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Literature summary for 1.1.3.40 extracted from

  • Vorhaben, J.E.; Smith, D.D., Jr.; Campbell, J.W.
    Mannitol oxidase: partial purification and characterization of the membrane-bound enzyme from the snail Helix aspersa (1986), Int. J. Biochem., 18, 337-344.
    View publication on PubMed

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 [┬Ámol/min/mg] Specific Activity Maximum [┬Ámol/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