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Information on EC 1.14.17.4 - aminocyclopropanecarboxylate oxidase and Organism(s) Actinidia deliciosa and UniProt Accession P31237

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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:
Actinidia deliciosa
UNIPROT: P31237
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The taxonomic range for the selected organisms is: Actinidia deliciosa
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
ACC oxidase
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ethylene-forming enzyme
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oxidase, aminocyclopropanecarboxylate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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oxidative decarboxylation
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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
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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 + H2O
show the reaction diagram
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?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
i.e. ACC
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?
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 + H2O
show the reaction diagram
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.073
purified recombinant mutant K172C
0.1
purified recombinant mutant K172A
0.11
purified recombinant mutant G137P
0.16
purified recombinant wild-type enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
kiwi
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACCO_ACTDE
319
0
36292
Swiss-Prot
other Location (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type enzyme and mutants from Escherichia coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutants in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lay, V.J.; Prescott, A.G.; Thomas, P.G.; John, P.
Heterologous expression and site-directed mutagenesis of the 1-aminocyclopropane-1-carboxylate oxidase from kiwi fruit
Eur. J. Biochem.
242
228-234
1996
Actinidia deliciosa (P31237), Actinidia deliciosa
Manually annotated by BRENDA team