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EC Tree
IUBMB Comments A nonheme iron enzyme. Requires CO2 for activity. In the enzyme from plants, the ethene has signalling functions such as stimulation of fruit-ripening.
The taxonomic range for the selected organisms is: Solanum lycopersicum The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
acc oxidase, ethylene-forming enzyme, 1-aminocyclopropane-1-carboxylic acid oxidase, 1-aminocyclopropane-1-carboxylate oxidase, acc-oxidase, leaco1, md-aco1, asaco, leaco4, md-aco3,
more
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1-aminocyclopropane-1-carboxylate oxidase
-
1-aminocyclopropane-1-carboxylate oxidase
-
1-aminocyclopropane-1-carboxylic acid oxidase
-
-
oxidase, aminocyclopropanecarboxylate
-
-
-
-
ACC oxidase
-
-
-
-
ethylene-forming enzyme
-
-
-
-
ethylene-forming enzyme
-
-
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1-aminocyclopropane-1-carboxylate + ascorbate + O2 = ethene + cyanide + dehydroascorbate + CO2 + 2 H2O
1-aminocyclopropane-1-carboxylate + ascorbate + O2 = ethene + cyanide + dehydroascorbate + CO2 + 2 H2O
reaction mechanism
-
1-aminocyclopropane-1-carboxylate + ascorbate + O2 = ethene + cyanide + dehydroascorbate + CO2 + 2 H2O
catalytic mechanism
-
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oxidative decarboxylation
-
-
-
-
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1-aminocyclopropane-1-carboxylate oxygenase (ethylene-forming)
A nonheme iron enzyme. Requires CO2 for activity. In the enzyme from plants, the ethene has signalling functions such as stimulation of fruit-ripening.
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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 + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
i.e. ACC
-
?
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2
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
additional information
?
-
-
L-galactono-gamma-lactone is no cosubstrate
-
-
?
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-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-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
-
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 + 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
-
?
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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 + 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 + 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
-
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
-
?
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ascorbate
-
ascorbate
-
-
ascorbate
-
best at 20 mM, kinetics, overview
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Fe2+
-
-
Fe2+
-
a single bound Fe2+ per monomer
Fe2+
-
iron binding ligands are His177, Asp179, His234
Fe2+
-
kinetic role in catalysis forming oxygen complexes, overview
Fe2+
-
a nonheme Fe(II)-containing enzyme
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2-aminoisobutyric acid
competitive inhibitor
n-propyl gallate
free-radical scavenger
(1-amino-1-methyl)ethylphosphonic acid
-
competitive inhibitor versus both 1-aminocyclopropane-1-carboxylate and bicarbonate
1-aminocyclopropane-1-carboxylate
-
slight inhibition at high concentration
1-aminocyclopropane-1-phosphonic acid
-
competitive inhibitor versus both 1-aminocyclopropane-1-carboxylate and bicarbonate
2-aminoisobutyric acid
competitive inhibitor
alpha-aminoisobutyric acid
competitive inhibitor
diethyl dicarbonate
-
complete inactivation at 1.5 mM, pH 6.8, after 20 min
n-propyl gallate
free-radical scavenger
Zn2+
-
competitive to Fe2+
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ascorbate
3 isozymes: absolutely dependent on invitro, no requirement in vivo
CO2
absolutely dependent on
methyl jasmonate
0.02 mM methyl jasmonate increases the activity of the enzyme to 148%. 0.2 mM and 1.0 mM methyl jasmonate increases enzyme activity by 46% and 47%, while 0.05 mM induces a smaller elevation of activity by 21% in tomato fruits
bicarbonate
-
the enzyme requires the presence of CO2 or bicarbonate for activity
bovine serum albumin
-
stimulates the recombinant enzyme by 41% at 0.1 mM
-
catalase
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recombinant enzyme, stimulates by 36% at 0.5 mg/ml
-
dithiothreitol
-
recombinant enzyme, stimulates by 38% at 1 mM
methyl jasmonate
0.02 mM methyl jasmonate increases the activity of the enzyme to 148%. 0.2 mM and 1.0 mM methyl jasmonate increases enzyme activity by 46% and 47%, while 0.05 mM induces a smaller elevation of activity by 21% in tomato fruits
additional information
-
no activation by bisulfite, isozyme AOC1
-
ascorbate
-
required
ascorbate
3 isozymes: absolutely dependent on invitro, no requirement in vivo
ascorbate
-
cannot be replaced by DTT or NADH
CO2
-
-
CO2
absolutely dependent on
CO2
-
requires HCO3-/CO2 mixture
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0.013 - 0.03
1-aminocyclopropane-1-carboxylate
0.012 - 0.15
1-aminocyclopropane-1-carboxylate
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
2.7
ascorbate
-
in 50 mM MOPS, pH 7.0, at 29°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
-
steady-state kinetics, solvent isotope effects, and competitive oxygen kinetic isotope effects, overview
-
0.013
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
0.012
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
0.032
1-aminocyclopropane-1-carboxylate
-
recombinant enzyme, in presence of 5mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°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
0.067
1-aminocyclopropane-1-carboxylate
recombinant isozyme ACO1, in presence of 3mM L-ascorbate and 10 mM HCO3-, pH 7.2, 29°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
0.083
1-aminocyclopropane-1-carboxylate
-
recombinant wild-type enzyme, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C
0.121
1-aminocyclopropane-1-carboxylate
-
recombinant mutant H56Q, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C
0.132
1-aminocyclopropane-1-carboxylate
-
recombinant mutant D179E, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C
0.15
1-aminocyclopropane-1-carboxylate
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00867 - 5.9
1-aminocyclopropane-1-carboxylate
0.2
ascorbate
-
in 50 mM MOPS, pH 7.0, at 29°C
0.00867
1-aminocyclopropane-1-carboxylate
-
recombinant mutant D179E, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C
0.0095
1-aminocyclopropane-1-carboxylate
-
recombinant mutant H177E, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C
0.19
1-aminocyclopropane-1-carboxylate
-
in 50 mM MOPS, pH 7.0, at 29°C
0.223
1-aminocyclopropane-1-carboxylate
-
pH 7.2, 25°C, 2 mM ascorbate, recombinant enzyme
0.612
1-aminocyclopropane-1-carboxylate
-
pH 7.2, 25°C, 20 mM ascorbate, recombinant enzyme
5.17
1-aminocyclopropane-1-carboxylate
-
recombinant mutant H56Q, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C
5.9
1-aminocyclopropane-1-carboxylate
-
recombinant wild-type enzyme, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2.3
(1-amino-1-methyl)ethylphosphonic acid
-
in 50 mM MOPS, pH 7.0, at 29°C
38.9
1-aminocyclopropane-1-carboxylate
-
recombinant isozyme ACO1, in presence of 5 mM L-ascorbate and 20 mM CO2/HCO3-, pH 7.2, 25°C
1.5
1-aminocyclopropane-1-phosphonic acid
-
in 50 mM MOPS, pH 7.0, at 29°C
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0.012
partially purified recombinant isozyme ACO3
0.003
partially purified recombinant isozyme ACO2
0.025
partially purified recombinant isozyme ACO1
additional information
-
-
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cultivar Lichun
SwissProt
brenda
cv. VF36, formerly Lycopersicon esculentum
SwissProt
brenda
isozyme ACO3
SwissProt
brenda
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vascular tissues in the pedicel, the main expression site of LeACO1 is in cell layers just outside the flower pedicel abscission zone in its proximal and distal part
brenda
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brenda
vascular tissues in the pedicel, the main expression site of LeACO1 is in cell layers just outside the flower pedicel abscission zone in its proximal and distal part
brenda
vascular tissues in the pedicel, the main expression site of LeACO1 is in cell layers just outside the flower pedicel abscission zone in its proximal and distal part
brenda
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brenda
after abscission induction, ACO1 protein is synthesized in phloem companion cells, in which it is localized mainly in the cytoplasm
brenda
vascular tissues in the pedicel, the main expression site of LeACO1 is in cell layers just outside the flower pedicel abscission zone in its proximal and distal part
brenda
the ethylene biosynthesis genes LeACO4 is preferentially expressed in vascular tissues
brenda
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brenda
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brenda
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brenda
-
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additional information
immunolocalization study and and expression pattern analysis
brenda
additional information
immunolocalization study and and expression pattern analysis
brenda
additional information
-
immunolocalization study and and expression pattern analysis
brenda
additional information
immunolocalization study and expression pattern analysis
brenda
additional information
immunolocalization study and expression pattern analysis
brenda
additional information
-
immunolocalization study and expression pattern analysis
brenda
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-
brenda
additional information
immunolocalization study
-
brenda
additional information
immunolocalization study
-
brenda
additional information
-
immunolocalization study
-
brenda
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metabolism
two tomato ACO genes, LeACO1, and LeACO4 encode the last enzyme in ethylene biosynthesis, 1-aminocyclopropane-1-carboxylate oxidase (ACO) catalyzes the terminal step in ethylene biosynthesis
metabolism
two tomato ACO genes, LeACO1, and LeACO4 encode the last enzyme in ethylene biosynthesis, 1-aminocyclopropane-1-carboxylate oxidase (ACO) catalyzes the terminal step in ethylene biosynthesis
physiological function
the enzyme is involved in methyl jasmonate-induced resistance in tomato
physiological function
the ethylene biosynthesis genes LeACO4 is preferentially expressed in vascular tissues, and is only moderately ethylene sensitive during pedicel abscission
physiological function
the enzyme is involved in methyl jasmonate-induced resistance in tomato
physiological function
the ethylene biosynthesis genes LeACO1 is preferentially expressed in vascular tissues, and is only moderately ethylene sensitive during pedicel abscission
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ACCO4_SOLLC
316
0
35974
Swiss-Prot
other Location (Reliability: 1 )
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35820
-
electron spray mass spectrometry
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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
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enzyme has a short half-life under catalytic conditions undergoing metal-catalyzed oxidative fragmentation
-
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partial, recombinant from Saccharomyces cerevisiae
DEAE Sepharose resin column chromatography
-
partial, recombinant from Saccharomyces cerevisiae
recombinant enzyme from Escherichia coli to homogeneity
-
recombinant from E. coli, 9.8fold to near homogeneity
-
recombinant isozyme ACO1 from Escherichia coli BL21(DE3)-pLysS, to near homogeneity
-
recombinant wild-type enzyme and mutants from Escherichia coli BL21(DE3) to near homogeneity
-
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gene aco4, quantitative reverse transcription real-time PCR expression analysis
isozyme ACO3, DNA sequence determination and analysis, expression in Saccharomyces cerevisiae
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
gene aco1, quantitative reverse transcription real-time PCR expression analysis
isozyme ACO1, DNA sequence determination and analysis, expression in Saccharomyces cerevisiae
isozyme ACO1, overexpression in Escherichia coli BL21(DE3)-pLysS
-
isozyme ACO2, DNA sequence determination and analysis, expression in Saccharomyces cerevisiae
overexpression in Escherichia coli BL21(DE3)
-
wild-type enzyme and mutants, expression in Escherichia coli BL21(DE3)
-
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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
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
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
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
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
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
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