Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.4.1.1 extracted from

  • Hutter, B.; Singh, M.
    Properties of the 40 kDa antigen of Mycobacterium tuberculosis, a functional L-alanine dehydrogenase (1999), Biochem. J., 343, 669-672.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.4.1.1

Inhibitors

Inhibitors Comment Organism Structure
CuSO4 50.7% inhibition by 1 mM, 96.3% inhibition by 20 mM, EDTA in a 10fold molar excess restores activity almost completely, recombinant enzyme Mycobacterium tuberculosis
Zn2+ 26.5% inhibition by 1 mM ZnCl2, 90.1% inhibition by 20 mM ZnCl2, EDTA in a 10fold molar excess restores activity almost completely, recombinant enzyme Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0982
-
 NADH
-
 Mycobacterium tuberculosis
0.31
-
 NAD+
-
 Mycobacterium tuberculosis
1.45
-
 pyruvate
-
 Mycobacterium tuberculosis
13.8
-
 L-Ala
-
 Mycobacterium tuberculosis
35.4
-
 NH4+
-
 Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-Ala + H2O + NAD+ Mycobacterium tuberculosis since the physiological environment of the organism has a neutral pH, it can be assumed that the enzyme catalyzes exclusively the formation of L-Ala pyruvate + NH3 + NADH
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-alanine + H2O + NAD+ = pyruvate + NH3 + NADH + H+ oxidative deamination proceeds by an random-ordered mechanism Mycobacterium tuberculosis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-2-aminobutanoate + H2O + NAD+ in the reverse reaction 2-oxobutanoate reacts with 1.2% of the activity with pyruvate Mycobacterium tuberculosis 2-oxobutanoate + NH3 + NADH + H+
-
 r
L-2-aminobutanoate + H2O + NAD+ 0.7% of the activity with L-Ala Mycobacterium tuberculosis 2-oxobutanoate + NH3 + NADH + H+
-
 r
L-Ala + H2O + NAD+
-
 Mycobacterium tuberculosis pyruvate + NH3 + NADH
-
 r
L-Ala + H2O + NAD+ since the physiological environment of the organism has a neutral pH, it can be assumed that the enzyme catalyzes exclusively the formation of L-Ala Mycobacterium tuberculosis pyruvate + NH3 + NADH
-
 ?
L-Ala + H2O + NADP+ in the reverse direction NADPH reacts at 1.6% of the activity with NADH Mycobacterium tuberculosis pyruvate + NH3 + NADPH
-
 r
L-Ala + H2O + NADP+ 2.5% of the activity with NAD+ Mycobacterium tuberculosis pyruvate + NH3 + NADPH
-
 r
L-Ser + H2O + NAD+ no activity Mycobacterium tuberculosis 3-hydroxypyruvate + NH3 + NADH
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
 4 h, 25% loss of activity, recombinant enzyme Mycobacterium tuberculosis
65.7
-
 5 min, 50% loss of activity, recombinant enzyme Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 7.5 reductive amination Mycobacterium tuberculosis
10 11 oxidative deamination Mycobacterium tuberculosis

pH Range

pH Minimum pH Maximum Comment Organism
6 8 pH 6.0: about 30% of maximal activity, pH 8.5: about 25% of maximal activity, reductive amination Mycobacterium tuberculosis
8.5 11.5 pH 8.5: about 35% of maximal activity, pH 11.5: about 20% of maximal activity, oxidative deamination Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Mycobacterium tuberculosis
NADH
-
 Mycobacterium tuberculosis
NADP+
-
 Mycobacterium tuberculosis
NADPH
-
 Mycobacterium tuberculosis