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

BRENDA support

Literature summary for 1.4.1.11 extracted from

  • Baker, J.J.; Jeng, I.; Barker, H.A.
    Purification and properties of L-erythro-3,5-diaminohexanoate dehydrogenase from a lysine-fermenting Clostridium (1972), J. Biol. Chem., 247, 7724-7734.
    View publication on PubMed
Search for more literature for 1.4.1.11

General Stability

General Stability Organism
enzyme is very unstable in crude extracts and to dilution in buffer, purified enzyme is only partially inactivated by dilution in a solution of low ionic strength Clostridium sp.

Inhibitors

Inhibitors Comment Organism Structure
D-erythro-3,5-diaminohexanoate non-competitive inhibitor of L-erythro-3,5-diaminohexanoate Clostridium sp.
DL-threo-3,5-diaminohexanoate partial inhibition by concentrations above 0.3 mM, pH 6.8 Clostridium sp.
NADH dimeric and tetrameric form of enzyme: product inhibition, competitive inhibitor to NAD+ and uncompetitive inhibitor to 5-amino-3-oxohexanoate Clostridium sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.074
-
 NADH pH 7.0, 23°C Clostridium sp.
0.13
-
 NAD+ pH 6.6, 24°C, dimeric form of enzyme Clostridium sp.
0.18
-
 L-erythro-3,5-diaminohexanoate pH 6.8, 24°C, tetrameric form of enzyme, pH 6.8 Clostridium sp.
0.22
-
 L-erythro-3,5-diaminohexanoate pH 6.8, 24°C, tetrameric form of enzyme, above pH 6.8 Clostridium sp.
0.25
-
 L-erythro-3,5-diaminohexanoate pH 6.6, 24°C, dimeric form of enzyme, pH 6.6 Clostridium sp.
0.26
-
 5-amino-3-oxohexanoate pH 7.0, 23°C Clostridium sp.
0.28
-
 NAD+ pH 6.8, 24°C, tetrameric form of enzyme Clostridium sp.
0.77
-
 L-erythro-3,5-diaminohexanoate pH 6.8, 24°C, tetrameric form of enzyme, pH 7.6 and pH 8.9 Clostridium sp.
140
-
 NH4+ pH 7.0, 23°C Clostridium sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
37000
-
 2 * 37000, the dimer is about one third as active as the tetramer, SDS-PAGE Clostridium sp.
37000
-
 4 * 37000, the dimer is about one third as active as the tetramer, SDS-PAGE Clostridium sp.
68000
-
 dimer, gel filtration Clostridium sp.
135000
-
 tetramer, gel filtration Clostridium sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-erythro-3,5-diaminohexanoate + H2O + NAD+ Clostridium sp. enzyme is involved in lysine degradation 5-amino-3-oxohexanoate + NH3 + NADH + H+
-
 ?
L-erythro-3,5-diaminohexanoate + H2O + NAD+ Clostridium sp. SB4 enzyme is involved in lysine degradation 5-amino-3-oxohexanoate + NH3 + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Clostridium sp.
-
-
-
Clostridium sp. SB4
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Clostridium sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
34
-
-
 Clostridium sp.

Storage Stability

Storage Stability Organism
12°C, 100 mM EDTA, pH 6.8, 5 months, 50% loss of activity Clostridium sp.
4°C, suspension in ammonium sulfate, 6 months, no detectable loss of activity Clostridium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-erythro-3,5-diaminohexanoate + H2O + NAD+ enzyme is involved in lysine degradation Clostridium sp. 5-amino-3-oxohexanoate + NH3 + NADH + H+
-
 ?
L-erythro-3,5-diaminohexanoate + H2O + NAD+ enzyme is involved in lysine degradation Clostridium sp. SB4 5-amino-3-oxohexanoate + NH3 + NADH + H+
-
 ?
L-erythro-3,5-diaminohexanoate + H2O + NAD+ the equilibrium of the dehydrogenase reaction is more favorable for amino acid oxidation than are the equilibria of other similar reactions Clostridium sp. 5-amino-3-oxohexanoate + NADH + NH4+
-
 r
L-erythro-3,5-diaminohexanoate + H2O + NAD+ the equilibrium of the dehydrogenase reaction is more favorable for amino acid oxidation than are the equilibria of other similar reactions Clostridium sp. SB4 5-amino-3-oxohexanoate + NADH + NH4+
-
 r

Subunits

Subunits Comment Organism
dimer 2 * 37000, the dimer is about one third as active as the tetramer, SDS-PAGE Clostridium sp.
More the enzyme can exist in at least two forms which have different specific activities. The more active form is favored by a high concentration of enzyme and by the presence of a saturating level of L-erythro-3,5-diaminohexanoate and of high concentrations of various salts of which ammonium chloride, Tris chloride, and sodium EDTA are most effective. The less active form is favored by a low concentration of enzyme and low ionic strength Clostridium sp.
tetramer 4 * 37000, the dimer is about one third as active as the tetramer, SDS-PAGE Clostridium sp.

Synonyms

Synonyms Comment Organism
L-erythro-3,5-diaminohexanoate dehydrogenase
-
 Clostridium sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4
-
 in absence of glycerol and EDTA, half-life is 100 h Clostridium sp.

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 7 the pH at which the enzyme is most stable depends on the buffer, but generally it is between 6 and 7 Clostridium sp.
7.8
-
 in the absence of glycerol the enzyme dissociates and inactivates at pH 7.8 or above Clostridium sp.

Cofactor

Cofactor Comment Organism Structure
3-acetylpyridine-NAD+ 70% of activity with NAD+, activity with NADP is 1.3% of the activity with NAD+ Clostridium sp.
additional information activity with NADP+ is 1.3% of the activity with NAD+ Clostridium sp.
NAD+ NAD+ is most active cofactor Clostridium sp.

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.004
-
 NADH pH 6.8, 24°C, tetrameric form of enzyme Clostridium sp.
0.5
-
 D-erythro-3,5-diaminohexanoate pH 6.7, 24°C Clostridium sp.
1.2
-
 DL-threo-3,5-diaminohexanoate pH 6.7, 24°C Clostridium sp.
16
-
 NADH pH 6.6, 24°C, dimeric form of enzyme Clostridium sp.