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Literature summary extracted from

  • Kato, K.; Walde, P.; Mitsui, H.; Higashi, N.
    Enzymatic activity and stability of D-fructose dehydrogenase and sarcosine dehydrogenase immobilized onto giant vesicles (2003), Biotechnol. Bioeng., 84, 415-423.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.5.8.3 additional information immobilization of the enzyme on sorbitan esters Span 80 and Tween 80 containing phospholipid lecithin-bilayer membrane vesicles increases the enzyme activity and stability Pseudomonas putida

Protein Variants

EC Number Protein Variants Comment Organism
1.5.8.3 additional information immobilization of the enzyme on sorbitan esters Span 80 and Tween 80 containing phospholipid lecithin-bilayer membrane vesicles, vesicle preparation overview Pseudomonas putida

General Stability

EC Number General Stability Organism
1.1.5.14 the enzyme immobilized onto giant vesicles is stable for at least 20 days at 25°C, while the activity of the free enzyme dropps to about 20% of its initial activity during the same period of time Gluconobacter sp.
1.5.8.3 immobilization of the enzyme on sorbitan esters Span 80 and Tween 80 containing phospholipid lecithin-bilayer membrane vesicles increases the enzyme activity and stability Pseudomonas putida

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.5.8.3 1.3
-
 sarcosine pH 7.5, 37°C, immobilized enzyme Pseudomonas putida
1.5.8.3 1.9
-
 sarcosine pH 7.5, 37°C, non-immobilized enzyme Pseudomonas putida

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.5.14 membrane
-
 Gluconobacter sp. 16020
-
1.5.8.3 membrane
-
 Pseudomonas putida 16020
-

Organism

EC Number Organism UniProt Comment Textmining
1.1.5.14 Gluconobacter sp.
-
-
-
1.5.8.3 Pseudomonas putida
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.5.8.3 commercial preparation diagnostic reagent grade Pseudomonas putida
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.5.8.3 additional information
-
-
 Pseudomonas putida

Storage Stability

EC Number Storage Stability Organism
1.5.8.3 storage stability at room temperature is increased for vesicle-immobilized enzyme Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.14 D-fructose + [Fe(CN)6]3-
-
 Gluconobacter sp. 5-dehydro-D-fructose + [Fe(CN)6]4-
-
 ?
1.5.8.3 sarcosine + oxidized 1-methoxy-5-methylphenazinium methylsulfate quantification with nitroblue tetrazolium chloride, i.e. NBT or 2,2'-bis(4-nitrophenyl)-5,5'-diphenyl-3,3'-(3,3'-dimethoxy-4,4'-diphenylene)ditetrazolium chloride, giving NBT-formazan in reaction with reduced 1-methoxy-5-methylphenazinium methylsulfate, overview Pseudomonas putida glycine + formaldehyde + reduced 1-methoxy-5-methylphenazinium methylsulfate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.5.14 FDH
-
 Gluconobacter sp.
1.5.8.3 SDH
-
 Pseudomonas putida

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.8.3 37
-
 assay at Pseudomonas putida

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.5.14 25
-
 the enzyme immobilized onto giant vesicles is stable for at least 20 days at 25°C, while the activity of the free enzyme dropps to about 20% of its initial activity during the same period of time Gluconobacter sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.8.3 7.5
-
 assay at Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.8.3 additional information 1-methoxy-5-methylphenazinium methylsulfate acts as electron acceptor Pseudomonas putida