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Information on EC 1.14.17.4 - aminocyclopropanecarboxylate oxidase and Organism(s) Malus domestica and UniProt Accession Q00985

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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.
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This record set is specific for:
Malus domestica
UNIPROT: Q00985
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The taxonomic range for the selected organisms is: Malus domestica
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-carboxylic acid oxidase
-
1-aminocyclopropane-1-carboxylic acid oxidase
ACC oxidase
ethylene-forming enzyme
-
-
-
-
MD-ACO3
-
-
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
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
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-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
-
-
?
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2
1-butene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2 + HCO3-
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 + 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
1-aminocyclopropane-1-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
-
-
?
alpha-aminoisobutyric acid + L-ascorbate + O2
ammonia + acetone + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
D-alanine + L-ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
D-alpha-aminobutyric acid + L-ascorbate + O2
ammonia + acetone + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
L-alanine + L-ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
L-alpha-aminobutyric acid + L-ascorbate + O2
ammonia + acetone + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
N-hydroxy-alpha-aminoisobutyric acid + L-ascorbate + O2
ammonia + acetone + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
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-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
1-aminocyclopropane-1-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
required for catalysis, residue Lys292 is essential for enzyme activation by ascorbate
ascorbate
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
cyanide
-
inhibitory beyond 1 mM
cyclopropyl-1-aminocyclopropane-1-carboxylate
-
mechanism-based suicide activator
D-alanine
-
competitive to 1-aminocyclopropane-1-carboxylate
D-alpha-aminobutyric acid
-
competitive to 1-aminocyclopropane-1-carboxylate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-aminoisobutryric acid
activates enzyme ACCO, prevents enzyme inactivation
bicarbonate
activates enzyme ACCO
cyanide
activates enzyme ACCO, prevents enzyme inactivation
2,4-pteridinediol
-
i.e. lumazine, competitively activates the enzyme with respect to ascorbate
ascorbate
bicarbonate
-
20 mM bicarbonate pretreatment for 20 min is sufficient to protect and activate the enzyme
cyanide
-
the enzyme is activated by cyanide concentrations between 0.1 and 1 mM with most efficient activation at 0.5 mM
dithiothreitol
-
activates in presence of ascorbate, but cannot replace ascorbate
ethylene
-
activation, in vivo and in vitro
Triton X-100
-
2fold activation
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.031 - 2.3
1-aminocyclopropane-1-carboxylate
0.08939
1-aminocyclopropane-1-carboxylic acid
-
0.031 - 2.3
1-aminocyclopropane-1-carboxylate
0.2445 - 0.401
1-aminocyclopropane-1-carboxylic acid
14.7
alpha-aminoisobutyrate
-
recombinant enzyme, pH 7.0, 30°C
0.27 - 1.25
ascorbate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.066
1-aminocyclopropane-1-carboxylic acid
-
0.07
1-aminocyclopropane-1-carboxylate
-
recombinant enzyme, pH 7.0, 30°C
0.0344 - 0.0914
1-aminocyclopropane-1-carboxylic acid
0.07
alpha-aminoisobutyrate
-
recombinant enzyme, pH 7.0, 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.5
alpha-aminoisobutyric acid
-
pH 7.0, 30°C
28
D-alanine
-
pH7.0, 30°C
4.2
D-alpha-aminobutyric acid
-
pH 7.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000000064
recombinant His-tagged mutant R175E/T157A, pH 7.2, 20°C
0.0000024
recombinant His-tagged mutant R175E/R244K, pH 7.2, 20°C
0.0000029
recombinant His-tagged mutant R244K/T157A, pH 7.2, 20°C
0.0000033
recombinant His-tagged mutant K158E, pH 7.2, 20°C
0.0000083
recombinant His-tagged mutant R299H, pH 7.2, 20°C
0.00001
recombinant His-tagged mutant S246A/R244K/T157A, pH 7.2, 20°C
0.000012
recombinant His-tagged mutant K158Q/R175Q, pH 7.2, 20°C
0.000021
recombinant His-tagged mutant K158Q/R175E, pH 7.2, 20°C
0.00004
recombinant His-tagged mutant R299L, pH 7.2, 20°C
0.000061
recombinant His-tagged mutant R175E/S246A, pH 7.2, 20°C
0.00007
recombinant His-tagged mutant K158L, pH 7.2, 20°C
0.000083
recombinant His-tagged mutant R175Q, pH 7.2, 20°C
0.00011
recombinant His-tagged mutant K158Q, pH 7.2, 20°C
0.00015
0.00017
recombinant His-tagged mutant R175G, pH 7.2, 20°C
0.0002
recombinant His-tagged mutant T157A, pH 7.2, 20°C
0.00022
recombinant His-tagged mutant K292E, pH 7.2, 20°C
0.00024
recombinant His-tagged mutant R175E, pH 7.2, 20°C
0.00025
recombinant His-tagged mutant K158R, pH 7.2, 20°C
0.00028
recombinant His-tagged mutant R175A, pH 7.2, 20°C
0.00065
recombinant His-tagged mutant R175K, pH 7.2, 20°C
0.00092
recombinant His-tagged mutant R244K/S246A, pH 7.2, 20°C
0.00116
recombinant His-tagged mutant R244K, pH 7.2, 20°C
0.00128
recombinant His-tagged mutant K292R, pH 7.2, 20°C
0.00147
recombinant His-tagged mutant R299K, pH 7.2, 20°C
0.00174
recombinant His-tagged mutant S246A, pH 7.2, 20°C
0.00348
recombinant His-tagged wild-type enzyme, pH 7.2, 20°C
0.003
-
at 10 mM L-alpha-aminobutyric acid, purified recombinant enzyme
0.008
-
at 10 mM L-alanine, purified recombinant enzyme
0.011
-
purified enzyme
0.02
-
purified enzyme
0.023
-
at 10 mM D-alanine, purified recombinant enzyme
0.051
-
at 10 mM alpha-aminoisobutyric acid, purified recombinant enzyme
0.059
-
at 10 mM D-alpha-aminobutyric acid, purified recombinant enzyme
0.13
-
at 10 mM 1-aminocyclopropane-1-carboxylate, purified recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7
-
at 20% CO2
7
-
assay at
7 - 7.5
-
-
7.2
-
assay at
7.4
-
at ambient CO2
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
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
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACCO1_MALDO
314
0
35410
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35350
determined by SDA-PAGE and Western blot analysis
35000
-
1 * 35000, SDS-PAGE
36310
determined by SDA-PAGE and Western blot analysis
39000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 35000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
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
C165A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
C283A
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
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/R175Q
site-directed mutagenesis, 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
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
K230W
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
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/S146A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R175E/T157A
site-directed mutagenesis, almost inactive mutant
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/S246A
site-directed mutagenesis, 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
R299E
site-directed mutagenesis, inactive mutant
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/R244K/T157A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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
C133A
-
the mutant showsincreased activity compared to the wild type enzyme
C133P
-
the mutant shows slightly increased activity compared to the wild type enzyme
C165A
-
the mutant shows reduced activity compared to the wild type enzyme
C28A
-
the mutant shows increased activity compared to the wild type enzyme
E294F
-
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
-
the mutant shows reduced activity compared to the wild type enzyme
E301L
-
the mutant shows reduced activity compared to the wild type enzyme
F187Y
-
the mutant shows increased activity compared to the wild type enzyme
F300Q
-
the mutant shows reduced activity compared to the wild type enzyme
F300Y
-
the mutant shows reduced activity compared to the wild type enzyme
K144E
-
the mutant shows reduced activity compared to the wild type enzyme
K158E
-
the mutant shows reduced activity compared to the wild type enzyme
K158L
-
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
-
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
-
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
-
the mutant shows reduced activity compared to the wild type enzyme
K199E
-
the mutant shows reduced activity compared to the wild type enzyme
K230E
-
the mutant shows reduced activity compared to the wild type enzyme
K230Q
-
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
K292R
-
the mutant shows reduced activity compared to the wild type enzyme
K296E
-
the mutant shows increased activity compared to the wild type enzyme
N216F
-
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
-
the mutant shows reduced activity compared to the wild type enzyme
Q188K
-
the mutant shows reduced activity compared to the wild type enzyme
Q188N
-
the mutant shows reduced activity compared to the wild type enzyme
R175A
-
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
-
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
-
the mutant shows reduced activity compared to the wild type enzyme
R175G
-
the mutant shows reduced activity compared to the wild type enzyme
R175H
-
the mutant shows reduced activity compared to the wild type enzyme
R175K
-
the mutant shows reduced activity compared to the wild type enzyme
R175Q
-
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
R244K/S246A
-
the mutant shows reduced activity compared to the wild type enzyme
R244K/S246A/T157A
-
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
R299H
-
the mutant shows reduced activity compared to the wild type enzyme
R299K
-
the mutant shows reduced activity compared to the wild type enzyme
R299L
-
the mutant shows reduced activity compared to the wild type enzyme
S246A
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
T157A
V159G
-
enzymic activity about 30% of wild-type
W203F
-
the mutant shows reduced activity compared to the wild type enzyme
Y251F
-
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 His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE) plysS by nickel affinity chromatography, ammonium sulfate precipitation
180fold to near homogeneity
-
ammonium sulfate precipitation, column chromatography, and gel filtration
-
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 from Escherichia coli
-
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
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE) plysS
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
into the vector pGEM-T Easy and subsequently into pProEX-1 for expression of the protein in Escherichia coli BL21 cells
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
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
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team