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Information on EC 1.1.3.40 - D-mannitol oxidase
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1.1.3.40 D-mannitol oxidaseIUBMB Comments
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.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
mannitol oxidase, d-mannitol oxidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-arabitol oxidase
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H2O2 generating mannitol oxidase
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H2O2-generating mannitol oxidase
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hydrogen peroxide-generating mannitol oxidase
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mannitol oxidase
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oxidase, mannitol
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-mannitol + O2 = D-mannose + H2O2
utilization of the sugar alcohols generally proceeds by an initial oxidation, producing a hexose
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D-mannitol + O2 = D-mannose + H2O2
also catalyses the oxidation of D-arabinitol and, to a lesser extent, D-glucitol: sorbitol, whereas L-arabinitol is not a good substrate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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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.
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CAS REGISTRY NUMBER
COMMENTARY
73562-29-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-arabinitol + O2
arabinose + H2O2
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122% activity compared with D-mannitol
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-
?
D-arabinitol + O2
arabinose + H2O2
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136% activity compared with D-mannitol
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-
?
D-glucitol + O2
D-glucose + H2O2
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20% activity compared with D-arabinitol
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-
?
D-glucitol + O2
D-glucose + H2O2
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26.5% activity compared with D-mannitol
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-
?
D-glucitol + O2
D-glucose + H2O2
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19.1% activity compared with D-mannitol
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?
D-glycero-D-galactoheptitol + O2
? + H2O2
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9% activity compared with D-arabinitol
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-
?
D-mannitol + O2
mannose + H2O2
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mannitol is a common and abundant carbohydrate component of plant food consumed by terrestrial gastropods, the presence and properties of mannitol oxidase imply an unusual route for mannitol metabolism via mannitol oxidase, hexokinase and phosphomannose isomerase
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?
D-mannitol + O2
mannose + H2O2
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93% activity compared with D-arabinitol
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?
D-mannitol + O2
mannose + H2O2
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mannitol oxidase plays an active role in the utilization of dietary mannitol
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?
D-mannitol + O2
mannose + H2O2
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because of high mannitol content of many plants, the herbivorous diet of terrestrial snails, and the association of mannitol oxidase with their digestive tract, the snail enzyme may represent a unique nutritional adaption of these and possibly other herbivorous molluscs
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?
galactitol + O2
D-galactose + H2O2
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16% activity compared with D-arabinitol
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?
additional information
?
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mannitol is a common and abundant carbohydrate component of plant food consumed by terrestrial gastropods, the presence and properties of mannitol oxidase imply an unusual route for mannitol metabolism via mannitol oxidase, hexokinase and phosphomannose isomerase
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?
additional information
?
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H2O2 generating at the surface of alimentary canal could have protective role against microorganisms
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?
additional information
?
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configuration around carbon-2 and carbon-4 is critical for binding and reactivity, reactivity requires trans-configuration of the oxygens at carbons 2 and 4
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?
additional information
?
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utilization of the sugar alcohols generally proceeds by an initial oxidation, producing a hexose
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?
additional information
?
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no or very poor activity with L-arabinitol, glycerol, ribitol, erythritol, inositol, aplha-glycerol-phosphate, xylitol, ascorbate, D-glucose and D-galactose
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?
additional information
?
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because of high mannitol content of many plants, the herbivorous diet of terrestrial snails, and the association of mannitol oxidase with their digestive tract, the snail enzyme may represent a unique nutritional adaption of these and possibly other herbivorous molluscs
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?
additional information
?
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naturally occuring polyols may be of nutritional value to herbivorous gastropod mollusc, mannitol oxidase plays a role in the metabolism of dietary sugar alcohols, gastropod molluscs derive nutritional benefit from ingestion of naturally orrurring polyols
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-mannitol + O2
mannose + H2O2
-
mannitol is a common and abundant carbohydrate component of plant food consumed by terrestrial gastropods, the presence and properties of mannitol oxidase imply an unusual route for mannitol metabolism via mannitol oxidase, hexokinase and phosphomannose isomerase
-
-
?
D-mannitol + O2
mannose + H2O2
-
mannitol oxidase plays an active role in the utilization of dietary mannitol
-
-
?
D-mannitol + O2
mannose + H2O2
-
because of high mannitol content of many plants, the herbivorous diet of terrestrial snails, and the association of mannitol oxidase with their digestive tract, the snail enzyme may represent a unique nutritional adaption of these and possibly other herbivorous molluscs
-
-
?
additional information
?
-
-
mannitol is a common and abundant carbohydrate component of plant food consumed by terrestrial gastropods, the presence and properties of mannitol oxidase imply an unusual route for mannitol metabolism via mannitol oxidase, hexokinase and phosphomannose isomerase
-
-
?
additional information
?
-
-
H2O2 generating at the surface of alimentary canal could have protective role against microorganisms
-
-
?
additional information
?
-
-
because of high mannitol content of many plants, the herbivorous diet of terrestrial snails, and the association of mannitol oxidase with their digestive tract, the snail enzyme may represent a unique nutritional adaption of these and possibly other herbivorous molluscs
-
-
?
additional information
?
-
-
naturally occuring polyols may be of nutritional value to herbivorous gastropod mollusc, mannitol oxidase plays a role in the metabolism of dietary sugar alcohols, gastropod molluscs derive nutritional benefit from ingestion of naturally orrurring polyols
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cd2+
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mannitol oxidase is inhibited by heavy metals more than other oxidases
deoxycholate
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1% w/v: 36% inhibition, deoxycholate, 1%, readily releases membrane-bound activity, but is slightly inhibitory
Pb2+
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mannitol oxidase is inhibited by heavy metals more than other oxidases
Zn2+
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mannitol oxidase is inhibited by heavy metals more than other oxidases
additional information
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no inhibition by cyanide and metal chelators such as EDTA
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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no requirement or activation by sulfhydryl reagents, such as DTT
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23
25
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
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enzyme concentrated within alimentary canal and digestive gland with highest specific activity in crop
brenda
additional information
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occurs in several tissues in terrestrial snails, concentrated within the alimentary tract and digestive glands with highest activity in the crop
brenda
additional information
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not in albumen gland, buccal mass, heart and hemolymph
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
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the enzyme from the snails Helix aspersa, Arion ater and Arion lucitanicus is found in a specialised tubular distinct organelle that has been termed the mannosome, they commonly have a hexagonal arrangement surrounded by smooth membrane and enclose a central tubule
brenda
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the enzyme from the snails Helix aspersa, Arion ater and Arion lucitanicus is found in a specialised tubular distinct organelle that has been termed the mannosome, they commonly have a hexagonal arrangement surrounded by smooth membrane and enclose a central tubule
brenda
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in alimentary system the enzyme is associated with its own subcellular membrane system of unique tubular morphology, most likely representing a structural modification of the endoplasmic reticulum, termed mannosomes
brenda
-
the enzyme from the snails Helix aspersa, Arion ater and Arion lucitanicus is found in a specialised tubular distinct organelle that has been termed the mannosome, they commonly have a hexagonal arrangement surrounded by smooth membrane and enclose a central tubule
brenda
additional information
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analytical subcellular fractionation experiments
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brenda
additional information
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analytical subcellular fractionation experiments
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brenda
additional information
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histochemical and biochemical localization
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brenda
additional information
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analytical subcellular fractionation experiments
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brenda
additional information
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analytical subcellular fractionation experiments
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brenda
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
mannitol oxidase activity elutes near the void volume of Sephacryl S300 columns which suggests a high molecular weight
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
additional information
oligomer
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two major peptides, one, possibly a doublet, of 68000 Da and the other of higher mass. Two faint, faster moving peptides located between 45000 and 68000 Da, SDS-PAGE
oligomer
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presence of a predominant peptide at 68000-70000 Da, faster migrating fainter bands at 58000-60000 Da, SDS-PAGE
oligomer
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two major peptides, one, possibly a doublet, of 68000 Da and the other of higher mass. Two faint, faster moving peptides located between 45000 and 68000 Da, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no modification
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not a glycoprotein, the presence of amino sugar residues cannot be ruled out
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11
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enzyme relatively stable at alkaline pH, pH 11: 30% of maximum activity remains
287629
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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REF.
AUTHORS