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Literature summary extracted from

  • Laurinavicius, V.; Razumiene, J.; Ramanavicius, A.; Ryabov, A.D.
    Wiring of PQQ-dehydrogenases (2004), Biosens. Bioelectron., 20, 1217-1222.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.1.5.5 analysis the enzyme can be used in biosensors, method development, overview Gluconobacter sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.5.5 additional information
-
 additional information kinetic parameters of the enzymatic behavior in solution (photometric data) and electrochemical characteristics of the immobilized enzymes on different electro-active surfaces are compared Gluconobacter sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.5.5 Ca2+
-
 Gluconobacter sp.

Organism

EC Number Organism UniProt Comment Textmining
1.1.5.5 Gluconobacter sp.
-
-
-
1.1.5.5 Gluconobacter sp. DSM 3504 / ATCC 15163
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.5.5 additional information
-
 171 U/ml Gluconobacter sp.

Subunits

EC Number Subunits Comment Organism
1.1.5.5 trimer subunit I contains one PQQ and one heme moiety, subunit II contains three heme moieties, and subunit III is a small protein subunit essential for the enzymatic activity providing electron exchange between PQQ and hemes, overview Gluconobacter sp.

Synonyms

EC Number Synonyms Comment Organism
1.1.5.5 membrane-bound alcohol dehydrogenase
-
-
1.1.5.5 PQQ ADH
-
-
1.1.5.5 PQQ dependent alcohol dehydrogenase
-
 Gluconobacter sp.
1.1.5.5 PQQ-alcohol dehydrogenase
-
-
1.1.5.5 pyrroloquinoline quinone dependent ADH
-
 Gluconobacter sp.
1.1.5.5 pyrroloquinoline quinone dependent alcohol dehydrogenase
-
 Gluconobacter sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.5.5 pyrroloquinoline quinone
-
 Gluconobacter sp.