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Literature summary for 1.1.5.5 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

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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

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

Organism

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

Specific Activity [micromol/min/mg]

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

Subunits

Subunits Comment Organism
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

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

Cofactor

Cofactor Comment Organism Structure
pyrroloquinoline quinone
-
Gluconobacter sp.