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Literature summary for 1.14.17.4 extracted from

  • Xiao, G.; Li, L.; Teng, K.; Chao, Y.; Han, L.
    Cloning and expression of the 1-aminocyclopropane-1-carboxylic oxidase gene from agrostis stolonifera (2016), Genet. Mol. Res., 15, gmr15049034.
    View publication on PubMed
Search for more literature for 1.14.17.4

Cloned(Commentary)

Cloned (Comment) Organism
gene ACO, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of FLAG-tagged enzyme ACO, recombinant expression of ACO in transgenic Nicotiana benthamiana plants via tranfection by Agrobacterium tumefaciens strain EHA105 under control of promoter CaMV35S Agrostis stolonifera

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Agrostis stolonifera 5737
-
additional information subcellular localization study Agrostis stolonifera
-
-
nucleus
-
 Agrostis stolonifera 5634
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the conserved domains of ACO enzyme from the ACO family of different species are identical by confirming Fe(II)-binding cofactors (His-Xaa-Asp-Xaa-His) and cosubstrate-binding motifs (Arg-Xaa-Ser) Agrostis stolonifera

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Agrostis stolonifera A0A161G0R4
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-aminocyclopropane-1-carboxylate + ascorbate + O2
-
 Agrostis stolonifera ethylene + cyanide + dehydroascorbate + CO2 + 2 H2O
-
 ?

Subunits

Subunits Comment Organism
? x * 36250, sequence calculation Agrostis stolonifera

Synonyms

Synonyms Comment Organism
1-aminocyclopropane-1-carboxylic oxidase
-
 Agrostis stolonifera
AsACO
-
 Agrostis stolonifera

Cofactor

Cofactor Comment Organism Structure
ascorbate
-
 Agrostis stolonifera

pI Value

Organism Comment pI Value Maximum pI Value
Agrostis stolonifera sequence calculation
-
 4.89

General Information

General Information Comment Organism
evolution the conserved domains of ACO enzyme from the ACO family of different species are identical by confirming Fe(II)-binding cofactors (His-Xaa-Asp-Xaa-His) and cosubstrate-binding motifs (Arg-Xaa-Ser) Agrostis stolonifera
metabolism the enzyme catalyzes the terminal step in ethylene biosynthesis Agrostis stolonifera