Information on EC 1.14.17.4 - aminocyclopropanecarboxylate oxidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.14.17.4
-
RECOMMENDED NAME
GeneOntology No.
aminocyclopropanecarboxylate oxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
1-aminocyclopropane-1-carboxylate + ascorbate + O2 = ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
show the reaction diagram
in the enzyme from plants, the ethylene has signalling functions such as stimulation of fruit ripening
-
-
-
1-aminocyclopropane-1-carboxylate + ascorbate + O2 = ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
show the reaction diagram
catalytic mechanism
-
1-aminocyclopropane-1-carboxylate + ascorbate + O2 = ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
show the reaction diagram
catalytic mechanism
Malus x domestica
-
1-aminocyclopropane-1-carboxylate + ascorbate + O2 = ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
show the reaction diagram
catalytic mechanism
-
1-aminocyclopropane-1-carboxylate + ascorbate + O2 = ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
show the reaction diagram
modelling studies, catalytic mechanism
Malus x domestica
-
1-aminocyclopropane-1-carboxylate + ascorbate + O2 = ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
show the reaction diagram
active site contains a single Fe(II) ligated by residues His177, Asp179, His234, mechanism
-
1-aminocyclopropane-1-carboxylate + ascorbate + O2 = ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
show the reaction diagram
ENDOR studies, structural model of active site both in presence and in absence of substrate
-
1-aminocyclopropane-1-carboxylate + ascorbate + O2 = ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
show the reaction diagram
mechanism, reaction begins with binding of 1-aminocyclopropane-1-carboxylate and O2, and proceeds via iron oxidation and one-electron reduction to form a peroxy intermediate. Breakdown of the intermediate yields a high-valent iron species which is the true oxidizing reagent for bound 1-aminocyclopropane-1-carboxylate
-
1-aminocyclopropane-1-carboxylate + ascorbate + O2 = ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
show the reaction diagram
reaction mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidation
Q0PNH5
-
oxidation
Malus x domestica
O48882, Q00985
-
oxidation
-
-
oxidation
-, Q069K4
-
oxidation
-
-
oxidative decarboxylation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
reduction
Q0PNH5
-
reduction
Malus x domestica
O48882, Q00985
-
reduction
-
-
reduction
-, Q069K4
-
reduction
-
-
PATHWAY
KEGG Link
MetaCyc Link
ethylene biosynthesis I (plants)
-
Cysteine and methionine metabolism
-
Metabolic pathways
-
Biosynthesis of secondary metabolites
-
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 ethylene has signalling functions such as stimulation of fruit-ripening.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1-aminocyclopropane-1-carboxylate oxidase
-
-
1-aminocyclopropane-1-carboxylate oxidase
Antirrhinum majus L.
-
-
-
1-aminocyclopropane-1-carboxylate oxidase
-
-
1-aminocyclopropane-1-carboxylate oxidase
-
-
1-aminocyclopropane-1-carboxylate oxidase
-
-
1-aminocyclopropane-1-carboxylate oxidase
-
-
1-aminocyclopropane-1-carboxylate oxidase
Q0PNH5
-
1-aminocyclopropane-1-carboxylate oxidase
-
-
1-aminocyclopropane-1-carboxylate oxidase
Q1HK33
-
1-aminocyclopropane-1-carboxylate oxidase
Q1HK31
-
1-aminocyclopropane-1-carboxylate oxidase
-
-
1-aminocyclopropane-1-carboxylate oxidase
Q9XER3
-
1-aminocyclopropane-1-carboxylic acid oxidase
H9ZYN5
-
1-aminocyclopropane-1-carboxylic acid oxidase
-
-
1-aminocyclopropane-1-carboxylic acid oxidase
B9A0T8
gene Ls-ACO1
1-aminocyclopropane-1-carboxylic acid oxidase
B9A0T9
gene Ls-ACO2
1-aminocyclopropane-1-carboxylic acid oxidase
B9A0U0
gene Ls-ACO3
1-aminocyclopropane-1-carboxylic acid oxidase
Malus x domestica
-
-
1-aminocyclopropane-1-carboxylic acid oxidase
Malus x domestica
O48882, Q00985
-
1-aminocyclopropane-1-carboxylic acid oxidase
Q069K4
-
1-aminocyclopropane-1-carboxylic acid oxidase
-
-
1-aminocyclopropane-1-carboxylic acid oxidase
Q400P0, Q400U7, Q400U9, Q400V0, Q75QN1
-
1-aminocyclopropane-1-carboxylic acid oxidase
-
-
1-aminocyclopropane-1-carboxylic acid oxidase (gene CM-ACO1)
-
-
1-aminocyclopropane-1-carboxylic acid oxidase (gene CM-ACO1)
Cucumis melo cv. Andes
-
-
-
1-aminocyclopropyl-1-carboxylic acid oxidase
-
-
ACC oxidase
-
-
-
-
ACC oxidase
H9ZYN5
-
ACC oxidase
Q43404
-
ACC oxidase
-
-
ACC oxidase
-
-
ACC oxidase
-
-
ACC oxidase
-
-
ACC oxidase
-
-
ACC oxidase
B9A0T8, B9A0T9, B9A0U0
-
ACC oxidase
-
-
ACC oxidase
Malus x domestica
-
-
ACC oxidase
Malus x domestica
O48882, Q00985
-
ACC oxidase
-
-
ACC oxidase
Q0PNH5
-
ACC oxidase
Q069K4
-
ACC oxidase
-
-
ACC oxidase
-
-
ACC oxidase
-
-
ACC oxidase
Q400P0, Q400U7, Q400U9, Q400V0, Q75QN1
-
ACC oxidase
-
-
ACC oxidase 1
-
-
ACC oxidase 2
-
-
ACC-oxidase
-
-
ACCO1
Malus x domestica
-
-
ACO
H9ZYN5
-
ACO
Antirrhinum majus L.
-
-
-
ACO
Q43404
-
ACO
Malus x domestica
O48882, Q00985
-
ACO
Q1HK33
-
ACO
P05116, P07920, P24157
-
ACO
Q400P0, Q400U7, Q400U9, Q400V0, Q75QN1
-
ACO
-
-
Aco1
P05116
isoform
Aco3
P24157
isoform
ACO4
Q9ZWP2
isoform
ACO6
A4ZYQ6
isoform
aminocyclopropane-1-carboxylate oxidase
-
-
aminocyclopropane-2-carboxylic oxidase
-
-
ethylene-forming enzyme
-
-
-
-
ethylene-forming enzyme
A1Z3B9
-
ethylene-forming enzyme
-
-
MD-ACO1
Malus x domestica
Q00985
-
MD-ACO2
Malus x domestica
O48882
-
MD-ACO3
Malus x domestica
-
-
NsACO
Q069K4
-
oxidase, aminocyclopropanecarboxylate
-
-
-
-
PgACO
-
-
PmACO
Q1HK31
-
PsACO
Q1HK33
-
TR-ACO1p
-
-
TR-ACO2p
-
-
TR-ACO3p
-
-
TR-ACO4p
-
-
ZmACO
-
-
CAS REGISTRY NUMBER
COMMENTARY
98668-53-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Antirrhinum majus L.
L.
-
-
Manually annotated by BRENDA team
ACO1; broccoli or wild cabbage, genes ACO1 and ACO2
UniProt
Manually annotated by BRENDA team
L. var. italica cv. Triathalon
-
-
Manually annotated by BRENDA team
L. var. italica doubled-haploid line GDDH33
-
-
Manually annotated by BRENDA team
cv. Maradol, gene ACCO-1
-
-
Manually annotated by BRENDA team
cantaloupe
-
-
Manually annotated by BRENDA team
L. var Galia
-
-
Manually annotated by BRENDA team
var. Galia
-
-
Manually annotated by BRENDA team
var. reticulatus, Galia muskmelon, an Israeli melon hybrid
-
-
Manually annotated by BRENDA team
Cucumis melo cv. Andes
-
-
-
Manually annotated by BRENDA team
cvs. Ebisu and Miyako; inducible by wounding and ethylene
-
-
Manually annotated by BRENDA team
gene ACO-1, climacteric plant
-
-
Manually annotated by BRENDA team
Thumb.
-
-
Manually annotated by BRENDA team
2 isozymes in roots and leaves; var. Dahlgren 131
-
-
Manually annotated by BRENDA team
var. Dahlgren 131
-
-
Manually annotated by BRENDA team
cv. Grand Rapids
UniProt
Manually annotated by BRENDA team
Malus sylvestris L. Mill. Var. domestica, Borkh., Mansf.
-
-
Manually annotated by BRENDA team
var. domestica
-
-
Manually annotated by BRENDA team
Malus x domestica
-
-
-
Manually annotated by BRENDA team
Malus x domestica
-
UniProt
Manually annotated by BRENDA team
Malus x domestica
Borkh.
-
-
Manually annotated by BRENDA team
Malus x domestica
cv. Golden Delicious
-
-
Manually annotated by BRENDA team
Malus x domestica
cv. Golden Delicious; inducible by ethylene
-
-
Manually annotated by BRENDA team
Malus x domestica
cv. Golden Delicious; purified enzyme
-
-
Manually annotated by BRENDA team
cv. Bappakai
-
-
Manually annotated by BRENDA team
cv. Manila, gene ACO
-
-
Manually annotated by BRENDA team
fragment; Morus alba L.
UniProt
Manually annotated by BRENDA team
AVOe3 gene
-
-
Manually annotated by BRENDA team
plant
-
-
-
Manually annotated by BRENDA team
pv. glycinea, strain ICMP2189, gene efe
UniProt
Manually annotated by BRENDA team
cv.Blanquilla
-
-
Manually annotated by BRENDA team
var. La France, gene ACO1
-
-
Manually annotated by BRENDA team
cultivar Lichun
UniProt
Manually annotated by BRENDA team
cultivar Lichun
SwissProt
Manually annotated by BRENDA team
cultivar Lichun
UniProt
Manually annotated by BRENDA team
isozyme ACO1
SwissProt
Manually annotated by BRENDA team
isozyme ACO1
-
-
Manually annotated by BRENDA team
isozyme ACO2
SwissProt
Manually annotated by BRENDA team
isozyme ACO3
SwissProt
Manually annotated by BRENDA team
expression in Escherichia coli, GST-fusion protein
-
-
Manually annotated by BRENDA team
genotype 10 F, cv. Grasslands Challenge
UniProt
Manually annotated by BRENDA team
ACO1; cv. Murasakizuisho, gene ACO1
UniProt
Manually annotated by BRENDA team
ACO2; cv. Murasakizuisho, gene ACO2
UniProt
Manually annotated by BRENDA team
ACO3; cv. Murasakizuisho, gene ACO3
UniProt
Manually annotated by BRENDA team
ACO4; cv. Murasakizuisho, gene ACO4
UniProt
Manually annotated by BRENDA team
ACO5; cv. Murasakizuisho, gene ACO5
UniProt
Manually annotated by BRENDA team
Vicia sp.
vetch
-
-
Manually annotated by BRENDA team
2 isozymes, encoded by 2 genes: ACO1 and ACO2
-
-
Manually annotated by BRENDA team
2 isozymes in roots and leaves; cv. Texas 5855
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
Malus x domestica
-
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
physiological function
plant
-
involved in ethylene biosynthesis
physiological function
A4ZYQ6, P05116, P24157, Q9ZWP2
the enzyme is involved in methyl jasmonate-induced resistance in tomato; the enzyme is involved in methyl jasmonate-induced resistance in tomato; the enzyme is involved in methyl jasmonate-induced resistance in tomato; the enzyme is involved in methyl jasmonate-induced resistance in tomato
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
1-butene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Vigna radiata, Cucumis melo, Malus x domestica, Vicia sp.
-
stereoselectivity
-
-
?
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2
1-butene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Vigna radiata, Cucumis melo, Malus x domestica, Vicia sp.
-
i.e. allo-coronamic acid
-
-
?
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2
1-butene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
prefers mixture of 1R,2S- and 1S,2R-amino-2-ethylcyclopropane-1-carboxylate, less effective with racemic mixture of 1R,2R- and 1S,2S-diastereomers
-
-
?
1-amino-2-ethylcyclopropane-1-carboxylate + L-ascorbate + O2 + HCO3-
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
Malus x domestica
-
-
-
-
?
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-amino-2-methylcyclopropane-1-carboxylate + L-ascorbate + O2
?
show the reaction diagram
Vigna radiata, Cucumis melo, Malus x domestica, Vicia sp.
-
stereoselectivity
-
-
?
1-amino-2-methylcyclopropane-1-carboxylate + L-ascorbate + O2
?
show the reaction diagram
Vigna radiata, Cucumis melo, Malus x domestica, Vicia sp.
-
prefers mixture of 1R,2S-amino-2-methylcyclopropane-1-carboxylate
-
-
?
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 + 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 + 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 + 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 + 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 + 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 + 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 + H2O
show the reaction diagram
Malus x domestica
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
-
-
-
?
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 + 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 + H2O
show the reaction diagram
P31237
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
P05116, P07920, P24157
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Vicia sp.
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Q400P0, Q400U7, Q400U9, Q400V0, Q75QN1
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Q43404
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
A1Z3B9
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
absolutely dependent on CO2
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
absolutely dependent on CO2
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
absolutely dependent on CO2
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
biosynthesis of plant signalling molecule ethylene
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
biosynthesis of plant signalling molecule ethylene
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
biosynthesis of plant signalling molecule ethylene
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
catalyses the final step in ethylene biosynthesis
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
catalyses the final step in ethylene biosynthesis
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
ethylene regulates fruit ripening by regulating the expression of specific genes, especially in climacteric fruits
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
last step in ethylene biosynthesis
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Q400P0, Q400U7, Q400U9, Q400V0, Q75QN1
last step in the ethylene biosynthetic pathway
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
rate-limiting, one of two key enzymes in the pathway of ethylene biosynthesis are those catalyzing the conversion of S-adenosylmethyonine to 1-aminocyclopropane-1-carboxylic acid, ACC, exogenous ethylene accelerates rimpening, endogenous induces it, enzyme expression depends on the developmental stage of the fruit and ethylene
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
the enzyme is regulated by jasmonates
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
kinetics and mechanism of O2 activation, the rate-determining step is the formation of an FeIV=O species, which acts as the reactive intermediate in substrate oxidation, the FeIV=O species is linked to a rate-limiting proton or hydrogen atom transfer step, overview
-
-
?
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 + 2 H2O
show the reaction diagram
A4ZYQ6, P05116, P24157, Q9ZWP2
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
show the reaction diagram
-, H9ZYN5
-
-
-
?
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
-
specific for the substrates
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
specific for the substrates
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
absolutely dependent on CO2
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
absolutely dependent on CO2
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
absolutely dependent on CO2
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
absolutely dependent on CO2
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
specific for 1-aminocyclopropane-1-carboxylate
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Vigna radiata, Cucumis melo, Malus x domestica
-
stereoselectivity
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
stereoselectivity
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
P31237
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
P05116, P07920, P24157
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Vicia sp.
-
i.e. ACC
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
absolutely dependent on ascorbate
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
absolutely dependent on ascorbate
-
?
1-aminocyclopropane-1-carboxylate + L-ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
N-hydroxyl-1-aminocyclopropane-1-carboxylate is no intermediate
-
?
1-aminocyclopropane-1-carboxylic acid + 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
-
-
-
-
?
1-aminocyclopropane-1-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
O48882, Q00985
-
-
-
?
1-aminocyclopropane-1-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-, Q069K4
-
-
-
?
1-aminocyclopropane-1-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Q0PNH5
-
-
-
?
alpha-aminoisobutyric acid + L-ascorbate + O2
ammonia + acetone + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
-
-
-
?
D-alanine + L-ascorbate + O2
?
show the reaction diagram
Malus x domestica
-
-
-
-
?
D-alpha-aminobutyric acid + L-ascorbate + O2
ammonia + acetone + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
-
-
-
?
L-alanine + L-ascorbate + O2
?
show the reaction diagram
Malus x domestica
-
-
-
-
?
N-hydroxy-alpha-aminoisobutyric acid + L-ascorbate + O2
ammonia + acetone + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
-
-
-
?
O2 + 1-aminocyclopropyl-1-carboxylic acid + ascorbate
?
show the reaction diagram
-
assay at pH 7.2, 25C
-
-
?
L-alpha-aminobutyric acid + L-ascorbate + O2
ammonia + acetone + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
-
-
-
?
additional information
?
-
-
L-galactono-gamma-lactone is no cosubstrate
-
-
-
additional information
?
-
-
ascorbate is not required for O2 activation or product formation
-
-
-
additional information
?
-
-
2-oxoglutarate is not required for activity
-
-
-
additional information
?
-
Malus x domestica
-
the enzyme becomes inactivated by fragmentation and apparently has intrinsic protease and transpeptidase activity
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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 + 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 + 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 + 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 + 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 + H2O
show the reaction diagram
-
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
-
-
-
?
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 + H2O
show the reaction diagram
P31237
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
P05116, P07920, P24157
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Vicia sp.
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Q43404
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
A1Z3B9
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
absolutely dependent on CO2
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
absolutely dependent on CO2
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Malus x domestica
-
absolutely dependent on CO2
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
biosynthesis of plant signalling molecule ethylene
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
biosynthesis of plant signalling molecule ethylene
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
biosynthesis of plant signalling molecule ethylene
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
catalyses the final step in ethylene biosynthesis
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
catalyses the final step in ethylene biosynthesis
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
ethylene regulates fruit ripening by regulating the expression of specific genes, especially in climacteric fruits
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
last step in ethylene biosynthesis
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Q400P0, Q400U7, Q400U9, Q400V0, Q75QN1
last step in the ethylene biosynthetic pathway
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
rate-limiting, one of two key enzymes in the pathway of ethylene biosynthesis are those catalyzing the conversion of S-adenosylmethyonine to 1-aminocyclopropane-1-carboxylic acid, ACC, exogenous ethylene accelerates rimpening, endogenous induces it, enzyme expression depends on the developmental stage of the fruit and ethylene
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-
the enzyme is regulated by jasmonates
-
-
?
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 + 2 H2O
show the reaction diagram
A4ZYQ6, P05116, P24157, Q9ZWP2
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
show the reaction diagram
-, H9ZYN5
-
-
-
?
1-aminocyclopropane-1-carboxylate + ascorbate + O2 + H+
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
-
-
-
-
?
1-aminocyclopropane-1-carboxylic acid + 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
Malus x domestica
O48882, Q00985
-
-
-
?
1-aminocyclopropane-1-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
-, Q069K4
-
-
-
?
1-aminocyclopropane-1-carboxylic acid + ascorbate + O2
ethylene + cyanide + dehydroascorbate + CO2 + H2O
show the reaction diagram
Q0PNH5
-
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ascorbate
-
-
ascorbate
A1Z3B9
-
ascorbate
Q400P0, Q400U7, Q400U9, Q400V0, Q75QN1
-
ascorbate
Q43404
-
ascorbate
-
best at 20 mM, kinetics, overview
ascorbate
-
-
ascorbate
-
absolutely required
ascorbate
Malus x domestica
-
-
isoascorbate
-
may substitute for ascorbate, 75% of the efficiency of ascorbate
additional information
-, H9ZYN5
the enzyme does not require ascorbate
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Fe2+
Malus x domestica
-
absolutely required
Fe2+
-
optimal at 0.025 mM; required
Fe2+
-
required
Fe2+
-
iron binding ligands are His177, Asp179, His234; required
Fe2+
P05116, P07920, P24157
absolutely required; absolutely required; absolutely required
Fe2+
-
a single bound Fe2+ per monomer; required
Fe2+
-
absolutely required
Fe2+
Malus x domestica
-
together with cosubstrate ascorbate, located in 2-His-1-carboxylate facial triad binding pocket
Fe2+
-
oxidizes to Fe(III) during single turnover
Fe2+
-
KM-value 4 mM
Fe2+
-
kinetic role in catalysis forming oxygen complexes, overview
Fe2+
Q0PNH5
-
Fe2+
Malus x domestica
-
-
Fe2+
-, H9ZYN5
in the absence of Fe2+, the activity is 2.4fold lower than that in the steady-state reaction when 0.0025 mM Fe2+ is added (maximum activity at 0.01 mM Fe2+)
Fe2+
-
a nonheme Fe(II)-containing enzyme
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(1-amino-1-methyl)ethylphosphonic acid
-
competitive inhibitor versus both 1-aminocyclopropane-1-carboxylate and bicarbonate
-
1,10-phenanthroline
-
strong inhibition
1,10-phenanthroline
P05116, P07920, P24157
-
1-aminocyclopropane-1-carboxylate
-
slight inhibition at high concentration
1-aminocyclopropane-1-phosphonic acid
-
competitive inhibitor versus both 1-aminocyclopropane-1-carboxylate and bicarbonate
-
2,4,6-Trinitrobenzenesulfonate
-
5 mM, 0.7% residual activity
2,4-Dinitrophenol
-
1 mM, 40% residual activity
2-aminoisobutyric acid
A4ZYQ6, P05116, P24157, Q9ZWP2
competitive inhibitor; competitive inhibitor
-
2-oxoglutarate
-
at 1 mM
4-Chloromercuriphenylsulfonate
-
1 mM, 1.7% residual activity
8-hydroxyquinoline
-
-
alpha-aminoisobutyric acid
Malus x domestica
-
-
alpha-aminoisobutyric acid
Malus x domestica
-
competitive to 1-aminocyclopropane-1-carboxylate
alpha-aminoisobutyric acid
-
-
alpha-aminoisobutyric acid
A4ZYQ6, P05116, P24157, Q9ZWP2
competitive inhibitor; competitive inhibitor
ascorbate
-
required in vitro, inhibitory in vivo
carbonyl sulfide
-
in presence of HCO3-, noncompetitive and irreversible, not at CO2-binding site
catalase
-
-
-
Co2+
Malus x domestica
-
-
Co2+
P05116, P07920, P24157
-
cyanide
Malus x domestica
-
inhibitory beyond 1 mM
cyclopropyl-1-aminocyclopropane-1-carboxylate
Cucumis melo, Malus x domestica, Vigna radiata
-
mechanism-based suicide activator
D-alanine
Malus x domestica
-
competitive to 1-aminocyclopropane-1-carboxylate
D-alpha-aminobutyric acid
Malus x domestica
-
competitive to 1-aminocyclopropane-1-carboxylate
diethyl dicarbonate
-
complete inactivation at 1.5 mM, pH 6.8, after 20 min
EDTA
P05116, P07920, P24157
-
EDTA
-
5 mM, 2.1% residual activity
N-ethylmaleimide
-
1 mM, 10% residual activity
n-propyl gallate
P05116, P07920, P24157
free-radical scavenger; free-radical scavenger; free-radical scavenger
n-propyl gallate
-
3 mM, 1.3% residual activity
N2
-
complete inhibition of enzyme in anaerobic N2-atmosphere, reversible
p-chloromercuribenzoate
-
-
p-Chloromercuriphenylsulfonate
-
-
Salicylhydroxamic acid
-
1 mM, 15% residual activity
Zn2+
-
competitive to Fe2+
additional information
-
enzyme is inactivated when preincubated in presence of 1-aminocyclopropane-1-carboxylate, Fe2+ and ascorbate
-
additional information
-
the enzyme is partially suppressed in petals and completely in gynoecia at 32C, but expressed at 34C, the ACO expression rate decreases gradually after cutting, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,4-pteridinediol
Malus x domestica
-
i.e. lumazine, competitively activates the enzyme with respect to ascorbate
-
ascorbate
Malus x domestica
-
absolutely dependent on; minimal 1 mM
ascorbate
-
optimal at 5-10 mM; required
ascorbate
-
cannot be replaced by DTT or NADH; required
ascorbate
-
cannot be replaced by glutathione and NADPH; required invitro, inhibitory in vivo
ascorbate
P05116, P07920, P24157
3 isozymes: absolutely dependent on invitro, no requirement in vivo; 3 isozymes: absolutely dependent on invitro, no requirement in vivo; 3 isozymes: absolutely dependent on invitro, no requirement in vivo
ascorbate
-
required
ascorbate
-
absolutely dependent on
ascorbate
-
addition at 10% of its KM-value significantly accelerates iron oxidation and ethylene formation
ascorbate
plant
-
dependent
bicarbonate
Malus x domestica
-
20 mM bicarbonate pretreatment for 20 min is sufficient to protect and activate the enzyme
bicarbonate
-, H9ZYN5
the enzyme is completely dependent on bicarbonate
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
-
CO2
Malus x domestica
-
absolutely dependent on; half-maximal activity at 0.5% atmospheric CO2 in vivo or 0.15 mM in the medium in vitro
CO2
Malus x domestica
-
absolutely dependent on; HCO3- is not involved in activation; highest activity at pH 7.0; pH-dependence
CO2
-
pH-dependence; requires HCO3-/CO2 mixture
CO2
-
activates
CO2
-
influences Km, pH optimum, optimum concentration of ascorbate and 1-aminocyclopropane-1-carboxylate at varying concentrations
CO2
-
requires HCO3-/CO2 mixture
CO2
Malus x domestica
-
activates; pH-dependence
CO2
-
strong activation in leaves, but not in roots
CO2
-
activates; required
CO2
P05116, P07920, P24157
absolutely dependent on; absolutely dependent on; absolutely dependent on
CO2
-
absolutely dependent on; best at 14% or higher
cyanide
Malus x domestica
-
the enzyme is activated by cyanide concentrations between 0.1 and 1 mM with most efficient activation at 0.5 mM
dihydrojasmonate
-
exogenously applied onto fruit skin, it induces the enzyme and the ethylene production in fruits at day 0 of ripening, in the climacteric stage at day 20 of ripening at 20C the ethylene production increases without enzyme induction in trested and untreated fruits, overview
dithiothreitol
Malus x domestica
-
activates in presence of ascorbate, but cannot replace ascorbate
dithiothreitol
-
recombinant enzyme, stimulates by 38% at 1 mM
dithiothreitol
-
activates in presence of ascorbate, but cannot replace ascorbate
ethylene
Malus x domestica
-
activation, in vivo and in vitro
ethylene
-
induction is inhibited by 2,5-norbornadiene; stimulates, induction, regulation scheme
ethylene
-
stimulates
indole acetic acid
-
0.1 mM, increases level of ACO2 transcript in vivo, not ACO1
LiCl
-
1 mM, increases level of ACO2 transcript in vivo, not ACO1
n-propyl dihydrojasmonate
-
-
-
O2
-
dependent on
Triton X-100
Malus x domestica
-
2fold activation
Triton X-100
-
best at 0.8% or above
methyl jasmonate
A4ZYQ6, P05116, P24157, Q9ZWP2
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; 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; 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; 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 2-oxoglutarate
-
additional information
-
no activation by 2-oxoglutarate
-
additional information
-
no activation by bisulfite, isozyme AOC1
-
additional information
-
wounding induces the enzyme, which peaks after cutting and then decreases gradually, 2,5-norbornadiene inhibts the induction by wounding. Ethylene, alone or in presence of 2,5-norbornadiene, induces the enzyme, which afterwards decreases gradually
-
additional information
A1Z3B9
cellulose induces the enzyme, while very low level of ethylene is produced when sodium carboxymethyl cellulose or lactose are used as carbon sources
-
additional information
plant
-
increased enzyme activity after wounding of the potatoe
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
114
-
1-amino-2-ethylcyclopropane-1-carboxylate
-
-
0.012
-
1-aminocyclopropane-1-carboxylate
P05116, P07920, P24157
recombinant isozyme ACO1, in presence of 3mM L-ascorbate, pH 7.2, 29C
0.013
-
1-aminocyclopropane-1-carboxylate
P05116, P07920, P24157
recombinant isozyme ACO1, in presence of 3mM L-ascorbate, pH 7.2, 29C
0.029
-
1-aminocyclopropane-1-carboxylate
P05116, P07920, P24157
recombinant isozyme ACO1, in presence of 3mM L-ascorbate and 10 mM HCO3-, pH 7.2, 29C
0.03
-
1-aminocyclopropane-1-carboxylate
P05116, P07920, P24157
recombinant isozyme ACO1, in presence of 3mM L-ascorbate and 10 mM HCO3-, pH 7.2, 29C; recombinant isozyme ACO1, in presence of 3mM L-ascorbate, pH 7.2, 29C
0.031
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme E301L, in 50 mM MOPS-HCl (pH 7.2), at 30C; mutant enzyme R299L, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.032
-
1-aminocyclopropane-1-carboxylate
-
recombinant enzyme, in presence of 5mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28C
0.036
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme F300Y, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.042
-
1-aminocyclopropane-1-carboxylate
-
recombinant mutant H177E, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28C
0.046
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme K158R, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.047
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme R299K, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.051
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
wild type enzyme, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.057
-
1-aminocyclopropane-1-carboxylate
-
pH 6.7, 30C
0.06
-
1-aminocyclopropane-1-carboxylate
-
pH 7.5, 30C
0.06
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme K158Q, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.062
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme C28A, in 50 mM MOPS-HCl (pH 7.2), at 30C; mutant enzyme Y251F, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.063
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme W203F, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.067
-
1-aminocyclopropane-1-carboxylate
P05116, P07920, P24157
recombinant isozyme ACO1, in presence of 3mM L-ascorbate and 10 mM HCO3-, pH 7.2, 29C
0.07
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme T157A, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.077
-
1-aminocyclopropane-1-carboxylate
-
recombinant isozyme ACO1, in presence of 0.5 mM L-ascorbate and 20 mM CO2/HCO3-, pH 7.2, 25C
0.078
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme K199E, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.083
-
1-aminocyclopropane-1-carboxylate
-
recombinant wild-type enzyme, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28C
0.083
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme R175K, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.09
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme F187Y, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.094
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme R299H, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.121
-
1-aminocyclopropane-1-carboxylate
-
recombinant mutant H56Q, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28C
0.129
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme F300Q, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.132
-
1-aminocyclopropane-1-carboxylate
-
recombinant mutant D179E, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28C
0.139
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme R175H, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.142
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme R175G, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.15
-
1-aminocyclopropane-1-carboxylate
-
in 50 mM MOPS, pH 7.0, at 29C
0.158
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme N216F, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.173
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme K158E, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.175
-
1-aminocyclopropane-1-carboxylate
-
under atmospheric conditions, pH 7.2, 30C
0.175
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme R244K, in 50 mM MOPS-HCl (pH 7.2), at 30C; mutant enzyme R244K/S246A, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.193
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme R175A, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.206
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme K158Q/R175Q, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.218
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme R175Q, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.23
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
recombinant enzyme, pH 7.0, 30C
0.245
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme R244K/S246A/T157A, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.25
-
1-aminocyclopropane-1-carboxylate
-, H9ZYN5
at pH and C
0.277
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme S246A, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.279
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme K158R/R175Q, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.281
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme K158L, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.287
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme Q188N, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.379
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme R175E, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.659
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme K158Q/R175E, in 50 mM MOPS-HCl (pH 7.2), at 30C
1.2
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme R175E/S246A, in 50 mM MOPS-HCl (pH 7.2), at 30C
2.3
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
mutant enzyme R175E/T157A, in 50 mM MOPS-HCl (pH 7.2), at 30C
0.08939
-
1-aminocyclopropane-1-carboxylic acid
Malus x domestica
O48882, Q00985
-
0.2445
-
1-aminocyclopropane-1-carboxylic acid
Malus x domestica
O48882, Q00985
-
0.401
-
1-aminocyclopropane-1-carboxylic acid
Malus x domestica
O48882, Q00985
-
1
-
5,6-O-isopropylidine L-ascorbate
-
recombinant enzyme, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28C
14.7
-
alpha-aminoisobutyrate
Malus x domestica
-
recombinant enzyme, pH 7.0, 30C
0.27
-
ascorbate
Malus x domestica
-
mutant S246A, pH 7.4, 30C
0.34
-
ascorbate
Malus x domestica
-
mutant E109D, pH 7.4, 30C
0.36
-
ascorbate
Malus x domestica
-
mutant S257A, pH 7.4, 30C
0.38
-
ascorbate
Malus x domestica
-
wild-type, pH 7.4, 30C
0.82
-
ascorbate
Malus x domestica
-
mutant T157A, pH 7.4, 30C; mutant V159G, pH 7.4, 30C
0.92
-
ascorbate
Malus x domestica
-
mutant S246G, pH 7.4, 30C
0.99
-
ascorbate
Malus x domestica
-
mutant R244A, pH 7.4, 30C
1.2
-
ascorbate
Malus x domestica
-
mutant R244K, pH 7.4, 30C
1.25
-
ascorbate
Malus x domestica
-
mutant R244G, pH 7.4, 30C
2.7
-
ascorbate
-
in 50 mM MOPS, pH 7.0, at 29C
1.7
-
D-ascorbate
-
recombinant enzyme, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28C
0.00029
-
Fe2+
-
recombinant mutant H177E, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28C
0.00043
-
Fe2+
-
recombinant wild-type enzyme, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28C
0.00047
-
Fe2+
-
recombinant mutant H56Q, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28C
0.0046
-
Fe2+
-
recombinant mutant D179E, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28C
0.0053
-
Fe2+
-
recombinant enzyme, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28C
40
-
HCO3-
-
-
4.6
-
L-ascorbate
-
recombinant isozyme ACO1, in presence of 0.5 mM L-ascorbate and 20 mM CO2/HCO3-, pH 7.2, 25C
0.028
-
O2
-
recombinant isozyme ACO1, in presence of 0.5 mM L-ascorbate and 20 mM CO2/HCO3-, pH 7.2, 25C
16.7
-
L-ascorbate
-
recombinant enzyme, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28C
additional information
-
additional information
Malus x domestica
-
Km for O2 and 1-aminocyclopropane-1-carboxylate is dependent on CO2 concentration
-
additional information
-
additional information
-
Km for O2 and 1-aminocyclopropane-1-carboxylate is dependent on HCO3-/CO2 concentration
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
steady-state kinetics, solvent isotope effects, and competitive oxygen kinetic isotope effects, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00867
-
1-aminocyclopropane-1-carboxylate
-
recombinant mutant D179E, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28C
0.0095
-
1-aminocyclopropane-1-carboxylate
-
recombinant mutant H177E, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28C
0.07
-
1-aminocyclopropane-1-carboxylate
Malus x domestica
-
recombinant enzyme, pH 7.0, 30C
0.19
-
1-aminocyclopropane-1-carboxylate
-
in 50 mM MOPS, pH 7.0, at 29C
0.223
-
1-aminocyclopropane-1-carboxylate
-
pH 7.2, 25C, 2 mM ascorbate, recombinant enzyme
0.612
-
1-aminocyclopropane-1-carboxylate
-
pH 7.2, 25C, 20 mM ascorbate, recombinant enzyme
5.17
-
1-aminocyclopropane-1-carboxylate
-
recombinant mutant H56Q, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28C
5.9
-
1-aminocyclopropane-1-carboxylate
-
recombinant wild-type enzyme, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28C
0.0344
-
1-aminocyclopropane-1-carboxylic acid
Malus x domestica
O48882, Q00985
-
0.066
-
1-aminocyclopropane-1-carboxylic acid
Malus x domestica
O48882, Q00985
-
0.0914
-
1-aminocyclopropane-1-carboxylic acid
Malus x domestica
O48882, Q00985
-
0.07
-
alpha-aminoisobutyrate
Malus x domestica
-
recombinant enzyme, pH 7.0, 30C
0.2
-
ascorbate
-
in 50 mM MOPS, pH 7.0, at 29C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.021
-
O2
plant
-
-
9
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.3
-
(1-amino-1-methyl)ethylphosphonic acid
-
in 50 mM MOPS, pH 7.0, at 29C
-
38.9
-
1-aminocyclopropane-1-carboxylate
-
recombinant isozyme ACO1, in presence of 5 mM L-ascorbate and 20 mM CO2/HCO3-, pH 7.2, 25C
1.5
-
1-aminocyclopropane-1-phosphonic acid
-
in 50 mM MOPS, pH 7.0, at 29C
-
4.2
-
alpha-aminoisobutyric acid
-
pH 6.7, 30C
7.5
-
alpha-aminoisobutyric acid
Malus x domestica
-
pH 7.0, 30C
28
-
D-alanine
Malus x domestica
-
pH7.0, 30C
4.2
-
D-alpha-aminobutyric acid
Malus x domestica
-
pH 7.0, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.003
-
P05116, P07920, P24157
partially purified recombinant isozyme ACO2
0.003
-
Malus x domestica
-
at 10 mM L-alpha-aminobutyric acid, purified recombinant enzyme
0.0047
-
-
crude enzyme extract
0.006
-
-
pear fruit prior homogenization
0.008
-
Malus x domestica
-
at 10 mM L-alanine, purified recombinant enzyme
0.011
-
Malus x domestica
-
purified enzyme
0.012
-
P05116, P07920, P24157
partially purified recombinant isozyme ACO3
0.02
-
Malus x domestica
-
purified enzyme
0.023
-
Malus x domestica
-
at 10 mM D-alanine, purified recombinant enzyme
0.025
-
P05116, P07920, P24157
partially purified recombinant isozyme ACO1
0.035
-
-
purified enzyme
0.051
-
Malus x domestica
-
at 10 mM alpha-aminoisobutyric acid, purified recombinant enzyme
0.059
-
Malus x domestica
-
at 10 mM D-alpha-aminobutyric acid, purified recombinant enzyme
0.073
-
P31237
purified recombinant mutant K172C
0.1
-
P31237
purified recombinant mutant K172A
0.11
-
P31237
purified recombinant mutant G137P
0.13
-
Malus x domestica
-
at 10 mM 1-aminocyclopropane-1-carboxylate, purified recombinant enzyme
0.16
-
P31237
purified recombinant wild-type enzyme
additional information
-
-
activity of 2 isozymes in roots and leaves
additional information
-
Q43404
ethylene production in shoots of transgenic Petunia plants expressing broccoli ACO1 and longevity of cut flowers, overview
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.7
-
Malus x domestica
-
at 20% CO2
6.7
-
-
assay at
6.8
7.2
P05116, P07920, P24157
-
7
7.5
Malus x domestica
-
-
7
-
Malus x domestica
-
assay at
7.2
-
Malus x domestica
-
assay at
7.2
-
-
assay at
7.2
-
-
assay at
7.2
-
plant
-
assay at
7.2
-
Malus x domestica
O48882, Q00985
-
7.4
-
Malus x domestica
-
at ambient CO2
7.4
-
-
assay at
7.5
-
Malus x domestica
O48882, Q00985
-
7.5
-
-
-
7.8
-
Malus x domestica
O48882, Q00985
-
additional information
-
Malus x domestica
-
activity at different pH values is dependent on CO2 concentration
additional information
-
-
activity at different pH values is dependent on CO2 concentration
additional information
-
Malus x domestica
-
activity at different pH values is dependent on CO2 concentration
additional information
-
-
2 isozymes, dependent assay conditions
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.8
8
P05116, P07920, P24157
-
6.5
8
Malus x domestica
O48882, Q00985
;
6.5
8.5
Malus x domestica
O48882, Q00985
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
plant
-
assay at
28
-
-
assay at
28
-
-
2 optima at 28C and 38C
29
-
P05116, P07920, P24157
-
30
-
Malus x domestica
-
assay at
30
-
-
assay at
30
-
Malus x domestica
-
assay at
30
-
-
assay at
38
-
-
2 optima at 28C and 38C
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
the enzyme is partially suppressed in petals and completely in gynoecia at 32C, but expressed at 34C
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
highest expression in ontological younger tissue
Manually annotated by BRENDA team
Q1HK31
highest abundance in epithelial cells of cortical resin ducts
Manually annotated by BRENDA team
Q43404
genes ACO1 and ACO2 are expressed after harvest
Manually annotated by BRENDA team
plant
-
-
Manually annotated by BRENDA team
Malus x domestica
-
in climacteric stage
Manually annotated by BRENDA team
-
wounded tissue of mature fruit
Manually annotated by BRENDA team
-
mango is a climacteric fruit in which the rate of ethylene production varies widely depending on the cultivar, enzyme expression depends on the developmental stage of the fruit and ethylene
Manually annotated by BRENDA team
-
climacteric fruit
Manually annotated by BRENDA team
Malus x domestica
O48882, Q00985
-
Manually annotated by BRENDA team
A4ZYQ6, P05116, P24157, Q9ZWP2
-
Manually annotated by BRENDA team
-
ACO-1 expression analysis in cut flowers, activity during climateric development, overview
Manually annotated by BRENDA team
-
etiolated; isozyme ACO2 level is decreased by wounding; isozymes ACO1 and ACO2, transcripts accumulate constitutively
Manually annotated by BRENDA team
-
leaf-specific isozyme, stimulated by CO2
Manually annotated by BRENDA team
Q400P0, Q400U7, Q400U9, Q400V0, Q75QN1
expression of gene ACO1; expression of gene ACO3; expression of gene ACO5; low expression level of gene ACO2; low expression level of gene ACO4
Manually annotated by BRENDA team
plant
-
-
Manually annotated by BRENDA team
Malus x domestica
O48882, Q00985
;
Manually annotated by BRENDA team
-, Q069K4
relative RNA transcript level 5%
Manually annotated by BRENDA team
-
wounded and incubated before enzyme extraction
Manually annotated by BRENDA team
Q1HK31
highest abundance in polyphenolic and ray parenchyma cells
Manually annotated by BRENDA team
-
ACO-1 expression analysis in cut flowers, activity during climateric development, overview
Manually annotated by BRENDA team
Q400P0, Q400U7, Q400U9, Q400V0, Q75QN1
wilting, expression of gene ACO1; wilting, expression of gene ACO3; wilting, expression of gene ACO5; wilting, low expression level of gene ACO2; wilting, low expression level of gene ACO4
Manually annotated by BRENDA team
-, Q069K4
petal lobe, relative RNA transcript level 100%, petal tube, relative RNA transcript level 30%
Manually annotated by BRENDA team
-
protophloem sieve elements
Manually annotated by BRENDA team
-
root specific isozyme, not stimulated by CO2
Manually annotated by BRENDA team
-
primary; root specific isozyme, not stimulated by CO2
Manually annotated by BRENDA team
plant
-
-
Manually annotated by BRENDA team
-, Q069K4
relative RNA transcript level 10%
Manually annotated by BRENDA team
B9A0T8, B9A0T9, B9A0U0
-
Manually annotated by BRENDA team
-
activity is highest during the onset of embryogenesis, and declines gradually afterwards, no activity during desiccation period
Manually annotated by BRENDA team
-, Q069K4
relative RNA transcript level 8%
Manually annotated by BRENDA team
-, Q069K4
relative RNA transcript level 10%
Manually annotated by BRENDA team
-
increased homogeneous expression in gravistimulated stems
Manually annotated by BRENDA team
Q1HK31
constitutively expressed at low levels and expression is slightly increased after wounding
Manually annotated by BRENDA team
Q400P0, Q400U7, Q400U9, Q400V0, Q75QN1
expression of gene ACO1; expression of gene ACO3O4; expression of gene ACO5; low expression level of gene ACO2; low expression level of gene ACO4
Manually annotated by BRENDA team
plant
-
-
Manually annotated by BRENDA team
-, Q069K4
relative RNA transcript level 30%
Manually annotated by BRENDA team
Antirrhinum majus L.
-
increased homogeneous expression in gravistimulated stems
-
Manually annotated by BRENDA team
-, Q069K4
stigma/stylus, relative RNA transcript level 25%
Manually annotated by BRENDA team
plant
-
-
Manually annotated by BRENDA team
-
highest expression in ontological younger tissue
Manually annotated by BRENDA team
plant
-
-
Manually annotated by BRENDA team
-
companion cells associated with metaphloem sieve elements
Manually annotated by BRENDA team
additional information
-
silique wall
Manually annotated by BRENDA team
additional information
-
expression throughout all tissue types and at all ontological stages; highest expression in ontological older tissue
Manually annotated by BRENDA team
additional information
-
comparison of enzyme expression and activity in fresh and cut, vase-lived flowers, the ACO expression rate decreases gradually after cutting, overview
Manually annotated by BRENDA team
additional information
Q400P0, Q400U7, Q400U9, Q400V0, Q75QN1
tulip ACO genes are regulated differentially among the vegetative tissues and during flower senescence; tulip ACO genes are regulated differentially among the vegetative tissues and during flower senescence; tulip ACO genes are regulated differentially among the vegetative tissues and during flower senescence; tulip ACO genes are regulated differentially among the vegetative tissues and during flower senescence; tulip ACO genes are regulated differentially among the vegetative tissues and during flower senescence
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35350
-
Malus x domestica
O48882, Q00985
determined by SDA-PAGE and Western blot analysis
35800
-
Q1HK31
calculated from cDNA and confirmed by immunoblotting
35820
-
-
electron spray mass spectrometry
36310
-
Malus x domestica
O48882, Q00985
determined by SDA-PAGE and Western blot analysis
39000
-
Malus x domestica
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 35000, x * 40000, SDS-PAGE of accumulating recombinant fusion protein
?
-
x * 36800, deduced from gene sequence, x * 36000, SDS-PAGE
?
-
x * 41000, SDS-PAGE
monomer
Malus x domestica
-
1 * 35000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
apo-enzyme and in complex with Fe(II) or Co(II)
-
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
unstable, activity decreases during in vitro incubation with half-life of 9 min
-
highly unstable under assay conditions
-
enzyme has a short half-life under catalytic conditions undergoing metal-catalyzed oxidative fragmentation
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 30% glycerol, stable for 11 days
-
2C, 30% glycerol, loss of 30% activity after 24 h
-
2C, 30% glycerol, loss of 85% activity after 7 h
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant wild-type enzyme and mutants from Escherichia coli
P31237
partial
-
180fold to near homogeneity
Malus x domestica
-
ammonium sulfate precipitation, column chromatography, and gel filtration
Malus x domestica
-
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 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
Malus x domestica
O48882, Q00985
recombinant from Escherichia coli
Malus x domestica
-
DEAE Sepharose resin column chromatography
-
partial, recombinant from Saccharomyces cerevisiae; partial, recombinant from Saccharomyces cerevisiae; partial, recombinant from Saccharomyces cerevisiae
P05116, P07920, P24157
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
-
glutathione-Sepharose chromatography, anion-exchange chromatography
Q9XER3, -
recombinant GST-fusion protein
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression of wild-type and mutants in Escherichia coli
P31237
expressed in Escherichia coli BL21(DE3) cells
-, H9ZYN5
gene ACO1, antisense expression in Petunia x hybrida using the Agrobacterium tumefaciens strain LBA4404 transfection method
Q43404
gene ACCO-1, DNA and amino acid sequence determination and analysis
-
expression in transgenic plants
-
gene ACO-1, expression analysis in gynoecia and petals from three carnation flowers
-
expressed in Escherichia coli
Malus x domestica
-
expressed in Escherichia coli BL21(DE3) cells
Malus x domestica
-
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; into the vector pGEM-T Easy and subsequently into pProEX-1 for expression of the protein in Escherichia coli BL21 cells
Malus x domestica
O48882, Q00985
into the vector PMD 18-T for sequencing
Q0PNH5
a cDNA library is constructed
-, Q069K4
expression in antisense orientation under control of the 35S promoter in plum fruits, var. Bluebyrd and Stanley, by transformation of plum hypocotyls, the transgenic plants show reduced response to exogenous ethylene and delayed fruit ripening and softening in some lines
-
gene efe, expression under the control of Trichoderma reesei cbh1 promoter in Trichoderma viride strain TL124, protoplast transformation, one copy of efe gene is integrated into the chromosomal DNA, expression analysis
A1Z3B9
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
isozyme ACO1, DNA sequence determination and analysis, expression in Saccharomyces cerevisiae; isozyme ACO2, DNA sequence determination and analysis, expression in Saccharomyces cerevisiae; isozyme ACO3, DNA sequence determination and analysis, expression in Saccharomyces cerevisiae
P05116, P07920, P24157
isozyme ACO1, overexpression in Escherichia coli BL21(DE3)-pLysS
-
overexpression in Escherichia coli BL21(DE3)
-
wild-type enzyme and mutants, expression in Escherichia coli BL21(DE3)
-
GST-tagged version expressed in Escherichia coli BL21
Q9XER3, -
gene ACO1, differential screening of the petal cDNA library, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons, phylogenetic analysis, expression analysis, overview; gene ACO2, differential screening of the petal cDNA library, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons, phylogenetic analysis, expression analysis, overview; gene ACO3, differential screening of the petal cDNA library, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons, phylogenetic analysis, expression analysis, overview; gene ACO4, differential screening of the petal cDNA library, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons, phylogenetic analysis, expression analysis, overview; gene ACO5, differential screening of the petal cDNA library, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons, phylogenetic analysis, expression analysis, overview
Q400P0, Q400U7, Q400U9, Q400V0, Q75QN1
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in fruits during ripening stage
-
in fruits during ripening stage
Cucumis melo cv. Andes
-
-
mRNA level increased in the primary root after transfer to pH 4.0, addition of 1-aminocyclopropane-1-carboxylic acid or indole-3-acetic acid (at pH 6.0) induce accumulation of mRNA; white light irradation of dark-grown seedlings following transfer to pH 4.0 induces accumulation of mRNA; white light irradation of dark-grown seedlings following transfer to pH 4.0 induces accumulation of mRNA
B9A0T8, B9A0T9, B9A0U0
the mRNA level and enzyme activity are lower in the 9,10-ketol-octadecadienoic acid-treated fruit than in the untreated control at 119 days after full bloom
-
damage and low-temperature treatment promote the expression of 1-aminocyclopropane-1-carboxylate oxidase
Q0PNH5
ACO1 transcript accumulation in the lower parts of elongating internodes
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D179E
P31237
site-directed mutagenesis, 1% activity compared to the recombinant wild-type enzyme
G137P
P31237
site-directed mutagenesis, 98% activity compared to the recombinant wild-type enzyme
H177Q
P31237
site-directed mutagenesis, 1% activity compared to the recombinant wild-type enzyme
K158A
P31237
site-directed mutagenesis, 1% activity compared to the recombinant wild-type enzyme
K158C
P31237
site-directed mutagenesis, 1% activity compared to the recombinant wild-type enzyme
K172A
P31237
site-directed mutagenesis, 85% activity compared to the recombinant wild-type enzyme
K172C
P31237
site-directed mutagenesis, 64% activity compared to the recombinant wild-type enzyme
G289S
-, H9ZYN5
the enzyme activity of the mutant is 3times as high as that of the wild type enzyme
H216D
-, H9ZYN5
the mutant shows 76% of wild type activity
H216D/D218E
-, H9ZYN5
the mutant shows 78% of wild type activity
H216D/D218E/H273Q
-, H9ZYN5
the mutant does not completely lose catalytic activity
H273Q
-, H9ZYN5
the mutant shows 62% of wild type activity
C133A
Malus x domestica
-
the mutant showsincreased activity compared to the wild type enzyme
C133P
Malus x domestica
-
the mutant shows slightly increased activity compared to the wild type enzyme
C165A
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
C28A
Malus x domestica
-
the mutant shows increased activity compared to the wild type enzyme
E294F
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
E297L
Malus x domestica
-
the mutant shows strongly increased activity compared to the wild type enzyme
E301D
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
E301L
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
F187Y
Malus x domestica
-
the mutant shows increased activity compared to the wild type enzyme
F300Q
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
F300Y
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
K144E
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
K158E
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
K158L
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
K158Q
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
K158Q/R175E
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
K158Q/R175Q
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
K158R
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
K158R/R175Q
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
K172E
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
K199E
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
K230E
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
K230Q
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
K230R
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
K292E
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
K292R
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
K296E
Malus x domestica
-
the mutant shows increased activity compared to the wild type enzyme
N216F
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
P298A
Malus x domestica
-
the mutant shows strongly increased activity compared to the wild type enzyme
Q188A
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
Q188K
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
Q188N
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
R175A
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
R175E
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
R175E/R244K
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
R175E/S246A
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
R175E/T157A
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
R175G
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
R175H
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
R175K
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
R175Q
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
R244A
Malus x domestica
-
enzymic activity about 20% of wild-type
R244G
Malus x domestica
-
enzymic activity about 20% of wild-type
R244K
Malus x domestica
-
enzymic activity about 20% of wild-type
R244K
Malus x domestica
-
the mutant is less active than the native enzyme and has a 5fold higher Km value for 1-aminocyclopropane-1-carboxylate
R244K/S246A
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
R244K/S246A/T157A
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
R244K/T157A
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
R299E
Malus x domestica
-
inactive
R299H
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
R299K
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
R299L
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
S246A
Malus x domestica
-
enzymic activity about 50% of wild-type
S246A
Malus x domestica
-
the mutant is less active than the native enzyme and has a 3fold higher Km value for 1-aminocyclopropane-1-carboxylate
S246F
Malus x domestica
-
enzymic activity less than 5% of wild-type
S246G
Malus x domestica
-
enzymic activity about 50% of wild-type
S246T
Malus x domestica
-
enzymic activity less than 5% of wild-type
S246Y
Malus x domestica
-
enzymic activity less than 5% of wild-type
S257A
Malus x domestica
-
KM-value similar to wild-type
T157A
Malus x domestica
-
enzymic activity about 40% of wild-type
T157A
Malus x domestica
-
the mutation does not affect the Km for 1-aminocyclopropane-1-carboxylate but drastically reduces enzyme activity
V159G
Malus x domestica
-
enzymic activity about 30% of wild-type
W203F
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
Y251F
Malus x domestica
-
the mutant shows reduced activity compared to the wild type enzyme
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
R287G
-, H9ZYN5
the activity of the mutant is remarkably decreased to nearly 40% compared to the wild type enzyme
additional information
Q43404
antisense expression of the enzyme in Petunia x hybrida leads to delayed flower senescence and reduced ethylene production in transgenic shoots, overview
additional information
-
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
-
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
agriculture
-
plants transformed with an 1-aminocyclopropane-1-carboxylate oxidase antisense constructs show reduced ethylene production and a delayed senescence
agriculture
-
plants transformed with 1-aminocyclopropane-1-carboxylate oxidase 1 and 2 antisense constructs show a significantly reduced post-harvest ethylene production