1.14.17.4: aminocyclopropanecarboxylate oxidase
This is an abbreviated version!
For detailed information about aminocyclopropanecarboxylate oxidase, go to the full flat file.
Word Map on EC 1.14.17.4
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1.14.17.4
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ripening
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tomato
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climacteric
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1-methylcyclopropene
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softening
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postharvest
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esculentum
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polygalacturonase
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ripe
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abscission
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melon
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malus
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petal
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ethylene-induced
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cucumis
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phaseolicola
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ethylene-responsive
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ripening-related
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ethephon
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borkh
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mesocarp
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2-oxoglutarate-dependent
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carnation
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caryophyllus
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expansins
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non-climacteric
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preclimacteric
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kiwifruits
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dianthus
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ethylene-insensitive
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persea
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glycinea
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9-cis-epoxycarotenoid
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aminoethoxyvinylglycine
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2,5-norbornadiene
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1-mcp-treated
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delicious
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ethylene-independent
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agriculture
- 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
Reaction
Synonyms
1-aminocyclopropane-1-carboxylate oxidase, 1-aminocyclopropane-1-carboxylic acid oxidase, 1-aminocyclopropane-1-carboxylic acid oxidase (gene CM-ACO1), 1-aminocyclopropane-1-carboxylic oxidase, 1-aminocyclopropyl-1-carboxylic acid oxidase, ACC oxidase, ACC oxidase 1, ACC oxidase 2, ACC-oxidase, ACCO, ACCO1, ACO, Aco1, Aco2, Aco3, ACO4, ACO6, aminocyclopropane-1-carboxylate oxidase, aminocyclopropane-2-carboxylic oxidase, AsACO, AtACO1, ethylene-forming enzyme, LeACO1, LeACO4, Ls-ACO1, Ls-ACO2, Ls-ACO3, MD-ACO1, MD-ACO2, MD-ACO3, NsACO, oxidase, aminocyclopropanecarboxylate, PgACO, PmACO, PsACO, TR-ACO1p, TR-ACO2p, TR-ACO3p, TR-ACO4p, ZmACO
ECTree
1.14.17.4 aminocyclopropanecarboxylate oxidaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.14.17.4 - aminocyclopropanecarboxylate oxidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D179E
site-directed mutagenesis, 1% activity compared to the recombinant wild-type enzyme
G137P
site-directed mutagenesis, 98% activity compared to the recombinant wild-type enzyme
H177Q
site-directed mutagenesis, 1% activity compared to the recombinant wild-type enzyme
K158A
site-directed mutagenesis, 1% activity compared to the recombinant wild-type enzyme
K158C
site-directed mutagenesis, 1% activity compared to the recombinant wild-type enzyme
K172A
site-directed mutagenesis, 85% activity compared to the recombinant wild-type enzyme
K172C
site-directed mutagenesis, 64% activity compared to the recombinant wild-type enzyme
G289S
the enzyme activity of the mutant is 3times as high as that of the wild type enzyme
H216D/D218E/H273Q
the mutant does not completely lose catalytic activity
R287G
the activity of the mutant is remarkably decreased to nearly 40% compared to the wild type enzyme
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
D179E
-
site-directed mutagenesis, very low activity, stimulation by bicarbonate
H177E
-
site-directed mutagenesis, very low activity, stimulation by bicarbonate
additional information
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
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the mutant shows reduced activity compared to the wild type enzyme
R175E/T157A
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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
additional information
antisense expression of the enzyme in Petunia x hybrida leads to delayed flower senescence and reduced ethylene production in transgenic shoots, overview
additional information
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enzyme suppression leads to reduction in ethylene and CO2 production in transgenic fruits, which do not show an altered growth phenotype but no climacteric phenotype compared to the wild-type plants, overview
additional information
isozyme ACO1 knockout by expression of specific RNAi in calli via Agrobacterium tumefaciens strain LBA 4404 transformation method and regeneration of transgenic plants
additional information
isozyme ACO1 knockout by expression of specific RNAi in calli via Agrobacterium tumefaciens strain LBA 4404 transformation method and regeneration of transgenic plants
additional information
isozyme ACO2 knockout by expression of specific RNAi in calli via Agrobacterium tumefaciens strain LBA 4404 transformation method and regeneration of transgenic plants
additional information
isozyme ACO2 knockout by expression of specific RNAi in calli via Agrobacterium tumefaciens strain LBA 4404 transformation method and regeneration of transgenic plants
additional information
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expression of the antisense enzyme construct in the male parental line of Galia, co-transformation using the Agrobacterium tumefaciens system with antisense CMACO-1 and CP4 genes, phenotype with reduced growth and latered fruit properties, overview
