Application | Comment | Organism |
---|---|---|
biofuel production | alcohol dehydrogenase from cyanobacterium Synechocystis sp. PCC 6803 is a key enzyme for biofuel production. It is a necessary enzyme in the synthesis of ethanol and butanol with critical importance in the production of biofuels. Alcohol dehydrogenase from cyanobacterium Synechocystis sp. PCC 6803 has higher efficiency for the production of alcohols such as 1-butanol and isobutanol | Synechocystis sp. PCC 6803 |
Cloned (Comment) | Organism |
---|---|
gene slr1192, sequence comparisons and phylogenetic analysis and tree | Synechocystis sp. PCC 6803 |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | the enzyme contains two Zn2+ ions, one structural and one catalytic. The catalytic Zn2+ is found inside of a cleft between the domains and placed at the bottom of the hydrophobic coenzyme and substrate-binding pocket, coordinated by four residues including Cys39, His61, Cys148, and Glu62 | Synechocystis sp. PCC 6803 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
cinnamaldehyde + NADH + H+ | Synechocystis sp. PCC 6803 | - |
cinnamyl alcohol + NAD+ | - |
r | |
cinnamaldehyde + NADH + H+ | Synechocystis sp. PCC 6803 Kazusa | - |
cinnamyl alcohol + NAD+ | - |
r | |
ethanol + NAD+ | Synechocystis sp. PCC 6803 | - |
acetaldehyde + NADH + H+ | - |
r | |
ethanol + NAD+ | Synechocystis sp. PCC 6803 Kazusa | - |
acetaldehyde + NADH + H+ | - |
r | |
phenylethanol + NAD+ | Synechocystis sp. PCC 6803 | - |
phenylacetaldehyde + NADH + H+ | - |
r | |
phenylethanol + NAD+ | Synechocystis sp. PCC 6803 Kazusa | - |
phenylacetaldehyde + NADH + H+ | - |
r | |
sinapaldehyde + NADH | Synechocystis sp. PCC 6803 | preferred substrates | sinapyl alcohol + NAD+ | - |
r | |
sinapaldehyde + NADH + H+ | Synechocystis sp. PCC 6803 | preferred substrates | sinalcohol + NAD+ | - |
r | |
sinapaldehyde + NADH + H+ | Synechocystis sp. PCC 6803 Kazusa | preferred substrates | sinalcohol + NAD+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Synechocystis sp. PCC 6803 | P74721 | - |
- |
Synechocystis sp. PCC 6803 Kazusa | P74721 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
cinnamaldehyde + NADH + H+ | - |
Synechocystis sp. PCC 6803 | cinnamyl alcohol + NAD+ | - |
r | |
cinnamaldehyde + NADH + H+ | - |
Synechocystis sp. PCC 6803 Kazusa | cinnamyl alcohol + NAD+ | - |
r | |
ethanol + NAD+ | - |
Synechocystis sp. PCC 6803 | acetaldehyde + NADH + H+ | - |
r | |
ethanol + NAD+ | - |
Synechocystis sp. PCC 6803 Kazusa | acetaldehyde + NADH + H+ | - |
r | |
additional information | alcohol dehydrogenase catalyzes a reversible reaction of converting the aldehydes into alcohol | Synechocystis sp. PCC 6803 | ? | - |
- |
|
additional information | alcohol dehydrogenase catalyzes a reversible reaction of converting the aldehydes into alcohol | Synechocystis sp. PCC 6803 Kazusa | ? | - |
- |
|
phenylethanol + NAD+ | - |
Synechocystis sp. PCC 6803 | phenylacetaldehyde + NADH + H+ | - |
r | |
phenylethanol + NAD+ | - |
Synechocystis sp. PCC 6803 Kazusa | phenylacetaldehyde + NADH + H+ | - |
r | |
sinapaldehyde + NADH | preferred substrates | Synechocystis sp. PCC 6803 | sinapyl alcohol + NAD+ | - |
r | |
sinapaldehyde + NADH + H+ | preferred substrates | Synechocystis sp. PCC 6803 | sinalcohol + NAD+ | - |
r | |
sinapaldehyde + NADH + H+ | preferred substrates | Synechocystis sp. PCC 6803 Kazusa | sinalcohol + NAD+ | - |
r | |
sinapaldehyde + NADH + H+ | preferred substrates | Synechocystis sp. PCC 6803 | sinapyl alcohol + NAD+ | - |
r |
Subunits | Comment | Organism |
---|---|---|
More | enzyme three-dimensional structure homology modeling, the structure is formed by fifteen alpha-helices, three beta sheets, twenty-two beta turns, and three gamma turns. All these elements are connected by loops | Synechocystis sp. PCC 6803 |
Synonyms | Comment | Organism |
---|---|---|
ADH | - |
Synechocystis sp. PCC 6803 |
slr1192 | - |
Synechocystis sp. PCC 6803 |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | cofactor docking to the enzyme. The affinity for NADH coenzyme attachment is higher than the values provided for NADPH | Synechocystis sp. PCC 6803 | |
NAD+ | - |
Synechocystis sp. PCC 6803 | |
NADH | - |
Synechocystis sp. PCC 6803 |
General Information | Comment | Organism |
---|---|---|
additional information | docking studies suggest that the enzyme might have several active sites for different substrates, homology structure modeling, and detailed ligand molecular interaction analysis/molecular docking analysis using the template crystal structure with PDB ID 6C49, overview | Synechocystis sp. PCC 6803 |