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Literature summary for 1.4.1.1 extracted from

  • Ohashima, T.; Soda, K.
    Purification and properties of alanine dehydrogenase from Bacillus sphaericus (1979), Eur. J. Biochem., 100, 29-39.
    View publication on PubMed
Search for more literature for 1.4.1.1

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Lysinibacillus sphaericus

Inhibitors

Inhibitors Comment Organism Structure
Cu2+
-
 Lysinibacillus sphaericus
HgCl2
-
 Lysinibacillus sphaericus
Pb2+
-
 Lysinibacillus sphaericus
PCMB
-
 Lysinibacillus sphaericus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.014
-
 L-norvaline
-
 Lysinibacillus sphaericus
0.018
-
 L-Ala
-
 Lysinibacillus sphaericus
0.02
-
 L-Val
-
 Lysinibacillus sphaericus
0.039
-
 L-Ser
-
 Lysinibacillus sphaericus
0.33
-
 L-2-aminobutanoate
-
 Lysinibacillus sphaericus
1.7
-
 pyruvate
-
 Lysinibacillus sphaericus
11
-
 2-oxobutanoate
-
 Lysinibacillus sphaericus
11
-
 2-oxo-3-methylbutanoate
-
 Lysinibacillus sphaericus
12
-
 glyoxylate
-
 Lysinibacillus sphaericus
23
-
 2-oxopentanoate
-
 Lysinibacillus sphaericus
80
-
 3-hydroxypyruvate
-
 Lysinibacillus sphaericus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
230000
-
 gel filtration Lysinibacillus sphaericus
231000
-
 equilibrium sedimentation Lysinibacillus sphaericus

Organism

Organism UniProt Comment Textmining
Lysinibacillus sphaericus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Lysinibacillus sphaericus

Reaction

Reaction Comment Organism Reaction ID
L-alanine + H2O + NAD+ = pyruvate + NH3 + NADH + H+ sequential ordered ternary-binary mechanism, the enzyme is A-stereospecific, the pro-R hydrogen at C-4 of the reduced nicotinamide ring of NADH is exclusively transferred to pyruvate Lysinibacillus sphaericus
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
157
-
-
 Lysinibacillus sphaericus

Storage Stability

Storage Stability Organism
4°C, 80% saturated ammonium sulfate suspension, pH 7-8, 2 years, stable Lysinibacillus sphaericus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxo-3-methylbutanoate + NH3 + NADH
-
 Lysinibacillus sphaericus L-Val + NAD+ + H2O
-
 ?
2-oxobutanoate + NH3 + NADH
-
 Lysinibacillus sphaericus 2-aminobutanoate + H2O + NAD+
-
 r
glyoxylate + NH3 + NADH
-
 Lysinibacillus sphaericus aminoacetate + NAD+ + H2O
-
 ?
L-2-aminobutanoate + H2O + NAD+
-
 Lysinibacillus sphaericus 2-oxobutanoate + NH3 + NADH + H+
-
 r
L-Ala + H2O + NAD+
-
 Lysinibacillus sphaericus pyruvate + NH3 + NADH
-
 r
L-norvaline + H2O + NAD+
-
 Lysinibacillus sphaericus 2-oxopentanoate + NH3 + NADH
-
 r
L-Ser + H2O + NAD+
-
 Lysinibacillus sphaericus 3-hydroxypyruvate + NH3 + NADH
-
 r
L-Val + H2O + NAD+
-
 Lysinibacillus sphaericus 3-methyl-2-oxobutanoate + NH3 + NADH
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
 increase of activity up to Lysinibacillus sphaericus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 pH 6.0-10.0, 5 min, stable Lysinibacillus sphaericus
60
-
 pH 7.2, 10 mM potassium phosphate buffer, 5 min, stable up to Lysinibacillus sphaericus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
 reductive amination Lysinibacillus sphaericus
10 10.5 oxidative deamination Lysinibacillus sphaericus
10.5
-
 deamination of L-Ala Lysinibacillus sphaericus

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 10 50°C, 5 min, stable Lysinibacillus sphaericus

Cofactor

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