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Literature summary extracted from

  • Adolph, H.W.; Maurer, P.; Schneider-Bernloehr, H.; Sartorius, C.; Zeppezauer, M.
    Substrate specificity and stereoselectivity of horse liver alcohol dehydrogenase. Kinetic evaluation of binding and activation parameters controlling the catalytic cycles of unbranched, acyclic secondary alcohols and ketones as substrates of the native and active-site-specific Co(II)-substituted enzyme (1991), Eur. J. Biochem., 201, 615-625.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.1 additional information design of inhibitors Equus caballus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.1 additional information
-
 additional information Km-values of active-site Co(II)substituted enzyme Equus caballus
1.1.1.1 0.18
-
 (S)-2-octanol
-
 Equus caballus
1.1.1.1 0.73
-
 (S)-2-pentanol
-
 Equus caballus
1.1.1.1 1.35
-
 (S)-2-butanol
-
 Equus caballus
1.1.1.1 1.6
-
 3-Pentanol
-
 Equus caballus
1.1.1.1 1.92
-
 (R)-2-octanol
-
 Equus caballus
1.1.1.1 7.5
-
 (R)-2-butanol
-
 Equus caballus
1.1.1.1 9
-
 Isopropanol
-
 Equus caballus
1.1.1.1 14.2
-
 2-Pentanone
-
 Equus caballus
1.1.1.1 15
-
 2-butanone
-
 Equus caballus
1.1.1.1 31.7
-
 (R)-2-pentanol
-
 Equus caballus
1.1.1.1 75
-
 3-Pentanone
-
 Equus caballus
1.1.1.1 135
-
 acetone
-
 Equus caballus

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.1 Equus caballus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.1 a primary alcohol + NAD+ = an aldehyde + NADH + H+ ordered bi-bi mechanism Equus caballus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.1 liver
-
 Equus caballus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.1 (R)-2-butanol + NAD+
-
 Equus caballus butanone + NADH + H+
-
 r
1.1.1.1 (R)-2-octanol + NAD+
-
 Equus caballus 2-octanone + NADH + H+
-
 ?
1.1.1.1 (R)-2-pentanol + NAD+
-
 Equus caballus 2-pentanone + NADH + H+
-
 ?
1.1.1.1 (S)-2-butanol + NAD+
-
 Equus caballus butanone + NADH + H+
-
 r
1.1.1.1 (S)-2-octanol + NAD+
-
 Equus caballus 2-octanone + NADH + H+
-
 ?
1.1.1.1 (S)-2-pentanol + NAD+
-
 Equus caballus 2-pentanone + NADH + H+
-
 ?
1.1.1.1 2-pentanone + NADH + H+
-
 Equus caballus pentan-2-ol + NAD+
-
 r
1.1.1.1 3-pentanone + NADH
-
 Equus caballus pentan-3-ol + NAD+
-
 r
1.1.1.1 acetone + NADH
-
 Equus caballus isopropanol + NAD+
-
 r
1.1.1.1 butan-2-ol + NAD+ (R)-2-butanol and (S)-2-butanol Equus caballus butan-2-one + NADH
-
 ?
1.1.1.1 butan-2-one + NADH
-
 Equus caballus butan-2-ol + NAD+
-
 r
1.1.1.1 octan-2-ol + NAD+ (R)-2-octanol and (S)-2-octanol Equus caballus octan-2-one + NADH
-
 ?
1.1.1.1 pentan-2-ol + NAD+ (R)-2-pentanol and (S)-2-pentanol Equus caballus 2-pentanone + NADH
-
 r
1.1.1.1 pentan-3-ol + NAD+
-
 Equus caballus 3-pentanone + NADH
-
 r

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.1 additional information
-
 additional information Km-values of active-site Co(II)substituted enzyme Equus caballus
1.1.1.1 0.053
-
 (R)-2-octanol
-
 Equus caballus
1.1.1.1 0.0713
-
 2-Pentanone
-
 Equus caballus
1.1.1.1 0.12
-
 2-butanone
-
 Equus caballus
1.1.1.1 0.33
-
 acetone
-
 Equus caballus
1.1.1.1 0.36
-
 3-Pentanone
-
 Equus caballus
1.1.1.1 0.58
-
 Isopropanol
-
 Equus caballus
1.1.1.1 0.87
-
 (S)-2-pentanol
-
 Equus caballus
1.1.1.1 1
-
 (S)-2-butanol
-
 Equus caballus
1.1.1.1 1.01
-
 (R)-2-pentanol
-
 Equus caballus
1.1.1.1 1.52
-
 (S)-2-octanol
-
 Equus caballus
1.1.1.1 2
-
 (R)-2-butanol
-
 Equus caballus
1.1.1.1 2.26
-
 3-Pentanol
-
 Equus caballus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.1 NAD+
-
 Equus caballus
1.1.1.1 NADH
-
 Equus caballus