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Literature summary for 1.13.12.19 extracted from

  • Johansson, N.; Persson, K.; Norbeck, J.; Larsson, C.
    Expression of NADH-oxidases enhances ethylene productivity in Saccharomyces cerevisiae expressing the bacterial EFE (2017), Biotechnol. Bioprocess Eng., 22, 195-199 .
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, sequence comparisons with Pseudomonas digitatum and Pseudomonas chrysogenum, recombinant expression in Saccharomyces cerevisiae Pseudomonas savastanoi pv. phaseolicola
DNA and amino acid sequence determination and analysis, sequence comparisons with Pseudomonas digitatum and Pseudomonas chrysogenum, recombinant expression in Saccharomyces cerevisiae Pseudomonas syringae pv. pisi

Protein Variants

Protein Variants Comment Organism
A199G site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
A199G site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. pisi
C280F site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
C280F site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. pisi
D191A site-directed mutagenesis, inactive mutant Pseudomonas savastanoi pv. phaseolicola
D191A site-directed mutagenesis, inactive mutant Pseudomonas syringae pv. pisi
E235D site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
E235D site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme Pseudomonas syringae pv. pisi
F278Y site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
F278Y site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Pseudomonas syringae pv. pisi
H189A site-directed mutagenesis, inactive mutant Pseudomonas savastanoi pv. phaseolicola
H189A site-directed mutagenesis, inactive mutant Pseudomonas syringae pv. pisi
H233A site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
H233A site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Pseudomonas syringae pv. pisi
H268A site-directed mutagenesis, inactive mutant Pseudomonas savastanoi pv. phaseolicola
H268A site-directed mutagenesis, inactive mutant Pseudomonas syringae pv. pisi
I254M site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
I254M site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme Pseudomonas syringae pv. pisi
I304N site-directed mutagenesis, inactive mutant Pseudomonas savastanoi pv. phaseolicola
I304N site-directed mutagenesis, inactive mutant Pseudomonas syringae pv. pisi
I322V site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
I322V site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme Pseudomonas syringae pv. pisi
L22M site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
L22M site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme Pseudomonas syringae pv. pisi
additional information a loop deletion mutant is inactive Pseudomonas savastanoi pv. phaseolicola
additional information a loop deletion mutant is inactive Pseudomonas syringae pv. pisi
R236S site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
R236S site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. pisi
V172T site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
V172T site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme Pseudomonas syringae pv. pisi
V212Y/E213S site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas savastanoi pv. phaseolicola
V212Y/E213S site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. pisi

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ dependent on, residues H189, D191 and H268 are responsible for binding the Fe(II) ligand Pseudomonas savastanoi pv. phaseolicola
Fe2+ dependent on, residues H189, D191 and H268 are responsible for binding the Fe(II) ligand Pseudomonas syringae pv. pisi

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-oxoglutarate + O2 Pseudomonas savastanoi pv. phaseolicola
-
ethylene + 3 CO2 + H2O
-
?
2-oxoglutarate + O2 Pseudomonas syringae pv. pisi
-
ethylene + 3 CO2 + H2O
-
?

Organism

Organism UniProt Comment Textmining
Pseudomonas savastanoi pv. phaseolicola P32021
-
-
Pseudomonas syringae pv. pisi Q9Z3T0
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + O2
-
Pseudomonas savastanoi pv. phaseolicola ethylene + 3 CO2 + H2O
-
?
2-oxoglutarate + O2
-
Pseudomonas syringae pv. pisi ethylene + 3 CO2 + H2O
-
?

Synonyms

Synonyms Comment Organism
EFE
-
Pseudomonas savastanoi pv. phaseolicola
EFE
-
Pseudomonas syringae pv. pisi
ethylene forming enzyme
-
Pseudomonas savastanoi pv. phaseolicola
ethylene forming enzyme
-
Pseudomonas syringae pv. pisi

General Information

General Information Comment Organism
evolution the enzyme belongs to a subclass of 2-oxoglutarate/Fe(II) dependent dioxygenases, structure-function analysis of the ethylene forming subclass of 2-oxoglutarate/Fe(II)-dependent dioxygenases, overview Pseudomonas syringae pv. pisi
evolution the enzyme belongs to a subclass of 2-oxoglutarate/Fe(II) dependent dioxygenases, structure-function analysis of the ethylene forming subclass of 2-oxoglutarate/Fe(II)-dependent dioxygenases,overview Pseudomonas savastanoi pv. phaseolicola
additional information three of the amino acids correlating with ethylene production are located in the predicted 2-oxoglutarate binding domain, a protein domain specific for the EFE-class that is essential for activity. Residues H189, D191 and H268 are responsible for binding the Fe(II) ligand Pseudomonas savastanoi pv. phaseolicola
additional information three of the amino acids correlating with ethylene production are located in the predicted 2-oxoglutarate binding domain, a protein domain specific for the EFE-class that is essential for activity. Residues H189, D191 and H268 are responsible for binding the Fe(II) ligand Pseudomonas syringae pv. pisi