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Literature summary for 1.1.1.1 extracted from

  • Keung, W.M.; Yip, P.K.
    Rabbit liver alcohol dehydrogenase: isolation and characterization of class I isozymes (1989), Biochem. Biophys. Res. Commun., 158, 445-453.
    View publication on PubMed

General Stability

General Stability Organism
dithiothreitol stabilizes activity at all stages of purification Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
4-methoxypyrazole class I ADHs migrate towards cathode on starch gel and are very sensitive to 4-methylpyrazole inhibition, class II ADH migrates slowly towards anode and is less sensitive to 4-methylpyrazole, class II ADH migrates rapidly towards anode and is insensitive to 4-methylpyrazole Oryctolagus cuniculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
41700
-
2 * 41700, enzyme form CM-I: a polypeptide chain + C polypeptide chain, enzyme form CM-II: B-chain + C-chain, enzyme form CM III, homodimer of C chains, SDS-PAGE Oryctolagus cuniculus
74500
-
gel filtration Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
class I isoenzyme Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Oryctolagus cuniculus

Subunits

Subunits Comment Organism
dimer 2 * 41700, enzyme form CM-I: a polypeptide chain + C polypeptide chain, enzyme form CM-II: B-chain + C-chain, enzyme form CM III, homodimer of C chains, SDS-PAGE Oryctolagus cuniculus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Oryctolagus cuniculus
NADH
-
Oryctolagus cuniculus