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Literature summary for 1.14.17.4 extracted from

  • Dilley, D.R.; Wang, Z.; Kadirjan-Kalbach, D.K.; Ververidis, F.; Beaudry, R.; Padmanabhan, K.
    1-Aminocyclopropane-1-carboxylic acid oxidase reaction mechanism and putative post-translational activities of the ACCO protein (2013), AoB Plants, 5, plt03 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.17.4

Activating Compound

Activating Compound Comment Organism Structure
alpha-aminoisobutryric acid activates enzyme ACCO, prevents enzyme inactivation Malus domestica
bicarbonate activates enzyme ACCO Malus domestica
cyanide activates enzyme ACCO, prevents enzyme inactivation Malus domestica
additional information in the presence of cyanide (CN2) and alpha-aminoisobutryric acid, enzyme ACCO is activated and enzyme inactivation is prevented Malus domestica

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE) plysS Malus domestica

Protein Variants

Protein Variants Comment Organism
C133A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
C133P site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Malus domestica
C165A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
C283A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
E294F site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
E297L site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
E301D site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
E301L site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
F187Y site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Malus domestica
F300Q site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
F300Y site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
K144E site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
K158E site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
K158L site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
K158Q site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
K158Q/R175E site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
K158Q/R175Q site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
K158R site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
K158R/R175Q site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
K172E site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
K199E site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
K230Q site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
K230R site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
K230W site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
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 Malus domestica
K292R site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
K296E site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
N216F site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
P298A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
Q188A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
Q188K site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
Q188N site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
R175A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
R175E site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
R175E/R244K site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
R175E/S146A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
R175E/T157A site-directed mutagenesis, almost inactive mutant Malus domestica
R175G site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
R175H site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
R175K site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
R175Q site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
R244K site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
R244K/S246A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
R244K/T157A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
R299E site-directed mutagenesis, inactive mutant Malus domestica
R299H site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
R299K site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
R299L site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
S246A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
S246A/R244K/T157A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
T157A site-directed mutagenesis, the single-point mutation does not affect the substrate 1-aminocyclopropane-1-carboxylate Km but drastically reduces enzyme ACCO activity Malus domestica
W203F site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica
Y251F site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Malus domestica

Inhibitors

Inhibitors Comment Organism Structure
pyridoxal 5'-phosphate a competitive inhibitor of enzyme ACCO with respect to ascorbate. Pyridoxal 5'-phosphate may form a Schiff base with the 1-amino group of lysine blocking a binding site for ascorbate Malus domestica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Malus domestica
0.031
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant E301L, pH 7.2, 20°C Malus domestica
0.031
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant R299L, pH 7.2, 20°C Malus domestica
0.036
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant F300Y, pH 7.2, 20°C Malus domestica
0.046
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant K158R, pH 7.2, 20°C Malus domestica
0.047
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant R299K, pH 7.2, 20°C Malus domestica
0.051
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged wild-type enzyme, pH 7.2, 20°C Malus domestica
0.06
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant K158Q, pH 7.2, 20°C Malus domestica
0.062
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant C28A, pH 7.2, 20°C Malus domestica
0.062
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant P298A, pH 7.2, 20°C Malus domestica
0.062
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant Y251F, pH 7.2, 20°C Malus domestica
0.063
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant W203F, pH 7.2, 20°C Malus domestica
0.07
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant T157A, pH 7.2, 20°C Malus domestica
0.083
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant R175K, pH 7.2, 20°C Malus domestica
0.09
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant F187Y, pH 7.2, 20°C Malus domestica
0.094
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant R299H, pH 7.2, 20°C Malus domestica
0.129
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant F300Q, pH 7.2, 20°C Malus domestica
0.139
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant R175H, pH 7.2, 20°C Malus domestica
0.142
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant R175G, pH 7.2, 20°C Malus domestica
0.158
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant N216F, pH 7.2, 20°C Malus domestica
0.173
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant K158E, pH 7.2, 20°C Malus domestica
0.175
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant R244K, pH 7.2, 20°C Malus domestica
0.175
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant R244K/S246A, pH 7.2, 20°C Malus domestica
0.193
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant R175A, pH 7.2, 20°C Malus domestica
0.206
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant K158Q/R175Q, pH 7.2, 20°C Malus domestica
0.218
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant R175Q, pH 7.2, 20°C Malus domestica
0.245
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant S246A/R244K/T157A , pH 7.2, 20°C Malus domestica
0.277
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant S246A, pH 7.2, 20°C Malus domestica
0.279
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant K158R/R175Q, pH 7.2, 20°C Malus domestica
0.281
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant K158L, pH 7.2, 20°C Malus domestica
0.287
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant Q188N, pH 7.2, 20°C Malus domestica
0.379
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant R175E, pH 7.2, 20°C Malus domestica
0.659
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant K158Q/R175E, pH 7.2, 20°C Malus domestica
1.2
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant R175E/S246A, pH 7.2, 20°C Malus domestica
2.3
-
 1-aminocyclopropane-1-carboxylate recombinant His-tagged mutant R175E/T157A, pH 7.2, 20°C Malus domestica

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ required for catalysis Malus domestica

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1-aminocyclopropane-1-carboxylate + ascorbate + O2 Malus domestica
-
 ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Malus domestica Q00985
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein ACC oxidase is subject to autophosphorylaton in vitro and promotes phosphorylation of some apple fruit proteins in a ripening-dependent manner Malus domestica

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE) plysS by nickel affinity chromatography, ammonium sulfate precipitation Malus domestica

Reaction

Reaction Comment Organism Reaction ID
1-aminocyclopropane-1-carboxylate + ascorbate + O2 = ethene + cyanide + dehydroascorbate + CO2 + 2 H2O the reaction pathway incorporates cyanide as an ACCO/Fe(II) ligand after reaction turnover. The cyanide ligand is likely displaced upon binding of ACC and ascorbate to provide a binding site for oxygen Malus domestica
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.000000064
-
 recombinant His-tagged mutant R175E/T157A, pH 7.2, 20°C Malus domestica
0.0000024
-
 recombinant His-tagged mutant R175E/R244K, pH 7.2, 20°C Malus domestica
0.0000029
-
 recombinant His-tagged mutant R244K/T157A, pH 7.2, 20°C Malus domestica
0.0000033
-
 recombinant His-tagged mutant K158E, pH 7.2, 20°C Malus domestica
0.0000083
-
 recombinant His-tagged mutant R299H, pH 7.2, 20°C Malus domestica
0.00001
-
 recombinant His-tagged mutant S246A/R244K/T157A, pH 7.2, 20°C Malus domestica
0.000012
-
 recombinant His-tagged mutant K158Q/R175Q, pH 7.2, 20°C Malus domestica
0.000021
-
 recombinant His-tagged mutant K158Q/R175E, pH 7.2, 20°C Malus domestica
0.00004
-
 recombinant His-tagged mutant R299L, pH 7.2, 20°C Malus domestica
0.000061
-
 recombinant His-tagged mutant R175E/S246A, pH 7.2, 20°C Malus domestica
0.00007
-
 recombinant His-tagged mutant K158L, pH 7.2, 20°C Malus domestica
0.000083
-
 recombinant His-tagged mutant R175Q, pH 7.2, 20°C Malus domestica
0.00011
-
 recombinant His-tagged mutant K158Q, pH 7.2, 20°C Malus domestica
0.00015
-
 recombinant His-tagged mutant K158R/R175Q, pH 7.2, 20°C Malus domestica
0.00015
-
 recombinant His-tagged mutant R175H, pH 7.2, 20°C Malus domestica
0.00017
-
 recombinant His-tagged mutant R175G, pH 7.2, 20°C Malus domestica
0.0002
-
 recombinant His-tagged mutant T157A, pH 7.2, 20°C Malus domestica
0.00022
-
 recombinant His-tagged mutant K292E, pH 7.2, 20°C Malus domestica
0.00024
-
 recombinant His-tagged mutant R175E, pH 7.2, 20°C Malus domestica
0.00025
-
 recombinant His-tagged mutant K158R, pH 7.2, 20°C Malus domestica
0.00028
-
 recombinant His-tagged mutant R175A, pH 7.2, 20°C Malus domestica
0.00065
-
 recombinant His-tagged mutant R175K, pH 7.2, 20°C Malus domestica
0.00092
-
 recombinant His-tagged mutant R244K/S246A, pH 7.2, 20°C Malus domestica
0.00116
-
 recombinant His-tagged mutant R244K, pH 7.2, 20°C Malus domestica
0.00128
-
 recombinant His-tagged mutant K292R, pH 7.2, 20°C Malus domestica
0.00147
-
 recombinant His-tagged mutant R299K, pH 7.2, 20°C Malus domestica
0.00174
-
 recombinant His-tagged mutant S246A, pH 7.2, 20°C Malus domestica
0.00348
-
 recombinant His-tagged wild-type enzyme, pH 7.2, 20°C Malus domestica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-aminocyclopropane-1-carboxylate + ascorbate + O2
-
 Malus domestica ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
-
 ?
additional information ACC oxidase amino acids Cys28, Thr157, Lys158, Arg175, Gln188, Lys199, Arg244, Ser246, Lys230, Lys292, Glu294, Glu297, Arg299, Phe300 and Glu301 are important residues affecting enzyme activity. alpha-Aminoisobutryric acid is an alternative substrate for enzyme ACCO producing acetone, ammonia and CO2 Malus domestica ?
-
 ?

Synonyms

Synonyms Comment Organism
1-aminocyclopropane-1-carboxylic acid oxidase
-
 Malus domestica
ACC oxidase
-
 Malus domestica
ACCO
-
 Malus domestica
ACCO1
-
 Malus domestica

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
 assay at Malus domestica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at Malus domestica

Cofactor

Cofactor Comment Organism Structure
ascorbate required for catalysis, residue Lys292 is essential for enzyme activation by ascorbate Malus domestica

General Information

General Information Comment Organism
metabolism the enzyme catalyzes the terminal step in ethylene biosynthesis converting ACC to ethylene, cyanide, CO2, dehydroascorbate and water with inputs of Fe(II), ascorbate, bicarbonate (as activators) and oxygen Malus domestica
additional information the binding sites for ACC, bicarbonate and ascorbic acid for Malus domestica ACCO1 include Arg175, Arg244, Ser246, Lys158, Lys292, Arg299 and Phe300. Glu297, Phe300 and Glu301 in alpha-helix 11 are also important for the ACCO reaction. The ACC substrate has been shown to bind to ACCO/Fe(II) in a bidentate manner. ACC oxidase contains several amino acid sequence motifs for putative protein-protein interactions, phosphokinases and cysteine protease. Residue Thr157 is essential for ACCO activity in a protein structural role. Protein-protein interactions and phosphorylation studies with ACCO, overview Malus domestica
physiological function enzyme ACCO is involved in ethylene biosynthesis. ACCO may be also involved in the ethylene signal transduction pathway not directly linked to the ACCO reaction and may playa role in signal transduction after post-translational processing by functioning as protease and as regulator of 1-aminocyclopropane-1-carboxylic acid synthase (Acs2) gene expression, overview. ACC oxidase is subject to autophosphorylaton in vitro and promotes phosphorylation of some apple fruit proteins in a ripening-dependent manner Malus domestica