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Literature summary for 1.1.1.1 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

Inhibitors Comment Organism Structure
additional information design of inhibitors Equus caballus

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Equus caballus
-
-
-

Reaction

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

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Equus caballus
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Equus caballus
NADH
-
Equus caballus