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Information on EC 1.14.17.4 - aminocyclopropanecarboxylate oxidase and Organism(s) Malus domestica and UniProt Accession O48882
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1.14.17.4 aminocyclopropanecarboxylate oxidaseIUBMB 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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Word Map
- 1.14.17.4
-
ripening
- tomato
-
climacteric
- 1-methylcyclopropene
-
softening
-
postharvest
- esculentum
- polygalacturonase
-
ripe
-
abscission
- melon
- malus
- petal
-
ethylene-induced
-
cucumis
- phaseolicola
-
ethylene-responsive
-
ripening-related
-
ethephon
-
borkh
- mesocarp
-
2-oxoglutarate-dependent
- carnation
- caryophyllus
-
expansins
-
non-climacteric
-
preclimacteric
- kiwifruits
-
dianthus
-
ethylene-insensitive
- persea
- glycinea
-
9-cis-epoxycarotenoid
- aminoethoxyvinylglycine
-
2,5-norbornadiene
-
1-mcp-treated
-
delicious
-
ethylene-independent
- agriculture
The taxonomic range for the selected organisms is: Malus domestica
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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, asaco, md-aco1, leaco4, md-aco3, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-aminocyclopropane-1-carboxylic acid oxidase
ACC oxidase
ACCO1
ethylene-forming enzyme
-
-
-
-
oxidase, aminocyclopropanecarboxylate
-
-
-
-
ACC oxidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-aminocyclopropane-1-carboxylate + ascorbate + O2 = ethene + cyanide + dehydroascorbate + CO2 + 2 H2O
1-aminocyclopropane-1-carboxylate + ascorbate + O2 = ethene + cyanide + dehydroascorbate + CO2 + 2 H2O
catalytic mechanism
-
1-aminocyclopropane-1-carboxylate + ascorbate + O2 = ethene + cyanide + dehydroascorbate + CO2 + 2 H2O
modelling studies, catalytic mechanism
-
1-aminocyclopropane-1-carboxylate + ascorbate + O2 = ethene + cyanide + dehydroascorbate + CO2 + 2 H2O
the reaction pathway incorporates cyanide as an ACCO/Fe(II) ligand after reaction turnover. The cyanide ligand is likely displaced upon binding of ACC and ascorbate to provide a binding site for oxygen
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
reduction
oxidative decarboxylation
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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
98668-53-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-aminocyclopropane-1-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 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 + HCO3-
1-butene + 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 + 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-alpha-aminobutyric acid + L-ascorbate + O2
ammonia + acetone + dehydroascorbate + CO2 + H2O
-
-
-
-
?
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
-
-
-
-
?
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-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 + 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 + 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
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + H2O
1-aminocyclopropane-1-carboxylic acid + 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
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbate
required for catalysis, residue Lys292 is essential for enzyme activation by ascorbate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
-
together with cosubstrate ascorbate, located in 2-His-1-carboxylate facial triad binding pocket
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cyclopropyl-1-aminocyclopropane-1-carboxylate
-
mechanism-based suicide activator
pyridoxal 5'-phosphate
a competitive inhibitor of enzyme ACCO with respect to ascorbate. Pyridoxal 5'-phosphate may form a Schiff base with the 1-amino group of lysine blocking a binding site for ascorbate
alpha-aminoisobutyric acid
-
competitive to 1-aminocyclopropane-1-carboxylate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4-pteridinediol
-
i.e. lumazine, competitively activates the enzyme with respect to ascorbate
alpha-aminoisobutryric acid
activates enzyme ACCO, prevents enzyme inactivation
dithiothreitol
-
activates in presence of ascorbate, but cannot replace ascorbate
bicarbonate
-
20 mM bicarbonate pretreatment for 20 min is sufficient to protect and activate the enzyme
CO2
-
half-maximal activity at 0.5% atmospheric CO2 in vivo or 0.15 mM in the medium in vitro
cyanide
-
the enzyme is activated by cyanide concentrations between 0.1 and 1 mM with most efficient activation at 0.5 mM
additional information
in the presence of cyanide (CN2) and alpha-aminoisobutryric acid, enzyme ACCO is activated and enzyme inactivation is prevented
-
additional information
-
in the presence of cyanide (CN2) and alpha-aminoisobutryric acid, enzyme ACCO is activated and enzyme inactivation is prevented
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.036
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
0.046
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
0.06
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
0.07
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
0.078
1-aminocyclopropane-1-carboxylate
-
mutant enzyme K199E, in 50 mM MOPS-HCl (pH 7.2), at 30°C
0.083
1-aminocyclopropane-1-carboxylate
-
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
0.129
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
0.139
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
0.158
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
-
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
0.245
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
0.277
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
additional information
additional information
-
Km for O2 and 1-aminocyclopropane-1-carboxylate is dependent on CO2 concentration
-
additional information
additional information
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00015
0.13
-
at 10 mM 1-aminocyclopropane-1-carboxylate, purified recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
additional information
additional information
-
activity at different pH values is dependent on CO2 concentration
additional information
-
activity at different pH values is dependent on CO2 concentration
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
enzyme ACCO is involved in ethylene biosynthesis. ACCO may be also involved in the ethylene signal transduction pathway not directly linked to the ACCO reaction and may playa role in signal transduction after post-translational processing by functioning as protease and as regulator of 1-aminocyclopropane-1-carboxylic acid synthase (Acs2) gene expression, overview. ACC oxidase is subject to autophosphorylaton in vitro and promotes phosphorylation of some apple fruit proteins in a ripening-dependent manner
additional information
metabolism
-
the enzyme catalyzes the final step in ethylene biosynthesis. The enzyme is involved in the ethylene signal transduction pathway not directly linked to the enzyme reaction
metabolism
the enzyme catalyzes the terminal step in ethylene biosynthesis converting ACC to ethylene, cyanide, CO2, dehydroascorbate and water with inputs of Fe(II), ascorbate, bicarbonate (as activators) and oxygen
additional information
the binding sites for ACC, bicarbonate and ascorbic acid for Malus domestica ACCO1 include Arg175, Arg244, Ser246, Lys158, Lys292, Arg299 and Phe300. Glu297, Phe300 and Glu301 in alpha-helix 11 are also important for the ACCO reaction. The ACC substrate has been shown to bind to ACCO/Fe(II) in a bidentate manner. ACC oxidase contains several amino acid sequence motifs for putative protein-protein interactions, phosphokinases and cysteine protease. Residue Thr157 is essential for ACCO activity in a protein structural role. Protein-protein interactions and phosphorylation studies with ACCO, overview
additional information
-
the binding sites for ACC, bicarbonate and ascorbic acid for Malus domestica ACCO1 include Arg175, Arg244, Ser246, Lys158, Lys292, Arg299 and Phe300. Glu297, Phe300 and Glu301 in alpha-helix 11 are also important for the ACCO reaction. The ACC substrate has been shown to bind to ACCO/Fe(II) in a bidentate manner. ACC oxidase contains several amino acid sequence motifs for putative protein-protein interactions, phosphokinases and cysteine protease. Residue Thr157 is essential for ACCO activity in a protein structural role. Protein-protein interactions and phosphorylation studies with ACCO, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ACCO2_MALDO
330
0
37522
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
ACC oxidase is subject to autophosphorylaton in vitro and promotes phosphorylation of some apple fruit proteins in a ripening-dependent manner
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C133A
C133P
C165A
C283A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E294F
E297L
E301D
E301L
F187Y
F300Q
F300Y
K144E
K158E
K158L
K158Q
K158Q/R175E
K158Q/R175Q
K158R
K158R/R175Q
K172E
K199E
K230Q
K230R
K230W
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K292E
K292R
K296E
N216F
P298A
Q188A
Q188K
Q188N
R175A
R175E
R175E/R244K
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
R175E/T157A
R175G
R175H
R175K
R175Q
R244K
R244K/S246A
R244K/S246A/T157A
-
the mutant shows reduced activity compared to the wild type enzyme
R244K/T157A
R299E
R299H
R299K
R299L
S246A
S246A/R244K/T157A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T157A
W203F
Y251F
C133A
site-directed mutagenesis, the mutant shows reduced 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
E294F
site-directed mutagenesis, 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
E301L
site-directed mutagenesis, 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
F300Q
site-directed mutagenesis, 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
K144E
site-directed mutagenesis, 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
K158L
site-directed mutagenesis, 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/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/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
K199E
site-directed mutagenesis, 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
K230R
site-directed mutagenesis, 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
K296E
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N216F
site-directed mutagenesis, 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
Q188K
site-directed mutagenesis, 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
R175A
site-directed mutagenesis, 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/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
-
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
R175H
site-directed mutagenesis, 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
R175Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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
R299H
site-directed mutagenesis, 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
R299L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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
-
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
Y251F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant ACO is purified by affinity chromatography using nickel nitrilotriacetic acid resin, furthermore Sephadex G-25 resin and a Mono-Q column are used, in addition ACO is extracted from apple leaf and fruit tissue
recombinant ACO is purified by affinity chromatography using nickel nitrilotriacetic acid resin, furthermore Sephadex G-25 resin and a Mono-Q column are used, in addition ACO is extracted from apple leaf and fruit tissue
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE) plysS by nickel affinity chromatography, ammonium sulfate precipitation
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into the vector pGEM-T Easy and subsequently into pProEX-1 for expression of the protein in Escherichia coli BL21 cells
into the vector pGEM-T Easy and subsequently into pProEX-1 for expression of the protein in Escherichia coli BL21 cells
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE) plysS
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
-
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.
-
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
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
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)
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
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
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