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Information on EC 1.14.17.4 - aminocyclopropanecarboxylate oxidase and Organism(s) Solanum lycopersicum and UniProt Accession P24157

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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.
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This record set is specific for:
Solanum lycopersicum
UNIPROT: P24157
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Word Map
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1-aminocyclopropane-1-carboxylate oxidase
-
1-aminocyclopropane-1-carboxylate oxidase
-
1-aminocyclopropane-1-carboxylic acid oxidase
-
-
ACC oxidase
ethylene-forming enzyme
oxidase, aminocyclopropanecarboxylate
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1-aminocyclopropane-1-carboxylate + ascorbate + O2 = ethene + cyanide + dehydroascorbate + CO2 + 2 H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
oxidative decarboxylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY hide
98668-53-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
show the reaction diagram
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
i.e. ACC
-
?
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2
1-butene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
1-amino-2-methylcyclopropane-1-carboxylate + L-ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + 5,6-O-isopropylidine L-ascorbate + O2
ethylene + cyanide + 5,6-O-isopropylidine L-dehydroascorbate + CO2 + H2O
show the reaction diagram
-
better cosubstrate than L-ascorbate
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
show the reaction diagram
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
1-aminocyclopropane-1-carboxylate + ascorbate + O2 + H+
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + D-ascorbate + O2
ethylene + cyanide + D-dehydroascorbate + CO2 + H2O
show the reaction diagram
-
better cosubstrate than L-ascorbate
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
additional information
?
-
-
L-galactono-gamma-lactone is no cosubstrate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
show the reaction diagram
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
show the reaction diagram
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
1-aminocyclopropane-1-carboxylate + ascorbate + O2 + H+
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
ascorbate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
absolutely required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
ascorbate
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
-
recombinant enzyme, stimulates by 36% at 0.5 mg/ml
-
dithiothreitol
-
recombinant enzyme, stimulates by 38% at 1 mM
ethylene
-
stimulates
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
0.00029 - 0.0053
Fe2+
4.6 - 16.7
L-ascorbate
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00867 - 5.9
1-aminocyclopropane-1-carboxylate
0.2
ascorbate
-
in 50 mM MOPS, pH 7.0, at 29°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.012
partially purified recombinant isozyme ACO3
0.003
partially purified recombinant isozyme ACO2
0.025
partially purified recombinant isozyme ACO1
0.035
-
purified enzyme
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
after abscission induction, ACO1 protein is synthesized in phloem companion cells, in which it is localized mainly in the cytoplasm
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
the ethylene biosynthesis genes LeACO4 is preferentially expressed in vascular tissues
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACCO4_SOLLC
316
0
35974
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35820
-
electron spray mass spectrometry
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme has a short half-life under catalytic conditions undergoing metal-catalyzed oxidative fragmentation
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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.
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team