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Information on EC 1.10.3.11 - ubiquinol oxidase (non-electrogenic) and Organism(s) Sauromatum venosum and UniProt Accession P22185

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EC Tree
IUBMB Comments
The enzyme, described from the mitochondria of plants and some fungi and protists, is an alternative terminal oxidase that is not sensitive to cyanide inhibition and does not generate a proton motive force. Unlike the electrogenic terminal oxidases that contain hemes (cf. EC 1.10.3.10 and EC 1.10.3.14), this enzyme contains a dinuclear non-heme iron complex. The function of this oxidase is believed to be dissipating excess reducing power, minimizing oxidative stress, and optimizing photosynthesis in response to changing conditions.
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Sauromatum venosum
UNIPROT: P22185
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The taxonomic range for the selected organisms is: Sauromatum venosum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
hide
2
ubiquinol
+
O2
=
2
ubiquinone
+
2
H2O
2
+
=
2
+
2
Synonyms
alternative oxidase, aox1a, mitochondrial alternative oxidase, alternative oxidases, aox1b, cyanide-insensitive oxidase, cyanide-resistant oxidase, aox1c, cioab, cyanide-resistant alternative oxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alternative oxidase
-
alternative oxidase
-
-
cyanide-insensitive alternative oxidase
-
-
cyanide-insensitive oxidase
-
-
-
-
cyanide-resistant alternative oxidase
-
-
cytochrome bb3 oxidase
-
-
-
-
plant alternative oxidase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
ubiquinol:O2 oxidoreductase (non-electrogenic)
The enzyme, described from the mitochondria of plants and some fungi and protists, is an alternative terminal oxidase that is not sensitive to cyanide inhibition and does not generate a proton motive force. Unlike the electrogenic terminal oxidases that contain hemes (cf. EC 1.10.3.10 and EC 1.10.3.14), this enzyme contains a dinuclear non-heme iron complex. The function of this oxidase is believed to be dissipating excess reducing power, minimizing oxidative stress, and optimizing photosynthesis in response to changing conditions.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 ubiquinol + O2
2 ubiquinone + 2 H2O
show the reaction diagram
-
-
-
?
NADH + O2
?
show the reaction diagram
-
-
-
-
?
ubiquinol + O2
ubiquinone + H2O
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 ubiquinol + O2
2 ubiquinone + 2 H2O
show the reaction diagram
-
-
-
?
ubiquinol + O2
ubiquinone + H2O
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
octyl gallate
-
octyl gallate
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Carbonyl cyanide m-chlorophenylhydrazone
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0046 - 0.0205
O2
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00007 - 0.0001
octyl gallate
0.012 - 0.02
sialic acid
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the alternative oxidase protein is expressed in the inner mitochondrial membrane in its reduced (active) form
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme is found in mitochondria of all higher plants studied to date
physiological function
the alternative oxidase (AOX) is a non-protonmotive ubiquinol oxidase
metabolism
-
the alternative oxidase actively competes with the cytochrome pathway for reducing equivalents and contributes up to 24% to the overall respiratory activity
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AOX1_SAUVE
349
0
38931
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
-
mature enzyme, SDS-PAGE
42000
-
precursor, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
the enzyme exists mainly as a non-covalently linked dimer when expressed in Schizosaccharomyces pombe
homodimer
-
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C172A
site-directed mutagenesis, the mutant shows reduced activity and oxygen affinity compared to the wild-type enzyme
T179A
site-directed mutagenesis, the mutant shows reduced activity and oxygen affinity compared to the wild-type enzyme
W206F
site-directed mutagenesis, inactive mutant
W206Y
site-directed mutagenesis, inactive mutant
Y253F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y299F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E217A
-
the mutation results in the loss of AOX activity
E270N
-
the mutation results in the loss of AOX activity
Y253F
-
the mutant exhibits a mitochondrial antimycin-resistant respiratory activity that is comparable with that of the wild type
Y275F
-
the mutant exhibits barely detectable mitochondrial antimycin-resistant respiratory activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in Schizosaccharomyces pombe strain Sp.011, subcloning in Escherichia coli strains JM101 and 110
expressed in Schizosaccharomyces pombe and Escherichia coli
-
expressed in Schizosaccharomyces pombe mitochondria and spheroplasts
-
expressed in Schizosaccharomyces pombe strain sp.011
-
wild type and mutant enzymes are expressed in Schizosaccharomyces pombe strain sp.011
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Siedow, J.N.; Umbach, A.L.; Moore. A.L.
The active site of the cyanide-resistant oxidase from plant mitochondria contains a binuclear iron center
FEBS Lett.
362
10-14
1995
Sauromatum venosum
Manually annotated by BRENDA team
Moore, A.L.; Umbach, A.L.; Siedow, J.N.
Structure-function relationships of the alternative oxidase of plant mitochondria: a model of the active site
J. Bioenerg. Biomembr.
27
367-377
1995
Arum maculatum, Sauromatum venosum
Manually annotated by BRENDA team
Albury, M.S.; Dudley, P.; Watts, F.Z.; Moore, A.L.
Targeting the plant alternative oxidase protein to Schizosaccharomyces pombe mitochondria confers cyanide-insensitive respiration
J. Biol. Chem.
271
17062-17066
1996
Sauromatum venosum
Manually annotated by BRENDA team
Affourtit, C.; Albury, M.S.; Krab, K.; Moore, A.L.
Functional expression of the plant alternative oxidase affects growth of the yeast Schizosaccharomyces pombe
J. Biol. Chem.
274
6212-6218
1999
Sauromatum venosum
Manually annotated by BRENDA team
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
J. Biol. Chem.
277
1190-1194
2002
Sauromatum venosum
Manually annotated by BRENDA team
Crichton, P.; Albury, M.; Affourtit, C.; Moore, A.
Mutagenesis of the Sauromatum guttatum alternative oxidase reveals features important for oxygen binding and catalysis
Biochim. Biophys. Acta
1797
732-737
2010
Sauromatum venosum (P22185), Sauromatum venosum
Manually annotated by BRENDA team