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Literature summary for 1.10.3.11 extracted from

  • Crichton, P.; Albury, M.; Affourtit, C.; Moore, A.
    Mutagenesis of the Sauromatum guttatum alternative oxidase reveals features important for oxygen binding and catalysis (2010), Biochim. Biophys. Acta, 1797, 732-737.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Schizosaccharomyces pombe strain Sp.011, subcloning in Escherichia coli strains JM101 and 110 Sauromatum venosum

Protein Variants

Protein Variants Comment Organism
C172A site-directed mutagenesis, the mutant shows reduced activity and oxygen affinity compared to the wild-type enzyme Sauromatum venosum
T179A site-directed mutagenesis, the mutant shows reduced activity and oxygen affinity compared to the wild-type enzyme Sauromatum venosum
W206F site-directed mutagenesis, inactive mutant Sauromatum venosum
W206Y site-directed mutagenesis, inactive mutant Sauromatum venosum
Y253F site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Sauromatum venosum
Y299F site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Sauromatum venosum

Inhibitors

Inhibitors Comment Organism Structure
octyl gallate
-
Sauromatum venosum
sialic acid
-
Sauromatum venosum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0046
-
O2 mutant T179A, pH and temperature not specified in the publication Sauromatum venosum
0.0092
-
O2 mutant C172A, pH and temperature not specified in the publication Sauromatum venosum
0.017
-
O2 mutant Y299F, pH and temperature not specified in the publication Sauromatum venosum
0.018
-
O2 wild-type enzyme, pH and temperature not specified in the publication Sauromatum venosum
0.0205
-
O2 mutant Y253F, pH and temperature not specified in the publication Sauromatum venosum

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Sauromatum venosum 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 ubiquinol + O2 Sauromatum venosum
-
2 ubiquinone + 2 H2O
-
?

Organism

Organism UniProt Comment Textmining
Sauromatum venosum P22185
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ubiquinol + O2
-
Sauromatum venosum 2 ubiquinone + 2 H2O
-
?

Synonyms

Synonyms Comment Organism
alternative oxidase
-
Sauromatum venosum
AOX
-
Sauromatum venosum

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.00007
-
mutant Y299F, pH and temperature not specified in the publication Sauromatum venosum octyl gallate
0.00008
-
mutants C172A and T179A, pH and temperature not specified in the publication Sauromatum venosum octyl gallate
0.00009
-
wild-type enzyme, pH and temperature not specified in the publication Sauromatum venosum octyl gallate
0.0001
-
mutant Y253F, pH and temperature not specified in the publication Sauromatum venosum octyl gallate
0.012
-
mutant T179A, pH and temperature not specified in the publication Sauromatum venosum sialic acid
0.016
-
wild-type enzyme, pH and temperature not specified in the publication Sauromatum venosum sialic acid
0.018
-
mutant Y299F, pH and temperature not specified in the publication Sauromatum venosum sialic acid
0.019
-
mutant C172A, pH and temperature not specified in the publication Sauromatum venosum sialic acid
0.02
-
mutant Y253F, pH and temperature not specified in the publication Sauromatum venosum sialic acid

General Information

General Information Comment Organism
evolution the enzyme is found in mitochondria of all higher plants studied to date Sauromatum venosum
physiological function the alternative oxidase (AOX) is a non-protonmotive ubiquinol oxidase Sauromatum venosum