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Literature summary for 1.1.5.9 extracted from

  • Sygmund, C.; Klausberger, M.; Felice, A.K.; Ludwig, R.
    Reduction of quinones and phenoxy radicals by extracellular glucose dehydrogenase from Glomerella cingulata suggests a role in plant pathogenicity (2011), Microbiology, 157, 3203-3212.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, phylogenetic analysis Colletotrichum gloeosporioides

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Colletotrichum gloeosporioides
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
68000
-
1 * 68000, deglycosylated enzyme, SDS-PAGE Colletotrichum gloeosporioides
95000 135000 glycoprotein, native PAGE Colletotrichum gloeosporioides

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glucose + a quinone Colletotrichum gloeosporioides
-
D-glucono-1,5-lactone + a quinol
-
?
D-glucose + a quinone Colletotrichum gloeosporioides DSM 62728
-
D-glucono-1,5-lactone + a quinol
-
?

Organism

Organism UniProt Comment Textmining
Colletotrichum gloeosporioides
-
anamorph Colletotrichum gloeosporoides
-
Colletotrichum gloeosporioides DSM 62728
-
anamorph Colletotrichum gloeosporoides
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein four potential N-glycosylation sites at N55, N233, N255 and N339 Colletotrichum gloeosporioides

Purification (Commentary)

Purification (Comment) Organism
native extracellular enzyme 23.7fold from culture supernatant by anion exchange and hydrophobic interaction chromatography, ammonium sulfate fractionation, and ultrafiltration Colletotrichum gloeosporioides

Specific Activity [micromol/min/mg]

Specific Activity Minimum [┬Ámol/min/mg] Specific Activity Maximum [┬Ámol/min/mg] Comment Organism
565
-
purified enzyme with ferrocenium hexafluorophosphate, pH 5.5, 30┬░C Colletotrichum gloeosporioides
840
-
purified enzyme with 2,6-dichlorophenol indophenol , pH 5.5, 30┬░C Colletotrichum gloeosporioides

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + 1,4-benzoquinone
-
Colletotrichum gloeosporioides D-glucono-1,5-lactone + 1,4-benzoquinol
-
?
D-glucose + 1,4-benzoquinone
-
Colletotrichum gloeosporioides DSM 62728 D-glucono-1,5-lactone + 1,4-benzoquinol
-
?
D-glucose + a quinone
-
Colletotrichum gloeosporioides D-glucono-1,5-lactone + a quinol
-
?
D-glucose + a quinone
-
Colletotrichum gloeosporioides DSM 62728 D-glucono-1,5-lactone + a quinol
-
?
D-glucose + ferricenium hexafluorophosphate
-
Colletotrichum gloeosporioides D-glucono-1,5-lactone + ferrocenium hexafluorophosphate
-
?
D-glucose + ferricenium hexafluorophosphate
-
Colletotrichum gloeosporioides DSM 62728 D-glucono-1,5-lactone + ferrocenium hexafluorophosphate
-
?
D-glucose + ferricyanide
-
Colletotrichum gloeosporioides D-glucono-1,5-lactone + ferrocyanide
-
?
D-glucose + ferricyanide
-
Colletotrichum gloeosporioides DSM 62728 D-glucono-1,5-lactone + ferrocyanide
-
?
D-glucose + oxidized 2,6-dichlorophenol indophenol
-
Colletotrichum gloeosporioides D-glucono-1,5-lactone + reduced 2,6-dichlorophenol indophenol
-
?
additional information suitable electron acceptors are quinones, phenoxy radicals, 2,6-dichloroindophenol, ferricyanide and ferrocenium hexafluorophosphate. Reduction of quinones and phenoxy radicals by extracellular enzyme, overview Colletotrichum gloeosporioides ?
-
?
additional information suitable electron acceptors are quinones, phenoxy radicals, 2,6-dichloroindophenol, ferricyanide and ferrocenium hexafluorophosphate. Reduction of quinones and phenoxy radicals by extracellular enzyme, overview Colletotrichum gloeosporioides DSM 62728 ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 68000, deglycosylated enzyme, SDS-PAGE Colletotrichum gloeosporioides

Synonyms

Synonyms Comment Organism
FAD-dependent glucose dehydrogenase
-
Colletotrichum gloeosporioides

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
30
-
assay at Colletotrichum gloeosporioides

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
assay at with 2,6-dichlorophenol indophenol or ferrocenium hexafluorophosphate Colletotrichum gloeosporioides
7.5
-
assay at with 1,4-benzoquinone Colletotrichum gloeosporioides

Cofactor

Cofactor Comment Organism Structure
FAD dependent on, non-covalently bound Colletotrichum gloeosporioides

pI Value

Organism Comment pI Value Maximum pI Value
Colletotrichum gloeosporioides isoelectric focusing
-
5.6

General Information

General Information Comment Organism
evolution the enzyme belongs to the to the GMC family of oxidoreductases, phylogenetic analysis Colletotrichum gloeosporioides
physiological function the enzyme from Glomerella cingulata might play a role in plant pathogenicity. The quinone and phenoxy radical reducing enzyme light act to neutralize the action of plant laccase, phenoloxidase or peroxidase activities, which are increased in infected plants to evade fungal attack Colletotrichum gloeosporioides