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Literature summary for 1.1.1.1 extracted from

  • Haghighi, O.; Moradi, M.
    In silico study of the structure and ligand interactions of alcohol dehydrogenase from cyanobacterium Synechocystis sp. PCC 6803 as a key enzyme for biofuel production (2020), Appl. Biochem. Biotechnol., 192, 1346-1367 .
    View publication on PubMed

Application

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(Commentary)

Cloned (Comment) Organism
gene slr1192, sequence comparisons and phylogenetic analysis and tree Synechocystis sp. PCC 6803

Metals/Ions

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Synechocystis sp. PCC 6803 P74721
-
-
Synechocystis sp. PCC 6803 Kazusa P74721
-
-

Substrates and Products (Substrate)

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

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

Synonyms Comment Organism
ADH
-
Synechocystis sp. PCC 6803
slr1192
-
Synechocystis sp. PCC 6803

Cofactor

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

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