Information on EC 1.1.3.40 - D-mannitol oxidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.3.40
-
RECOMMENDED NAME
GeneOntology No.
D-mannitol oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
mannitol + O2 = mannose + H2O2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
mannitol:oxygen oxidoreductase (cyclizing)
Also catalyses the oxidation of D-arabinitol and, to a lesser extent, D-glucitol (sorbitol), whereas L-arabinitol is not a good substrate. The enzyme from the snails Helix aspersa and Arion ater is found in a specialised tubular organelle that has been termed the mannosome.
CAS REGISTRY NUMBER
COMMENTARY hide
73562-29-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
aquatic snail, low levels
-
-
Manually annotated by BRENDA team
common garden snail; terrestrial snail
-
-
Manually annotated by BRENDA team
terrestrial gastropod mollusc, slug
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D,L-threitol + O2
? + H2O2
show the reaction diagram
-
7% activity compared with D-arabinitol
-
-
?
D-arabinitol + O2
arabinose + H2O2
show the reaction diagram
D-glucitol + O2
D-glucose + H2O2
show the reaction diagram
D-glycero-D-galactoheptitol + O2
? + H2O2
show the reaction diagram
D-mannitol + O2
mannose + H2O2
show the reaction diagram
galactitol + O2
D-galactose + H2O2
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-mannitol + O2
mannose + H2O2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cd2+
-
mannitol oxidase is inhibited by heavy metals more than other oxidases
deoxycholate
-
1% w/v: 36% inhibition, deoxycholate, 1%, readily releases membrane-bound activity, but is slightly inhibitory
n-butanol
-
n-butyl alcohol
Pb2+
-
mannitol oxidase is inhibited by heavy metals more than other oxidases
Zn2+
-
mannitol oxidase is inhibited by heavy metals more than other oxidases
additional information
-
no inhibition by cyanide and metal chelators such as EDTA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no requirement or activation by sulfhydryl reagents, such as DTT
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17.3 - 54.6
D-arabinitol
5.2 - 15.4
D-mannitol
0.04
O2
-
oxygen, substrate: D-mannitol
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0137
-
esophagus and crop
0.984
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
8 - 8.5
-
alkaline pH-optimum
8
-
assay at
additional information
-
alkaline pH-optimum; pI: 5.4-5.6
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 10
-
at pH 6.5 and pH 10.0: about 50% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
highest activity
Manually annotated by BRENDA team
-
very poor
Manually annotated by BRENDA team
-
substantial activity
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
mannitol oxidase activity elutes near the void volume of Sephacryl S300 columns which suggests a high molecular weight
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no modification
-
not a glycoprotein, the presence of amino sugar residues cannot be ruled out
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11
-
enzyme relatively stable at alkaline pH, pH 11: 30% of maximum activity remains
287629
additional information
-
enzyme relatively stable at alkaline pH
287629
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of EDTA and/or DTT does not appreciably improve stability
-
glycerol stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20% glycerol, one week, remains active
-
5°C, Tris buffer, 10% glycerol, 4 days, 35% activity retained
-
5°C, Tris buffer, 20% glycerol, 4 days, 69% activity retained
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
-
solubilization and partial purification. Both ionic and non-ionic as well as zwitterionic detergents are effective in solubilizing mannitol oxidase, deoxycholate, 1%, readily releases membrane-bound activity, but is slightly inhibitory
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