BRENDA - Enzyme Database
show all sequences of 1.1.3.40

Mannitol oxidase: partial purification and characterization of the membrane-bound enzyme from the snail Helix aspersa

Vorhaben, J.E.; Smith, D.D., Jr.; Campbell, J.W.; Int. J. Biochem. 18, 337-344 (1986)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
no requirement or activation by sulfhydryl reagents, such as DTT
Helix aspersa
General Stability
General Stability
Organism
addition of EDTA and/or DTT does not appreciably improve stability
Helix aspersa
glycerol stabilizes
Helix aspersa
Inhibitors
Inhibitors
Commentary
Organism
Structure
deoxycholate
1% w/v: 36% inhibition, deoxycholate, 1%, readily releases membrane-bound activity, but is slightly inhibitory
Helix aspersa
additional information
no inhibition by cyanide and metal chelators such as EDTA
Helix aspersa
n-butanol
n-butyl alcohol
Helix aspersa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.04
-
O2
oxygen, substrate: D-mannitol
Helix aspersa
5.9
-
D-mannitol
-
Helix aspersa
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
Golgi membrane
membrane-bound
Helix aspersa
139
-
mitochondrion
-
Helix aspersa
5739
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
additional information
-
mannitol oxidase activity elutes near the void volume of Sephacryl S300 columns which suggests a high molecular weight
Helix aspersa
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
D-mannitol + O2
Helix aspersa
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
mannose + H2O2
-
-
?
additional information
Helix aspersa
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
?
-
-
-
Organism
Organism
UniProt
Commentary
Textmining
Helix aspersa
-
common garden snail; terrestrial snail
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
no modification
not a glycoprotein, the presence of amino sugar residues cannot be ruled out
Helix aspersa
Purification (Commentary)
Purification (Commentary)
Organism
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
Helix aspersa
Reaction
Reaction
Commentary
Organism
Reaction ID
D-mannitol + O2 = D-mannose + H2O2
stoichiometry, mannose/H2O2 = 0.86; utilization of the sugar alcohols generally proceeds by an initial oxidation, producing a hexose
Helix aspersa
Source Tissue
Source Tissue
Commentary
Organism
Textmining
alimentary canal
-
Helix aspersa
-
crop
highest activity
Helix aspersa
-
digestive gland
hepatopancreas
Helix aspersa
-
gut
inner lining of lumen of the gut
Helix aspersa
-
additional information
occurs in several tissues in terrestrial snails, concentrated within the alimentary tract and digestive glands with highest activity in the crop
Helix aspersa
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.984
-
-
Helix aspersa
Storage Stability
Storage Stability
Organism
-20°C, 20% glycerol, one week, remains active
Helix aspersa
5°C, Tris buffer, 10% glycerol, 4 days, 35% activity retained
Helix aspersa
5°C, Tris buffer, 20% glycerol, 4 days, 69% activity retained
Helix aspersa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
D,L-threitol + O2
7% activity compared with D-arabinitol
287629
Helix aspersa
? + H2O2
-
-
-
?
D-arabinitol + O2
best substrate
287629
Helix aspersa
arabinose + H2O2
-
-
-
?
D-glucitol + O2
sorbitol
287629
Helix aspersa
D-glucose + H2O2
-
-
-
?
D-glucitol + O2
20% activity compared with D-arabinitol
287629
Helix aspersa
D-glucose + H2O2
-
-
-
?
D-glycero-D-galactoheptitol + O2
9% activity compared with D-arabinitol
287629
Helix aspersa
? + H2O2
-
-
-
?
D-glycero-D-galactoheptitol + O2
perseitol
287629
Helix aspersa
? + H2O2
-
-
-
?
D-mannitol + O2
93% activity compared with D-arabinitol
287629
Helix aspersa
mannose + H2O2
-
-
-
?
D-mannitol + O2
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
287629
Helix aspersa
mannose + H2O2
-
-
-
?
galactitol + O2
16% activity compared with D-arabinitol
287629
Helix aspersa
D-galactose + H2O2
-
-
-
?
galactitol + O2
dulcitol
287629
Helix aspersa
D-galactose + H2O2
-
-
-
?
additional information
substrate specificity
287629
Helix aspersa
?
-
-
-
-
additional information
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
287629
Helix aspersa
?
-
-
-
-
additional information
utilization of the sugar alcohols generally proceeds by an initial oxidation, producing a hexose
287629
Helix aspersa
?
-
-
-
-
additional information
activity only with acyclic polyols
287629
Helix aspersa
?
-
-
-
-
additional information
no or very poor activity with L-arabinitol, glycerol, ribitol, erythritol, inositol, aplha-glycerol-phosphate, xylitol, ascorbate, D-glucose and D-galactose
287629
Helix aspersa
?
-
-
-
-
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
287629
Helix aspersa
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
More
-
Helix aspersa
oligomer
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
Helix aspersa
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Helix aspersa
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
alkaline pH-optimum; pI: 5.4-5.6
Helix aspersa
8
8.5
alkaline pH-optimum
Helix aspersa
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6.5
10
at pH 6.5 and pH 10.0: about 50% of maximum activity
Helix aspersa
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
additional information
-
enzyme relatively stable at alkaline pH
Helix aspersa
11
-
enzyme relatively stable at alkaline pH, pH 11: 30% of maximum activity remains
Helix aspersa
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
no evidence for a flavin or heme cofactor; pyridine nucleotide or cytochrome c not required
Helix aspersa
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
no requirement or activation by sulfhydryl reagents, such as DTT
Helix aspersa
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
no evidence for a flavin or heme cofactor; pyridine nucleotide or cytochrome c not required
Helix aspersa
General Stability (protein specific)
General Stability
Organism
addition of EDTA and/or DTT does not appreciably improve stability
Helix aspersa
glycerol stabilizes
Helix aspersa
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
deoxycholate
1% w/v: 36% inhibition, deoxycholate, 1%, readily releases membrane-bound activity, but is slightly inhibitory
Helix aspersa
additional information
no inhibition by cyanide and metal chelators such as EDTA
Helix aspersa
n-butanol
n-butyl alcohol
Helix aspersa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.04
-
O2
oxygen, substrate: D-mannitol
Helix aspersa
5.9
-
D-mannitol
-
Helix aspersa
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
Golgi membrane
membrane-bound
Helix aspersa
139
-
mitochondrion
-
Helix aspersa
5739
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
additional information
-
mannitol oxidase activity elutes near the void volume of Sephacryl S300 columns which suggests a high molecular weight
Helix aspersa
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
D-mannitol + O2
Helix aspersa
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
mannose + H2O2
-
-
?
additional information
Helix aspersa
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
?
-
-
-
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
no modification
not a glycoprotein, the presence of amino sugar residues cannot be ruled out
Helix aspersa
Purification (Commentary) (protein specific)
Commentary
Organism
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
Helix aspersa
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
alimentary canal
-
Helix aspersa
-
crop
highest activity
Helix aspersa
-
digestive gland
hepatopancreas
Helix aspersa
-
gut
inner lining of lumen of the gut
Helix aspersa
-
additional information
occurs in several tissues in terrestrial snails, concentrated within the alimentary tract and digestive glands with highest activity in the crop
Helix aspersa
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.984
-
-
Helix aspersa
Storage Stability (protein specific)
Storage Stability
Organism
-20°C, 20% glycerol, one week, remains active
Helix aspersa
5°C, Tris buffer, 10% glycerol, 4 days, 35% activity retained
Helix aspersa
5°C, Tris buffer, 20% glycerol, 4 days, 69% activity retained
Helix aspersa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
D,L-threitol + O2
7% activity compared with D-arabinitol
287629
Helix aspersa
? + H2O2
-
-
-
?
D-arabinitol + O2
best substrate
287629
Helix aspersa
arabinose + H2O2
-
-
-
?
D-glucitol + O2
sorbitol
287629
Helix aspersa
D-glucose + H2O2
-
-
-
?
D-glucitol + O2
20% activity compared with D-arabinitol
287629
Helix aspersa
D-glucose + H2O2
-
-
-
?
D-glycero-D-galactoheptitol + O2
9% activity compared with D-arabinitol
287629
Helix aspersa
? + H2O2
-
-
-
?
D-glycero-D-galactoheptitol + O2
perseitol
287629
Helix aspersa
? + H2O2
-
-
-
?
D-mannitol + O2
93% activity compared with D-arabinitol
287629
Helix aspersa
mannose + H2O2
-
-
-
?
D-mannitol + O2
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
287629
Helix aspersa
mannose + H2O2
-
-
-
?
galactitol + O2
16% activity compared with D-arabinitol
287629
Helix aspersa
D-galactose + H2O2
-
-
-
?
galactitol + O2
dulcitol
287629
Helix aspersa
D-galactose + H2O2
-
-
-
?
additional information
substrate specificity
287629
Helix aspersa
?
-
-
-
-
additional information
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
287629
Helix aspersa
?
-
-
-
-
additional information
utilization of the sugar alcohols generally proceeds by an initial oxidation, producing a hexose
287629
Helix aspersa
?
-
-
-
-
additional information
activity only with acyclic polyols
287629
Helix aspersa
?
-
-
-
-
additional information
no or very poor activity with L-arabinitol, glycerol, ribitol, erythritol, inositol, aplha-glycerol-phosphate, xylitol, ascorbate, D-glucose and D-galactose
287629
Helix aspersa
?
-
-
-
-
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
287629
Helix aspersa
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
More
-
Helix aspersa
oligomer
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
Helix aspersa
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Helix aspersa
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
alkaline pH-optimum; pI: 5.4-5.6
Helix aspersa
8
8.5
alkaline pH-optimum
Helix aspersa
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6.5
10
at pH 6.5 and pH 10.0: about 50% of maximum activity
Helix aspersa
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
additional information
-
enzyme relatively stable at alkaline pH
Helix aspersa
11
-
enzyme relatively stable at alkaline pH, pH 11: 30% of maximum activity remains
Helix aspersa
Other publictions for EC 1.1.3.40
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
655277
Knigge
Mannosomes: a molluscan intrac ...
Arion lusitanicus
Comp. Biochem. Physiol. C
131
259-269
2002
-
-
-
-
-
-
3
-
1
-
-
-
-
4
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
287633
Large
-
Centrifugal evidence for assoc ...
Arion ater, Arion lusitanicus, Helix aspersa, Limax flavus
Comp. Biochem. Physiol. A
107
621-629
1994
-
-
-
-
-
-
-
10
7
-
-
4
-
4
-
-
-
-
-
7
-
-
25
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
10
7
-
-
4
-
-
-
-
-
7
-
-
25
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
287630
Large
-
The association of mannitol ox ...
Arion ater
Protoplasma
175
93-101
1993
-
-
-
-
-
-
-
-
2
-
-
2
-
1
-
-
-
-
-
1
-
-
3
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
2
-
-
-
-
-
1
-
-
3
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
287632
Malik
-
Assay and subcellular localiza ...
Arion ater
J. Exp. Zool.
242
9-15
1987
-
-
-
-
-
-
-
1
4
-
-
2
-
1
-
-
-
-
-
4
1
-
3
-
-
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
4
-
-
2
-
-
-
-
-
4
1
-
3
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
287629
Vorhaben
Mannitol oxidase: partial puri ...
Helix aspersa
Int. J. Biochem.
18
337-344
1986
1
-
-
-
-
2
3
2
2
-
1
2
-
2
-
1
1
1
-
5
1
3
16
2
-
1
-
-
-
2
1
2
1
-
-
-
1
-
-
1
-
-
2
-
3
-
2
2
-
1
2
-
-
1
1
-
5
1
3
16
2
1
-
-
-
2
1
2
-
-
-
-
-
-
-
287631
Vorhaben
-
Histochemical and biochemical ...
Biomphalaria glabrata, Helix aspersa
J. Exp. Zool.
231
157-160
1984
-
-
-
-
-
-
-
-
4
-
-
3
-
2
-
-
1
-
-
15
1
-
8
-
-
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
4
-
-
3
-
-
-
1
-
15
1
-
8
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-