Information on EC 1.1.3.49 - (R)-mandelonitrile oxidase

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The expected taxonomic range for this enzyme is: Chamberlinius hualienensis

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EC NUMBER
COMMENTARY hide
1.1.3.49
-
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RECOMMENDED NAME
GeneOntology No.
(R)-mandelonitrile oxidase
-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-mandelonitrile + O2 = benzoyl cyanide + H2O2
show the reaction diagram
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
(R)-mandelonitrile:oxygen oxidoreductase
Contains FAD. The enzyme, characterized from the millipede Chamberlinius hualienensis, is segregated from its substrate, which is contained in special sacs. The sacs are ruptured during defensive behavior, allowing the enzyme and substrate to mix in special reaction chambers leading to production of the defensive chemical benzoyl cyanide.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
A0A173MZJ8
UniProt
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
A0A173MZJ8
the enzyme stoichiometrically catalyzes oxygen consumption and synthesis of benzoyl cyanide and hydrogen peroxide from mandelonitrile. The enzymatic activity is suppressed at a blood pH of 7, and the enzyme is segregated by membranes of defensive sacs from its substrate mandelonitrile which has a pH of 4.6, the optimum pH for ChuaMOX activity. Strong body muscle contractions are necessary for de novo synthesis of benzoyl cyanide
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3E,5E)-2-hydroxydeca-3,5-dienenitrile + O2
(3E,5E)-2-oxodeca-3,5-dienenitrile + H2O2
show the reaction diagram
A0A173MZJ8
10% of the activity with (R)-mandelonitrile
-
-
?
(E)-2-hydroxy-4-phenylbut-3-enenitrile + O2
(3E)-2-oxo-4-phenylbut-3-enenitrile + H2O2
show the reaction diagram
A0A173MZJ8
29% of the activity with (R)-mandelonitrile
-
-
?
(R)-mandelonitrile + O2
benzoyl cyanide + H2O2
show the reaction diagram
A0A173MZJ8
-
enzyme stoichiometrically catalyzes oxygen consumption and synthesis of benzoyl cyanide and hydrogen peroxide from mandelonitrile
-
?
(R,S)-mandelonitrile + O2
benzoyl cyanide + H2O2
show the reaction diagram
A0A173MZJ8
-
-
-
?
2-(3-bromophenyl)-2-hydroxyacetonitrile + O2
(3-bromophenyl)(oxo)acetonitrile + H2O2
show the reaction diagram
A0A173MZJ8
22% of the activity with (R)-mandelonitrile
-
-
?
2-hydroxy-2-(2-methoxyphenyl)acetonitrile + O2
(2-methoxyphenyl)(oxo)acetonitrile + H2O2
show the reaction diagram
A0A173MZJ8
17% of the activity with (R)-mandelonitrile
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
A0A173MZJ8
sequence contains a FAD binding motif in the T22-S62 region
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ferric chloride
A0A173MZJ8
1 mM, 124% of initial activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8-hydroxyquinoline
A0A173MZJ8
1 mM, 56% residual activity
potassium cyanide
A0A173MZJ8
1 mM, 12.7% residual activity
Sodium azide
A0A173MZJ8
1 mM, 28.6% residual activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.1
(R,S)-mandelonitrile
A0A173MZJ8
pH 5.0, 25°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 4.5
A0A173MZJ8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5
A0A173MZJ8
80% of maximum activity
5
A0A173MZJ8
80% of maximum activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
A0A173MZJ8
90% of maximum activity
40
A0A173MZJ8
90% of maximum activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
A0A173MZJ8
calculated
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
A0A173MZJ8
gel filtration
67000
A0A173MZJ8
-
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
A0A173MZJ8
1 * 67000, SDS-PAGE, 1 * 62818, calculated
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
A0A173MZJ8
sequence contains six predicted N-glycosylation sites at resiudes N57, N79, N94, N149, N406, and N491
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
A0A173MZJ8
25-50 °C, 1 h, 80% residual activity
739691
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
A0A173MZJ8
1 h, complete loss of activity
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.3.49)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)