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

Synonyms

ADH IIB, ADH IIG, EC 1.1.98.1, 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)

Advanced search results

Do not include text mining results

Include

results (more...)

Include

results (more...)

Results	in table
282	AA Sequence
1	Application
1	Cloned(Commentary)
10	Cofactor
2	Crystallization (Commentary)
2	General Information
6	kcat/KM [mM/s]
106	KM Value [mM]
2	Metals/Ions
8	Molecular Weight [Da]
11	Organism
1	pH Optimum
1	Purification (Commentary)
1	Reaction
11	Reference
2	Specific Activity [micromol/min/mg]
2	Storage Stability
109	Substrates and Products (Substrate)
5	Subunits
9	Synonyms
1	Systematic Name
8	Turnover Number [1/s]

Application

print visible entries

print all entries

Application on EC 1.1.9.1 - alcohol dehydrogenase (azurin)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide

Go to Application Search

biotechnology

Comamonas testosteroni

co-immobilization of enzyme with redox polymer poly(vinylpyridine) complex functionalized with osmium bis(bipyridine) chloride on an electrode. The enzyme electrode readily oxidizes primary alcohols and secondary alcohols with maximum current densities varying between 0.43 and 0.98 A per m2 depending on the substrate and the operation temperature. The enzyme electrode is enantioselective in the oxidation of secondary alcohols. A strong preference is observed for the (S)-2-alcohols, the enantioselectivity increases with increasing chain length. The enantiomeric ratio E increases from 13 for (R,S)-2-butanol to approximately 80 for (R,S)-2-heptanol and (R,S)-2-octanol

701774