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Literature summary for 1.1.1.21 extracted from

  • Atsumi, S.; Wu, T.Y.; Eckl, E.M.; Hawkins, S.D.; Buelter, T.; Liao, J.C.
    Engineering the isobutanol biosynthetic pathway in Escherichia coli by comparison of three aldehyde reductase/alcohol dehydrogenase genes (2010), Appl. Microbiol. Biotechnol., 85, 651-657.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.1.21

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 cells Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1
-
 Isobutyraldehyde in 50 mM MOPS buffer, pH 7.0, at 37°C Escherichia coli
1.1
-
 acetaldehyde in 50 mM MOPS buffer, pH 7.0, at 37°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetaldehyde + NADPH + H+
-
 Escherichia coli ethanol + NADP+
-
 ?
isobutyraldehyde + NADPH + H+
-
 Escherichia coli isobutanol + NADP+
-
 ?

Synonyms

Synonyms Comment Organism
isobutyraldehyde reductase
-
 Escherichia coli
YqhD YqhD contributes significantly to the isobutyraldehyde reductase activity in Escherichia coli Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8
-
 Isobutyraldehyde in 50 mM MOPS buffer, pH 7.0, at 37°C Escherichia coli
27.6
-
 acetaldehyde in 50 mM MOPS buffer, pH 7.0, at 37°C Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADPH dependent on Escherichia coli