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant C28A, pH 7.2, 20°C
0.062
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant P298A, pH 7.2, 20°C
0.062
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant Y251F, pH 7.2, 20°C
0.063
1-aminocyclopropane-1-carboxylate
-
mutant enzyme W203F, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.063
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant W203F, pH 7.2, 20°C
0.067
1-aminocyclopropane-1-carboxylate
recombinant isozyme ACO1, in presence of 3mM L-ascorbate and 10 mM HCO3-, pH 7.2, 29°C
0.07
1-aminocyclopropane-1-carboxylate
-
mutant enzyme T157A, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.07
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant T157A, pH 7.2, 20°C
0.077
1-aminocyclopropane-1-carboxylate
-
recombinant isozyme ACO1, in presence of 0.5 mM L-ascorbate and 20 mM CO2/HCO3-, pH 7.2, 25°C
0.078
1-aminocyclopropane-1-carboxylate
-
mutant enzyme K199E, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.083
1-aminocyclopropane-1-carboxylate
-
recombinant wild-type enzyme, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C
0.083
1-aminocyclopropane-1-carboxylate
-
mutant enzyme R175K, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.083
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant R175K, pH 7.2, 20°C
0.09
1-aminocyclopropane-1-carboxylate
-
mutant enzyme F187Y, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.09
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant F187Y, pH 7.2, 20°C
0.094
1-aminocyclopropane-1-carboxylate
-
mutant enzyme R299H, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.094
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant R299H, pH 7.2, 20°C
0.121
1-aminocyclopropane-1-carboxylate
-
recombinant mutant H56Q, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C
0.129
1-aminocyclopropane-1-carboxylate
-
mutant enzyme F300Q, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.129
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant F300Q, pH 7.2, 20°C
0.132
1-aminocyclopropane-1-carboxylate
-
recombinant mutant D179E, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C
0.139
1-aminocyclopropane-1-carboxylate
-
mutant enzyme R175H, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.139
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant R175H, pH 7.2, 20°C
0.142
1-aminocyclopropane-1-carboxylate
-
mutant enzyme R175G, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.142
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant R175G, pH 7.2, 20°C
0.15
1-aminocyclopropane-1-carboxylate
-
in 50 mM MOPS, pH 7.0, at 29°C
0.158
1-aminocyclopropane-1-carboxylate
-
mutant enzyme N216F, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.158
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant N216F, pH 7.2, 20°C
0.173
1-aminocyclopropane-1-carboxylate
-
mutant enzyme K158E, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.173
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant K158E, pH 7.2, 20°C
0.175
1-aminocyclopropane-1-carboxylate
-
under atmospheric conditions, pH 7.2, 30°C
0.175
1-aminocyclopropane-1-carboxylate
-
mutant enzyme R244K, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.175
1-aminocyclopropane-1-carboxylate
-
mutant enzyme R244K/S246A, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.175
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant R244K, pH 7.2, 20°C
0.175
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant R244K/S246A, pH 7.2, 20°C
0.193
1-aminocyclopropane-1-carboxylate
-
mutant enzyme R175A, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.193
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant R175A, pH 7.2, 20°C
0.206
1-aminocyclopropane-1-carboxylate
-
mutant enzyme K158Q/R175Q, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.206
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant K158Q/R175Q, pH 7.2, 20°C
0.218
1-aminocyclopropane-1-carboxylate
-
mutant enzyme R175Q, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.218
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant R175Q, pH 7.2, 20°C
0.23
1-aminocyclopropane-1-carboxylate
-
recombinant enzyme, pH 7.0, 30°C
0.245
1-aminocyclopropane-1-carboxylate
-
mutant enzyme R244K/S246A/T157A, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.245
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant S246A/R244K/T157A , pH 7.2, 20°C
0.25
1-aminocyclopropane-1-carboxylate
at pH and °C
0.277
1-aminocyclopropane-1-carboxylate
-
mutant enzyme S246A, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.277
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant S246A, pH 7.2, 20°C
0.279
1-aminocyclopropane-1-carboxylate
-
mutant enzyme K158R/R175Q, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.279
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant K158R/R175Q, pH 7.2, 20°C
0.281
1-aminocyclopropane-1-carboxylate
-
mutant enzyme K158L, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.281
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant K158L, pH 7.2, 20°C
0.287
1-aminocyclopropane-1-carboxylate
-
mutant enzyme Q188N, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.287
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant Q188N, pH 7.2, 20°C
0.379
1-aminocyclopropane-1-carboxylate
-
mutant enzyme R175E, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.379
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant R175E, pH 7.2, 20°C
0.659
1-aminocyclopropane-1-carboxylate
-
mutant enzyme K158Q/R175E, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.659
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant K158Q/R175E, pH 7.2, 20°C
1.2
1-aminocyclopropane-1-carboxylate
-
mutant enzyme R175E/S246A, in 50 mM MOPS-HCl (pH 7.2), at 30°C
1.2
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant R175E/S246A, pH 7.2, 20°C
2.3
1-aminocyclopropane-1-carboxylate
-
mutant enzyme R175E/T157A, in 50 mM MOPS-HCl (pH 7.2), at 30°C
2.3
1-aminocyclopropane-1-carboxylate
recombinant His-tagged mutant R175E/T157A, pH 7.2, 20°C
0.08939
1-aminocyclopropane-1-carboxylic acid
-
0.2445
1-aminocyclopropane-1-carboxylic acid
-
0.401
1-aminocyclopropane-1-carboxylic acid
-
0.27
ascorbate
-
mutant S246A, pH 7.4, 30°C
0.34
ascorbate
-
mutant E109D, pH 7.4, 30°C
0.36
ascorbate
-
mutant S257A, pH 7.4, 30°C
0.38
ascorbate
-
wild-type, pH 7.4, 30°C
0.82
ascorbate
-
mutant T157A, pH 7.4, 30°C
0.82
ascorbate
-
mutant V159G, pH 7.4, 30°C
0.92
ascorbate
-
mutant S246G, pH 7.4, 30°C
0.99
ascorbate
-
mutant R244A, pH 7.4, 30°C
1.2
ascorbate
-
mutant R244K, pH 7.4, 30°C
1.25
ascorbate
-
mutant R244G, pH 7.4, 30°C
2.7
ascorbate
-
in 50 mM MOPS, pH 7.0, at 29°C
0.00029
Fe2+
-
recombinant mutant H177E, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C
0.00043
Fe2+
-
recombinant wild-type enzyme, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C
0.00047
Fe2+
-
recombinant mutant H56Q, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C
0.0046
Fe2+
-
recombinant mutant D179E, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C
0.0053
Fe2+
-
recombinant enzyme, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C
4.6
L-ascorbate
-
recombinant isozyme ACO1, in presence of 0.5 mM L-ascorbate and 20 mM CO2/HCO3-, pH 7.2, 25°C
16.7
L-ascorbate
-
recombinant enzyme, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C
additional information
additional information
-
kinetics
-
additional information
additional information
-
Km for O2 and 1-aminocyclopropane-1-carboxylate is dependent on HCO3-/CO2 concentration
-
additional information
additional information
-
Km for O2 and 1-aminocyclopropane-1-carboxylate is dependent on CO2 concentration
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
steady-state kinetics, solvent isotope effects, and competitive oxygen kinetic isotope effects, overview
-
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D179E
site-directed mutagenesis, 1% activity compared to the recombinant wild-type enzyme
G137P
site-directed mutagenesis, 98% activity compared to the recombinant wild-type enzyme
H177Q
site-directed mutagenesis, 1% activity compared to the recombinant wild-type enzyme
K158A
site-directed mutagenesis, 1% activity compared to the recombinant wild-type enzyme
K158C
site-directed mutagenesis, 1% activity compared to the recombinant wild-type enzyme
K172A
site-directed mutagenesis, 85% activity compared to the recombinant wild-type enzyme
K172C
site-directed mutagenesis, 64% activity compared to the recombinant wild-type enzyme
G289S
the enzyme activity of the mutant is 3times as high as that of the wild type enzyme
H216D
the mutant shows 76% of wild type activity
H216D/D218E
the mutant shows 78% of wild type activity
H216D/D218E/H273Q
the mutant does not completely lose catalytic activity
H273Q
the mutant shows 62% of wild type activity
R287G
the activity of the mutant is remarkably decreased to nearly 40% compared to the wild type enzyme
C283A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
C28A
-
the mutant shows increased activity compared to the wild type enzyme
K230E
-
the mutant shows reduced activity compared to the wild type enzyme
K230W
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R175E/S146A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R175E/S246A
-
the mutant shows reduced activity compared to the wild type enzyme
R244A
-
enzymic activity about 20% of wild-type
R244G
-
enzymic activity about 20% of wild-type
R244K/S246A/T157A
-
the mutant shows reduced activity compared to the wild type enzyme
S246A/R244K/T157A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S246F
-
enzymic activity less than 5% of wild-type
S246G
-
enzymic activity about 50% of wild-type
S246T
-
enzymic activity less than 5% of wild-type
S246Y
-
enzymic activity less than 5% of wild-type
S257A
-
KM-value similar to wild-type
V159G
-
enzymic activity about 30% of wild-type
D179E
-
site-directed mutagenesis, very low activity, stimulation by bicarbonate
D179N
-
site-directed mutagenesis, no activity
H177D
-
site-directed mutagenesis, no activity
H177D/D179E
-
site-directed mutagenesis, no activity
H177E
-
site-directed mutagenesis, very low activity, stimulation by bicarbonate
H177Q
-
site-directed mutagenesis, no activity
H211Q
-
site-directed mutagenesis, slightly reduced activity
H234D
-
site-directed mutagenesis, no activity
H234E
-
site-directed mutagenesis, no activity
H234Q
-
site-directed mutagenesis, no activity
H39Q
-
site-directed mutagenesis, slightly reduced activity
H56Q
-
site-directed mutagenesis, activity similar to the wild-type
H94Q
-
site-directed mutagenesis, slightly reduced activity
C133A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
C133A
-
the mutant showsincreased activity compared to the wild type enzyme
C133P
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
C133P
-
the mutant shows slightly increased activity compared to the wild type enzyme
C165A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
C165A
-
the mutant shows reduced activity compared to the wild type enzyme
E294F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E294F
-
the mutant shows reduced activity compared to the wild type enzyme
E297L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E297L
-
the mutant shows strongly increased activity compared to the wild type enzyme
E301D
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E301D
-
the mutant shows reduced activity compared to the wild type enzyme
E301L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E301L
-
the mutant shows reduced activity compared to the wild type enzyme
F187Y
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
F187Y
-
the mutant shows increased activity compared to the wild type enzyme
F300Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F300Q
-
the mutant shows reduced activity compared to the wild type enzyme
F300Y
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F300Y
-
the mutant shows reduced activity compared to the wild type enzyme
K144E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K144E
-
the mutant shows reduced activity compared to the wild type enzyme
K158E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K158E
-
the mutant shows reduced activity compared to the wild type enzyme
K158L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K158L
-
the mutant shows reduced activity compared to the wild type enzyme
K158Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K158Q
-
the mutant shows reduced activity compared to the wild type enzyme
K158Q/R175E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K158Q/R175E
-
the mutant shows reduced activity compared to the wild type enzyme
K158Q/R175Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K158Q/R175Q
-
the mutant shows reduced activity compared to the wild type enzyme
K158R
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K158R
-
the mutant shows reduced activity compared to the wild type enzyme
K158R/R175Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K158R/R175Q
-
the mutant shows reduced activity compared to the wild type enzyme
K172E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K172E
-
the mutant shows reduced activity compared to the wild type enzyme
K199E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K199E
-
the mutant shows reduced activity compared to the wild type enzyme
K230Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K230Q
-
the mutant shows reduced activity compared to the wild type enzyme
K230R
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K230R
-
the mutant shows reduced activity compared to the wild type enzyme
K292E
-
the mutant shows reduced activity compared to the wild type enzyme
K292E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme. The low residual activity of the Lys292Glu mutant is typically activated by bicarbonate
K292R
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K292R
-
the mutant shows reduced activity compared to the wild type enzyme
K296E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K296E
-
the mutant shows increased activity compared to the wild type enzyme
N216F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N216F
-
the mutant shows reduced activity compared to the wild type enzyme
P298A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
P298A
-
the mutant shows strongly increased activity compared to the wild type enzyme
Q188A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q188A
-
the mutant shows reduced activity compared to the wild type enzyme
Q188K
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q188K
-
the mutant shows reduced activity compared to the wild type enzyme
Q188N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q188N
-
the mutant shows reduced activity compared to the wild type enzyme
R175A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R175A
-
the mutant shows reduced activity compared to the wild type enzyme
R175E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R175E
-
the mutant shows reduced activity compared to the wild type enzyme
R175E/R244K
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R175E/R244K
-
the mutant shows reduced activity compared to the wild type enzyme
R175E/T157A
site-directed mutagenesis, almost inactive mutant
R175E/T157A
-
the mutant shows reduced activity compared to the wild type enzyme
R175G
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R175G
-
the mutant shows reduced activity compared to the wild type enzyme
R175H
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R175H
-
the mutant shows reduced activity compared to the wild type enzyme
R175K
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R175K
-
the mutant shows reduced activity compared to the wild type enzyme
R175Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R175Q
-
the mutant shows reduced activity compared to the wild type enzyme
R244K
-
enzymic activity about 20% of wild-type
R244K
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R244K
-
the mutant is less active than the native enzyme and has a 5fold higher Km value for 1-aminocyclopropane-1-carboxylate
R244K/S246A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R244K/S246A
-
the mutant shows reduced activity compared to the wild type enzyme
R244K/T157A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R244K/T157A
-
the mutant shows reduced activity compared to the wild type enzyme
R299E
-
inactive
R299E
site-directed mutagenesis, inactive mutant
R299H
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R299H
-
the mutant shows reduced activity compared to the wild type enzyme
R299K
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R299K
-
the mutant shows reduced activity compared to the wild type enzyme
R299L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R299L
-
the mutant shows reduced activity compared to the wild type enzyme
S246A
-
enzymic activity about 50% of wild-type
S246A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S246A
-
the mutant is less active than the native enzyme and has a 3fold higher Km value for 1-aminocyclopropane-1-carboxylate
T157A
-
enzymic activity about 40% of wild-type
T157A
-
the mutation does not affect the Km for 1-aminocyclopropane-1-carboxylate but drastically reduces enzyme activity
T157A
site-directed mutagenesis, the single-point mutation does not affect the substrate 1-aminocyclopropane-1-carboxylate Km but drastically reduces enzyme ACCO activity
W203F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W203F
-
the mutant shows reduced activity compared to the wild type enzyme
Y251F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y251F
-
the mutant shows reduced activity compared to the wild type enzyme
additional information
antisense expression of the enzyme in Petunia x hybrida leads to delayed flower senescence and reduced ethylene production in transgenic shoots, overview
additional information
-
enzyme suppression leads to reduction in ethylene and CO2 production in transgenic fruits, which do not show an altered growth phenotype but no climacteric phenotype compared to the wild-type plants, overview
additional information
isozyme ACO1 knockout by expression of specific RNAi in calli via Agrobacterium tumefaciens strain LBA 4404 transformation method and regeneration of transgenic plants
additional information
isozyme ACO1 knockout by expression of specific RNAi in calli via Agrobacterium tumefaciens strain LBA 4404 transformation method and regeneration of transgenic plants
additional information
isozyme ACO2 knockout by expression of specific RNAi in calli via Agrobacterium tumefaciens strain LBA 4404 transformation method and regeneration of transgenic plants
additional information
isozyme ACO2 knockout by expression of specific RNAi in calli via Agrobacterium tumefaciens strain LBA 4404 transformation method and regeneration of transgenic plants
additional information
-
expression of the antisense enzyme construct in the male parental line of Galia, co-transformation using the Agrobacterium tumefaciens system with antisense CMACO-1 and CP4 genes, phenotype with reduced growth and latered fruit properties, overview
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Dong, J.G.; Fernandez-Maculet, J.C.; Yang, S.F.
Purification and characterization of 1-aminocyclopropane-1-carboxylate oxidase from apple fruit
Proc. Natl. Acad. Sci. USA
89
9789-9793
1992
Malus domestica
brenda
Fernandez-Maculet, J.C.; Dong, J.G.; Yang, S.F.
Activation of 1-aminocyclopropane-1-carboxylate oxidase by carbon dioxide
Biochem. Biophys. Res. Commun.
193
1168-1173
1993
Malus domestica
brenda
Smith, J.J.; John, P.
Activation of 1-aminocyclopropane-1-carboxylate oxidase by bicarbonate/carbon dioxide
Phytochemistry
32
1381-1386
1993
Cucumis melo
-
brenda
Hyodo, H.; Hashimoto, C.; Morozumi, S.; Hu, W.; Tanaka, K.
Characterization and induction of the activity of 1-aminocyclopropane-1-carboxylate oxidase in the wounded mesocarp tissue of Cucurbita maxima
Plant Cell Physiol.
34
667-671
1993
Cucurbita maxima
-
brenda
Finlayson, S.A.; Reid, D.M.
Influence of CO2 on ACC oxidase activity from roots of sunflower (Helianthus annuus) seedlings
Phytochemistry
35
847-851
1994
Helianthus annuus
-
brenda
Zhang, Z.; Schofield, C.J.; Baldwin, J.E.; Thomas, P.; John, P.
Expression, purification and characterization of 1-aminocyclopropane-1-carboxylate oxidase from tomato in Escherichia coli
Biochem. J.
307
77-85
1995
Solanum lycopersicum
-
brenda
Mizutani, F.; Dong, J.G.; Yang, S.F.
Effect of pH on CO2-activated 1-aminocyclopropane-1-carboxylate oxidase activity from apple fruit
Phytochemistry
39
751-755
1995
Malus domestica
-
brenda
Lay, V.J.; Prescott, A.G.; Thomas, P.G.; John, P.
Heterologous expression and site-directed mutagenesis of the 1-aminocyclopropane-1-carboxylate oxidase from kiwi fruit
Eur. J. Biochem.
242
228-234
1996
Actinidia deliciosa (P31237), Actinidia deliciosa
brenda
Zhang, Z.H.; Barlow, J.N.; Baldwin, J.E.; Schofield, C.J.
Metal-catalyzed oxidation and mutagenesis studies on the iron(II) binding site of 1-aminocyclopropane-1-carboxylate oxidase
Biochemistry
36
15999-16007
1997
Solanum lycopersicum
brenda
Finlayson, S.A.; Reid, D.M.; Morgan, P.W.
Root and leaf specific ACC oxidase activity in corn and sunflower seedlings
Phytochemistry
45
869-877
1997
Helianthus annuus, Zea mays
-
brenda
Vioque, B.; Castellano, J.M.
In vivo and in vitro 1-aminocyclopropane-1-carboxylic acid oxidase activity in pear fruit: role of ascorbate and inactivation during catalysis
J. Agric. Food Chem.
46
1706-1711
1998
Pyrus communis
brenda
Yu, S.J.; Kim, S.; Lee, J.S.; Lee, D.H.
Differential accumulation of transcripts for ACC synthase and ACC oxidase homologs in etiolated mung bean hypocotyls in response to various stimuli
Mol. Cells
8
350-358
1998
Vigna radiata
brenda
Bidonde, S.; Ferrer, M.A.; Zegzouti, H.; Ramassamy, S.; Latche, A.; Pech, J.C.; Hamilton, A.J.; Grierson, D.; Bouzayen, M.
Expression and characterization of three tomato 1-aminocyclopropane-1-carboxylate oxidase cDNAs in yeast
Eur. J. Biochem.
253
20-26
1998
Solanum lycopersicum (P05116), Solanum lycopersicum (P07920), Solanum lycopersicum (P24157), Solanum lycopersicum
brenda
Pirrung, M.C.
Ethylene biosynthesis from 1-aminocyclopropanecarboxylic acid
Acc. Chem. Res.
32
711-718
1999
Cucumis melo, Solanum lycopersicum, Malus domestica, Vigna radiata, Vicia sp.
-
brenda
Charng, Y.; Chou, S.J.; Jiaang, W.T.; Chen, S.T.; Yang, S.F.
The catalytic mechanism of 1-aminocyclopropane-1-carboxylic acid oxidase
Arch. Biochem. Biophys.
385
179-185
2001
Malus domestica
brenda
Thrower, J.S.; Blalock, R.; Klinman, J.P.
Steady-state kinetics of substrate binding and iron release in tomato ACC oxidase
Biochemistry
40
9717-9724
2001
Solanum lycopersicum
brenda
Vioque, B.; Castellano, J.M.
Extraction and biochemical characterization of 1-aminocyclopropane-1-carboxylic acid oxidase from pear
Physiol. Plant.
90
334-338
1994
Pyrus communis
-
brenda
Seo, Y.S.; Yoo, A.; Jung, J.; Sung, S.K.; Yang, D.R.; Kim, W.T.; Lee, W.
The active site and substrate-binding mode of 1-aminocyclopropane-1-carboxylate oxidase determined by site-directed mutagenesis and comparative modeling studies
Biochem. J.
380
339-346
2004
Malus domestica
brenda
Zhang, Z.; Ren, J.S.; Clifton, I.J.; Schofield, C.J.
Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase--the ethylene-forming enzyme
Chem. Biol.
11
1383-1394
2004
Petunia x hybrida
brenda
Tierney, D.L.; Rocklin, A.M.; Lipscomb, J.D.; Que, L.Jr.; Hoffman, B.M.
ENDOR studies of the ligation and structure of the non-heme iron site in ACC oxidase
J. Am. Chem. Soc.
127
7005-7013
2005
Nicotiana tabacum
brenda
Rocklin, A.M.; Kato, K.; Liu, H.W.; Que, L.Jr.; Lipscomb, J.D.
Mechanistic studies of 1-aminocyclopropane-1-carboxylic acid oxidase: single turnover reaction
J. Biol. Inorg. Chem.
9
171-182
2004
Persea americana
brenda
Zheng, Q.L.; Nakatsuka, A.; Itamura, H.
Extraction and characterization of 1-aminocyclopropane-1-carboxylic acid (ACC) synthase and ACC oxidase from wounded persimmon fruit
J. Jpn. Soc. Hort. Sci.
74
159-166
2005
Diospyros kaki
-
brenda
Scott, R.W.; McManus, M.T.
Cloning of the full-length ACC oxidase isoform TR-ACO1 from white clover and expression as a recombinant protein
NATO Sci. Ser. Ser. I
349
76-77
2003
Trifolium repens
-
brenda
Rodriguez-Gacio, M.D.C.; Nicolas, C.; Matilla, A.J.
The final step of the ethylene biosynthesis pathway in turnip tops (Brassica rapa): Molecular characterization of the 1-aminocyclopropane-1-carboxylate oxidase BrACO1 throughout zygotic embryogenesis and germination of heterogeneous seeds
Physiol. Plant.
121
132-140
2004
Brassica rapa
brenda
Woltering, E.J.; Balk, P.A.; Nijenhuis-de Vries, M.A.; Faivre, M.; Ruys, G.; Somhorst, D.; Philosoph-Hadas, S.; Friedman, H.
Regulation and role of differential ethylene biosynthesis in gravistimulated Antirrhinum majus L. cut flower stems
Acta Hortic.
669
213-218
2005
Antirrhinum majus, Antirrhinum majus L.
-
brenda
Win, T.O.; Srilaong, V.; Kyu, K.L.; Kanlayanarat, S.
An increase in the activity of 1-aminocyclopropene 1-carboxylic acid (ACC) oxidase is associated with yellowing of lime fruit (Citrus aurantifolia, Swingle cv. "Paan")
Acta Hortic.
712
879-884
2006
Citrus aurantiifolia
-
brenda
Gapper, N.E.; Coupe, S.A.; McKenzie, M.J.; Scott, R.W.; Christey, M.C.; Lill, R.E.; McManus, M.T.; Jameson, P.E.
Senescence-associated down-regulation of 1-aminocyclopropane-1-carboxylate (ACC) oxidase delays harvest-induced senescence in broccoli
Funct. Plant Biol.
32
891-901
2005
Brassica oleracea
brenda
Murti, G.S.; Upreti, K.K.
Effects of paclobutrazol on leaf water potential, ethylene production, ACC, ACC-oxidase and polyamines in mango seedlings
J. Plant Biol.
32
183-188
2005
Mangifera indica
-
brenda
Higgins, J.D.; Newbury, H.J.; Barbara, D.J.; Muthumeenakshi, S.; Puddephat, I.J.
The Production of Marker-Free Genetically Engineered Broccoli with Sense and Antisense ACC synthase 1 and ACC oxidases 1 and 2 to Extend Shelf-Life
Mol. Breed.
17
7-20
2006
Brassica oleracea
brenda
Chen, B.C.; McManus, M.T.
Expression of 1-aminocyclopropane-1-carboxylate (ACC) oxidase genes during the development of vegetative tissues in white clover (Trifolium repens L.) is regulated by ontological cues
Plant Mol. Biol.
60
451-467
2006
Trifolium repens
brenda
Hudgins, J.W.; Ralph, S.G.; Franceschi, V.R.; Bohlmann, J.
Ethylene in induced conifer defense: cDNA cloning, protein expression, and cellular and subcellular localization of 1-aminocyclopropane-1-carboxylate oxidase in resin duct and phenolic parenchyma cells
Planta
224
865-877
2006
Picea glauca, Pseudotsuga menziesii (Q1HK31), Picea sitchensis (Q1HK33), Picea sitchensis
brenda
Lagunes, L.; Tovar, B.; Mata, M.; Vinay-Vadillo, J.C.; De La Cruz, J.; Garcia, H.S.
Effect of exogenous ethylene on ACC content and ACC oxidase activity during ripening of Manila mangoes subjected to hot water treatment
Plant Foods Hum. Nutr.
62
157-163
2007
Mangifera indica
brenda
Yangkhamman, P.; Tanase, K.; Ichimura, K.; Fukai, S.
Depression of enzyme activities and gene expression of ACC synthase and ACC oxidase in cut carnation flowers under high-temperature conditions
Plant Growth Regul.
53
155-162
2007
Dianthus caryophyllus
-
brenda
Nunez-Palenius, H.G.; Klee, H.J.; Huber, D.J.; Cantliffe, D.J.
A single insertion of ACC oxidase gene in antisense orientation extends the shelf life in muskmelon "Galia" hybrid parental line (Cucumis melo L. var. reticulatus Ser.)
Acta Hortic.
731
421-426
2007
Cucumis melo
-
brenda
Callahan, A.; Scorza, R.
Effects of a peach antisense ACC oxidase gene on plum fruit quality
Acta Hortic.
738
567-573
2007
Prunus persica
-
brenda
Hu, W.Z.; Jiang, A.L.; Qi, H.P.; Pang, K.
Changes in wound-induced ethylene production and ACC oxidase in fresh-cut squash
Acta Hortic.
746
357-361
2007
Cucurbita maxima
-
brenda
Tao, L.; Dong, H.J.; Chen, X.; Chen, S.F.; Wang, T.H.
Expression of ethylene-forming enzyme (EFE) of Pseudomonas syringae pv. glycinea in Trichoderma viride
Appl. Microbiol. Biotechnol.
80
573-578
2008
Pseudomonas syringae (A1Z3B9)
brenda
Kondo, S.; Yamada, H.; Setha, S.
Effect of jasmonates differed at fruit ripening stages on 1-aminocyclopropane-1-carboxylate (ACC) synthase and ACC oxidase gene expression in pears
J. Am. Soc. Hort. Sci.
132
120-125
2007
Pyrus communis
-
brenda
Momonoi, K.; Shoji, K.; Yoshida, K.
Cloning and characterization of ACC oxidase genes from tulip
Plant Biotechnol.
24
241-246
2007
Tulipa gesneriana (Q400P0), Tulipa gesneriana (Q400U7), Tulipa gesneriana (Q400U9), Tulipa gesneriana (Q400V0), Tulipa gesneriana (Q75QN1)
-
brenda
Huang, L.; Lai, U.; Yang, S.; Chu, M.; Kuo, C.; Tsai, M.; Sun, C.
Delayed flower senescence of Petunia hybrida plants transformed with antisense broccoli ACC synthase and ACC oxidase genes
Postharvest Biol. Technol.
46
47-53
2007
Brassica oleracea (Q43404)
-
brenda
Mirica, L.M.; Klinman, J.P.
The nature of O2 activation by the ethylene-forming enzyme 1-aminocyclopropane-1-carboxylic acid oxidase
Proc. Natl. Acad. Sci. USA
105
1814-1819
2008
Solanum lycopersicum
brenda
Lopez-Gomez, R.; Cabrera-Ponce, J.L.; Saucedo-Arias, L.J.; Carreto-Montoya, L.; Villanueva-Arce, R.; Diaz-Perez, J.C.; Gomez-Lim, M.A.; Herrera-Estrella, L.
Ripening in papaya fruit is altered by ACC oxidase cosuppression
Transgenic Res.
18
89-97
2009
Carica papaya
brenda
Mirica, L.M.; McCusker, K.P.; Munos, J.W.; Liu, H.W.; Klinman, J.P.
18O kinetic isotope effects in non-heme iron enzymes: probing the nature of Fe/O2 intermediates
J. Am. Chem. Soc.
130
8122-8123
2008
plant, Solanum tuberosum
brenda
Pan, G.; Lou, C.
Isolation of an 1-aminocyclopropane-1-carboxylate oxidase gene from mulberry (Morus alba L.) and analysis of the function of this gene in plant development and stresses response
J. Plant Physiol.
165
1204-1213
2008
Morus alba (Q0PNH5)
brenda
Binnie, J.E.; McManus, M.T.
Characterization of the 1-aminocyclopropane-1-carboxylic acid (ACC) oxidase multigene family of Malus domestica Borkh
Phytochemistry
70
348-360
2009
Malus domestica, Malus domestica (O48882), Malus domestica (Q00985)
brenda
Gallie, D.R.; Geisler-Lee, J.; Chen, J.; Jolley, B.
Tissue-specific expression of the ethylene biosynthetic machinery regulates root growth in maize
Plant Mol. Biol.
69
195-211
2009
Zea mays
brenda
Roeder, S.; Dreschler, K.; Wirtz, M.; Cristescu, S.M.; van Harren, F.J.; Hell, R.; Piechulla, B.
SAM levels, gene expression of SAM synthetase, methionine synthase and ACC oxidase, and ethylene emission from N. suaveolens flowers
Plant Mol. Biol.
70
535-546
2009
Nicotiana suaveolens (Q069K4), Nicotiana suaveolens
brenda
Kondo, S.; Meemak, S.; Ban, Y.; Moriguchi, T.; Harada, T.
Effects of auxin and jasmonates on 1-aminocyclopropane-1-carboxylate (ACC) synthase and ACC oxidase gene expression during ripening of apple fruit
Postharvest Biol. Technol.
51
281-284
2009
Malus sylvestris
-
brenda
Smith, J.; Ververidis, P.; John, P.
Characterization of the ethylene-forming enzyme partially purified from melon
Phytochemistry
31
1485-1494
1992
Cucumis melo
-
brenda
Iwamoto, M.; Baba-Kasai, A.; Kiyota, S.; Hara, N.; Takano, M.
ACO1, a gene for aminocyclopropane-1-carboxylate oxidase: Effects on internode elongation at the heading stage in rice
Plant Cell Environ.
33
805-815
2010
Oryza sativa
brenda
Takahashi, H.; Shinkawa, T.; Nakai, S.; Inoue, Y.
Differential expression of ACC oxidase genes during low-pH-induced root hair formation in lettuce (Lactuca sativa L.) seedlings
Plant Growth Regul.
62
137-149
2010
Lactuca sativa (B9A0T8), Lactuca sativa (B9A0T9), Lactuca sativa (B9A0U0)
-
brenda
Dorling, S.J.; Leung, S.; Anderson, C.W.; Albert, N.W.; McManus, M.T.
Changes in 1-aminocyclopropane-1-carboxlate (ACC) oxidase expression and enzyme activity in response to excess manganese in white clover (Trifolium repens L.)
Plant Physiol. Biochem.
49
1013-1019
2011
Trifolium repens (Q9XER3), Trifolium repens
brenda
Huang, S.; Sawaki, T.; Takahashi, A.; Mizuno, S.; Takezawa, K.; Matsumura, A.; Yokotsuka, M.; Hirasawa, Y.; Sonoda, M.; Nakagawa, H.; Sato, T.
Melon EIN3-like transcription factors (CmEIL1 and CmEIL2) are positive regulators of an ethylene- and ripening-induced 1-aminocyclopropane-1-carboxylic acid oxidase gene (CM-ACO1)
Plant Sci.
178
251-257
2010
Cucumis melo, Cucumis melo cv. Andes
brenda
Dilley, D.R.; Wang, Z.; Kadirjan-Kalbach, D.K.; Ververidis, F.; Beaudry, R.; Padmanabhan, K.
1-Aminocyclopropane-1-carboxylic acid oxidase reaction mechanism and putative post-translational activities of the ACCO protein
AoB plants
5
plt031
2013
Malus domestica
brenda
Meng, D.; Shen, L.; Yang, R.; Zhang, X.; Sheng, J.
Identification and active site analysis of the 1-aminocyclopropane-1-carboxylic acid oxidase catalysing the synthesis of ethylene in Agaricus bisporus
Biochim. Biophys. Acta
1840
120-128
2014
Agaricus bisporus (H9ZYN5), Agaricus bisporus
brenda
Brisson, L.; El Bakkali-Taheri, N.; Giorgi, M.; Fadel, A.; Kaizer, J.; Reglier, M.; Tron, T.; Ajandouz, e.l..H.; Simaan, A.J.
1-Aminocyclopropane-1-carboxylic acid oxidase: insight into cofactor binding from experimental and theoretical studies
J. Biol. Inorg. Chem.
17
939-949
2012
Solanum lycopersicum
brenda
Yu, M.; Shen, L.; Zhang, A.; Sheng, J.
Methyl jasmonate-induced defense responses are associated with elevation of 1-aminocyclopropane-1-carboxylate oxidase in Lycopersicon esculentum fruit
J. Plant Physiol.
168
1820-1827
2011
Solanum lycopersicum (A4ZYQ6), Solanum lycopersicum (P05116), Solanum lycopersicum (P24157), Solanum lycopersicum (Q9ZWP2), Solanum lycopersicum
brenda
Kondo, S.; Tomiyama, H.; Kittikorn, M.; Okawa, K.; Ohara, H.; Yokoyama, M.; Ifuku, O.; Saito, T.; Ban, Y.; Tatsuki, M.; Moriguchi, T.; Murata, A.; Watanabe, N.
Ethylene production and 1-aminocyclopropane-1-carboxylate (ACC) synthase and ACC oxidase gene expression in apple fruit are affected by 9,10-ketol-octadecadienoic acid (KODA)
Postharvest Biol. Technol.
72
20-26
2012
Malus sylvestris
-
brenda
Dilley, D.R.; Wang, Z.; Kadirjan-Kalbach, D.K.; Ververidis, F.; Beaudry, R.; Padmanabhan, K.
1-Aminocyclopropane-1-carboxylic acid oxidase reaction mechanism and putative post-translational activities of the ACCO protein
AoB Plants
5
plt03
2013
Malus domestica (Q00985), Malus domestica
brenda
Chersicola, M.; Kladnik, A.; Tu?ek ?nidari?, M.; Mrak, T.; Gruden, K.; Dermastia, M.
1-Aminocyclopropane-1-carboxylate oxidase induction in tomato flower pedicel phloem and abscission related processes are differentially sensitive to ethylene
Front. Plant Sci.
8
464
2017
Solanum lycopersicum (P05116), Solanum lycopersicum (P24157), Solanum lycopersicum
brenda
Xiao, G.; Li, L.; Teng, K.; Chao, Y.; Han, L.
Cloning and expression of the 1-aminocyclopropane-1-carboxylic oxidase gene from agrostis stolonifera
Genet. Mol. Res.
15
gmr15049034
2016
Agrostis stolonifera (A0A161G0R4), Agrostis stolonifera
brenda
Kosugi, Y.; Matsuoka, A.; Higashi, A.; Toyohara, N.; Satoh, S.
2-Aminooxyisobutyric acid inhibits the in vitro activities of both 1-aminocyclopropane-1-carboxylate (ACC) synthase and ACC oxidase in ethylene biosynthetic pathway and prolongs vase life of cut carnation flowers
J. Plant Biol.
57
218-224
2014
Dianthus caryophyllus (P31528)
-
brenda
Sekeli, R.; Abdullah, J.; Namasivayam, P.; Muda, P.; Bakar, U.; Yeong, W.; Pillai, V.
RNA interference of 1-aminocyclopropane-1-carboxylic acid oxidase (ACO1 and ACO2) genes expression prolongs the shelf life of eksotika (Carica papaya L.) papaya fruit
Molecules
19
8350-8362
2014
Carica papaya (Q5WM32), Carica papaya (Q8W2D6)
-
brenda
Datta, R.; Kumar, D.; Sultana, A.; Hazra, S.; Bhattacharyya, D.; Chattopadhyay, S.
Glutathione regulates 1-aminocyclopropane-1-carboxylate synthase transcription via WRKY33 and 1-aminocyclopropane-1-carboxylate oxidase by modulating messenger RNA stability to induce ethylene synthesis during stress
Plant Physiol.
169
2963-2981
2015
Arabidopsis thaliana (Q42560), Arabidopsis thaliana Col-0 (Q42560)
brenda