Any feedback?
Literature summary for 1.1.3.40 extracted from
- Mannitol oxidase: partial purification and characterization of the membrane-bound enzyme from the snail Helix aspersa (1986), Int. J. Biochem., 18, 337-344.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | no requirement or activation by sulfhydryl reagents, such as DTT | Cornu aspersum |
General Stability
| General Stability | Organism |
|---|---|
| addition of EDTA and/or DTT does not appreciably improve stability | Cornu aspersum |
| glycerol stabilizes | Cornu aspersum |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| deoxycholate | 1% w/v: 36% inhibition, deoxycholate, 1%, readily releases membrane-bound activity, but is slightly inhibitory | Cornu aspersum |  |
| additional information | no inhibition by cyanide and metal chelators such as EDTA | Cornu aspersum | |
| n-butanol | n-butyl alcohol | Cornu aspersum | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.04 | - |
O2 | oxygen, substrate: D-mannitol | Cornu aspersum | |
| 5.9 | - |
D-mannitol | - |
Cornu aspersum | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| Golgi membrane | membrane-bound | Cornu aspersum | 139 | - |
| mitochondrion | - |
Cornu aspersum | 5739 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| additional information | - |
mannitol oxidase activity elutes near the void volume of Sephacryl S300 columns which suggests a high molecular weight | Cornu aspersum |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-mannitol + O2 | Cornu aspersum | 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 | Cornu aspersum | 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 | Comment | Textmining |
|---|---|---|---|
| Cornu aspersum | - |
common garden snail | - |
| Cornu aspersum | - |
terrestrial snail | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| no modification | not a glycoprotein, the presence of amino sugar residues cannot be ruled out | Cornu aspersum |
Purification (Commentary)
| Purification (Comment) | 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 | Cornu aspersum |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| D-mannitol + O2 = D-mannose + H2O2 | utilization of the sugar alcohols generally proceeds by an initial oxidation, producing a hexose | Cornu aspersum | |
| D-mannitol + O2 = D-mannose + H2O2 | stoichiometry, mannose/H2O2 = 0.86 | Cornu aspersum |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| alimentary canal | - |
Cornu aspersum | - |
| crop | highest activity | Cornu aspersum | - |
| digestive gland | hepatopancreas | Cornu aspersum | - |
| gut | inner lining of lumen of the gut | Cornu aspersum | - |
| additional information | occurs in several tissues in terrestrial snails, concentrated within the alimentary tract and digestive glands with highest activity in the crop | Cornu aspersum | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.984 | - |
- |
Cornu aspersum |
Storage Stability
| Storage Stability | Organism |
|---|---|
| -20°C, 20% glycerol, one week, remains active | Cornu aspersum |
| 5°C, Tris buffer, 10% glycerol, 4 days, 35% activity retained | Cornu aspersum |
| 5°C, Tris buffer, 20% glycerol, 4 days, 69% activity retained | Cornu aspersum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D,L-threitol + O2 | 7% activity compared with D-arabinitol | Cornu aspersum | ? + H2O2 | - |
? | |
| D-arabinitol + O2 | best substrate | Cornu aspersum | arabinose + H2O2 | - |
? | |
| D-glucitol + O2 | sorbitol | Cornu aspersum | D-glucose + H2O2 | - |
? | |
| D-glucitol + O2 | 20% activity compared with D-arabinitol | Cornu aspersum | D-glucose + H2O2 | - |
? | |
| D-glycero-D-galactoheptitol + O2 | 9% activity compared with D-arabinitol | Cornu aspersum | ? + H2O2 | - |
? | |
| D-glycero-D-galactoheptitol + O2 | perseitol | Cornu aspersum | ? + H2O2 | - |
? | |
| D-mannitol + O2 | 93% activity compared with D-arabinitol | Cornu aspersum | 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 | Cornu aspersum | mannose + H2O2 | - |
? | |
| galactitol + O2 | 16% activity compared with D-arabinitol | Cornu aspersum | D-galactose + H2O2 | - |
? | |
| galactitol + O2 | dulcitol | Cornu aspersum | D-galactose + H2O2 | - |
? | |
| additional information | substrate specificity | Cornu aspersum | ? | - |
? | |
| 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 | Cornu aspersum | ? | - |
? | |
| additional information | utilization of the sugar alcohols generally proceeds by an initial oxidation, producing a hexose | Cornu aspersum | ? | - |
? | |
| additional information | activity only with acyclic polyols | Cornu aspersum | ? | - |
? | |
| additional information | no or very poor activity with L-arabinitol, glycerol, ribitol, erythritol, inositol, aplha-glycerol-phosphate, xylitol, ascorbate, D-glucose and D-galactose | Cornu aspersum | ? | - |
? | |
| 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 | Cornu aspersum | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | - |
Cornu aspersum |
| 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 | Cornu aspersum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Cornu aspersum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
alkaline pH-optimum | Cornu aspersum |
| additional information | - |
pI: 5.4-5.6 | Cornu aspersum |
| 8 | 8.5 | alkaline pH-optimum | Cornu aspersum |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 10 | at pH 6.5 and pH 10.0: about 50% of maximum activity | Cornu aspersum |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
enzyme relatively stable at alkaline pH | Cornu aspersum |
| 11 | - |
enzyme relatively stable at alkaline pH, pH 11: 30% of maximum activity remains | Cornu aspersum |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| additional information | no evidence for a flavin or heme cofactor | Cornu aspersum | |
| additional information | pyridine nucleotide or cytochrome c not required | Cornu aspersum |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
