1.1.9.1: alcohol dehydrogenase (azurin)

This is an abbreviated version, for detailed information about alcohol dehydrogenase (azurin), go to the full flat file.

Reaction

a primary alcohol
+
azurin
=
an aldehyde
+
reduced azurin

Synonyms

ADH IIB, ADH IIG, QH-ADH, quinohaemoprotein alcohol dehydrogenase, quinohemoprotein alcohol dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.9 With a copper protein as acceptor
                1.1.9.1 alcohol dehydrogenase (azurin)

Reference

Reference on EC 1.1.9.1 - alcohol dehydrogenase (azurin)

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Groen, B.W.; van Kleef, M.A.G.; Duine, J.A.
Quinohaemoprotein alcohol dehydrogenase apoenzyme from Pseudomonas testosteroni
Biochem. J.
234
611-615
1986
Comamonas testosteroni
Manually annotated by BRENDA team
De Jong, G.A.H.; Caldeira, J.; Sun, J.; Jongejan, J.A.; de Vries, S.; Loehr, T.M.; Moura, I.; Moura, J.J.G.; Duine, J.A.
Characterization of the interaction between PQQ and heme c in the quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni
Biochemistry
34
9451-9458
1995
Comamonas testosteroni
Manually annotated by BRENDA team
De Jong, G.A.H.; Geerlof, A.; Stoorvogel, J.; Jongejan, J.A.; de Vries, S.; Duine, J.a.
Quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni. Purification, characterization, and reconstitution of the apoenzyme with pyrolloquinoline quinone analogues
Eur. J. Biochem.
230
899-905
1995
Comamonas testosteroni
Manually annotated by BRENDA team
Jongejan, A.; Jongejan, J.A.; Hagen, W.R.
Deuterium isotope effect on enantioselectivity in the Comamonas testosteroni quinohemoprotein alcohol dehydrogenase-catalyzed kinetic resolution of rac-2,2-dimethyl-4-hydroxymethyl-1,3-dioxolane, solketal
Biochim. Biophys. Acta
1647
297-302
2003
Comamonas testosteroni
Manually annotated by BRENDA team
Oubrie, A.; Rozeboom, H.J.; Kalk, K.H.; Huizinga, E.G.; Dijkstra, B.W.
Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: structural basis for substrate oxidation and electron transfer
J. Biol. Chem.
277
3727-3732
2002
Comamonas testosteroni (Q46444)
Manually annotated by BRENDA team
Toyama, H.; Aoki, N.; Matsushita, K.; Adachi, O.
Azurin involved in alcohol oxidation system in Pseudomonas putida HK5: expression analysis and gene cloning.
Biosci. Biotechnol. Biochem.
65
1617-1626
2001
Pseudomonas putida (Q8GR64)
Manually annotated by BRENDA team
Toyama, H.; Fujii, A.; Matsushita, K.; Shinagawa, E.; Ameyama, M.; Adachi, O.
Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols
J. Bacteriol.
177
2442-2450
1995
Pseudomonas putida
Manually annotated by BRENDA team
Oubrie, A.; Huizinga, E.G.; Rozeboom, H.e.J.; Kalk, K.H.; de Jong, G.A.H.; Duine, J.A.; Dijkstra, B.W.
Crystallization of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: crystals with unique optical properties
Acta Crystallogr. Sect. D
D57
1732-1734
2001
Comamonas testosteroni
Manually annotated by BRENDA team
Somers, W.A.C.; Stigter, E.C.A.; Van Hartingsveldt, W.; Van Der Lugt, J.P.
Enantioselective oxidation of secondary alcohols at a quinohemoprotein alcohol dehydrogenase electrode
Appl. Biochem. Biotechnol.
75
151-161
1999
Comamonas testosteroni
-
Manually annotated by BRENDA team
Geerlof, A.; Rakels, J.J.L.; Straathof, A.J.J.; Heijnen, J.J.; Jongejan, J.A.; Duine, J.A.
Description of the kinetic mechanism and the enantioselectivity of quinohaemoprotein ethanol dehydrogenase from Comamonas testosteroni in the oxidation of alcohols and aldehydes
Eur. J. Biochem.
226
537-546
1994
Comamonas testosteroni
Manually annotated by BRENDA team
Stigter, E.C.A.; van der Lugt, J.P.; Somers, W.A.C.
Enantioselective oxidation of secondary alcohols by quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni
J. Mol. Catal. B
2
291-297
1997
Comamonas testosteroni
-
Manually annotated by BRENDA team