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]

Crystallization

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Crystallization 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 Crystallization (commentary) Search

to 1.44 A resolution. The N-terminal domain has a beta-propeller fold and binds one pyrroloquinoline quinone cofactor and one calcium ion in the active site. A tetrahydrofuran-2-carboxylic acid molecule is present in the substrate-binding cleft. The C-terminal domain is an -helical type I cytochrome c with His608 and Met647 as heme-iron ligands. An unusual disulfide bond between two adjacent cysteines bridges the redox centers. It appears essential for electron transfer. A water channel delineates a possible pathway for proton transfer from the active site to the solvent

Comamonas testosteroni

Q46444

656080

to 2.4 A resolution, space group C2

Comamonas testosteroni

701480