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Literature summary for 1.4.1.1 extracted from

  • Kuroda, S.; Tanizawa, K.; Sakamoto, Y.; Tanaka, H.; Soda, K.
    Alanine dehydrogenases from two Bacillus species with distinct thermostabilities: molecular cloning, DNA and protein sequence determination, and structural comparison with other NAD(P)(+)-dependent dehydrogenases (1990), Biochemistry, 29, 1009-1015.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
cloned and expressed in Escherichia coli Lysinibacillus sphaericus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
39465
-
6 * 39465, calculation from nucleotide sequence Lysinibacillus sphaericus
39500
-
6 * 39500, recombinant enzyme, SDS-PAGE Lysinibacillus sphaericus
235000
-
recombinant enzyme, gel filtration Lysinibacillus sphaericus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
-
-
Lysinibacillus sphaericus
-
gene cloned and expressed in Escherichia coli
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Lysinibacillus sphaericus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Ala + H2O + NAD+
-
Geobacillus stearothermophilus pyruvate + NH3 + NADH
-
r
L-Ala + H2O + NAD+
-
Lysinibacillus sphaericus pyruvate + NH3 + NADH
-
r

Subunits

Subunits Comment Organism
hexamer
-
Geobacillus stearothermophilus
hexamer 6 * 39500, recombinant enzyme, SDS-PAGE Lysinibacillus sphaericus
hexamer 6 * 39465, calculation from nucleotide sequence Lysinibacillus sphaericus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65
-
5 min, 50% loss of activity Lysinibacillus sphaericus
85
-
5 min, 50% loss of activity Geobacillus stearothermophilus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Geobacillus stearothermophilus
NAD+
-
Lysinibacillus sphaericus
NADH
-
Geobacillus stearothermophilus
NADH
-
Lysinibacillus sphaericus