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Literature summary for 1.10.3.11 extracted from

  • Albury, M.S.; Affourtit, C.; Crichton, P.G.; Moore, A.L.
    Structure of the plant alternative oxidase. Site-directed mutagenesis provides new information on the active site and membrane topology (2002), J. Biol. Chem., 277, 1190-1194.
    View publication on PubMed
Search for more literature for 1.10.3.11

Activating Compound

Activating Compound Comment Organism Structure
Carbonyl cyanide m-chlorophenylhydrazone
-
 Sauromatum venosum

Cloned(Commentary)

Cloned (Comment) Organism
wild type and mutant enzymes are expressed in Schizosaccharomyces pombe strain sp.011 Sauromatum venosum

Protein Variants

Protein Variants Comment Organism
E217A the mutation results in the loss of AOX activity Sauromatum venosum
E270N the mutation results in the loss of AOX activity Sauromatum venosum
Y253F the mutant exhibits a mitochondrial antimycin-resistant respiratory activity that is comparable with that of the wild type Sauromatum venosum
Y275F the mutant exhibits barely detectable mitochondrial antimycin-resistant respiratory activity Sauromatum venosum

Inhibitors

Inhibitors Comment Organism Structure
additional information the respiratory activity exhibited by mitochondria containing the wild type AOX is partially resistant to antimycin A (about 18% of the NADH-dependent rate) Sauromatum venosum
octyl gallate
-
 Sauromatum venosum

Localization

Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

Metals/Ions Comment Organism Structure
Iron a di-iron protein Sauromatum venosum

Organism

Organism UniProt Comment Textmining
Sauromatum venosum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADH + O2
-
 Sauromatum venosum ?
-
 ?

Synonyms

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