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EC Tree
IUBMB Comments 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.
The expected taxonomic range for this enzyme is: Chamberlinius hualienensis
Synonyms
ChuaMOX ,
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ChuaMOX
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(R)-mandelonitrile + O2 = benzoyl cyanide + H2O2
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(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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(3E,5E)-2-hydroxydeca-3,5-dienenitrile + O2
(3E,5E)-2-oxodeca-3,5-dienenitrile + H2O2
10% of the activity with (R)-mandelonitrile
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(E)-2-hydroxy-4-phenylbut-3-enenitrile + O2
(3E)-2-oxo-4-phenylbut-3-enenitrile + H2O2
29% of the activity with (R)-mandelonitrile
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(R)-mandelonitrile + O2
benzoyl cyanide + H2O2
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enzyme stoichiometrically catalyzes oxygen consumption and synthesis of benzoyl cyanide and hydrogen peroxide from mandelonitrile
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(R,S)-mandelonitrile + O2
benzoyl cyanide + H2O2
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2-(3-bromophenyl)-2-hydroxyacetonitrile + O2
(3-bromophenyl)(oxo)acetonitrile + H2O2
22% of the activity with (R)-mandelonitrile
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2-hydroxy-2-(2-methoxyphenyl)acetonitrile + O2
(2-methoxyphenyl)(oxo)acetonitrile + H2O2
17% of the activity with (R)-mandelonitrile
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FAD
sequence contains a FAD binding motif in the T22-S62 region
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ferric chloride
1 mM, 124% of initial activity
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8-hydroxyquinoline
1 mM, 56% residual activity
potassium cyanide
1 mM, 12.7% residual activity
Sodium azide
1 mM, 28.6% residual activity
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2.1
(R,S)-mandelonitrile
pH 5.0, 25°C
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3.5
80% of maximum activity
5
80% of maximum activity
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30
90% of maximum activity
40
90% of maximum activity
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UniProt
brenda
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brenda
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physiological function
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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A0A173MZJ8_9MYRI
593
0
64605
TrEMBL
-
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monomer
1 * 67000, SDS-PAGE, 1 * 62818, calculated
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glycoprotein
sequence contains six predicted N-glycosylation sites at resiudes N57, N79, N94, N149, N406, and N491
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8
25-50 °C, 1 h, 80% residual activity
739691
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70
1 h, complete loss of activity
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Ishida, Y; Kuwahara, Y.; Dadashipour, M; Ina, A; Yamaguchi, T; Morita, M.; Ichiki, Y; Asano, Y
A sacrificial millipede altruistically protects its swarm using a drone blood enzyme, mandelonitrile oxidase
Sci. Rep.
6
26998
2016
Chamberlinius hualienensis (A0A173MZJ8), Chamberlinius hualienensis
brenda
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Enzyme Nomenclature
1.1.3.49 (R)-mandelonitrile oxidase
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