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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
dehydrogenase, L-3,5-diaminohexanoate, L-3,5-diaminohexanoate dehydrogenase, L-erythro-3,5-diaminohexanoate dehydrogenase,
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dehydrogenase, L-3,5-diaminohexanoate
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L-3,5-diaminohexanoate dehydrogenase
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L-erythro-3,5-diaminohexanoate dehydrogenase
L-erythro-3,5-diaminohexanoate dehydrogenase
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L-erythro-3,5-diaminohexanoate dehydrogenase
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L-erythro-3,5-diaminohexanoate + H2O + NAD+ = (S)-5-amino-3-oxohexanoate + NH3 + NADH + H+
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L-erythro-3,5-diaminohexanoate:NAD+ oxidoreductase (deaminating)
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L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NADH + NH4+
L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NH3 + NADH + H+
L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NADH + NH4+
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the equilibrium of the dehydrogenase reaction is more favorable for amino acid oxidation than are the equilibria of other similar reactions
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L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NADH + NH4+
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the equilibrium of the dehydrogenase reaction is more favorable for amino acid oxidation than are the equilibria of other similar reactions
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L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NH3 + NADH + H+
Brevibacterium L5
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3-keto-5-aminohexanoate has the (5S) configuration. First step in the decomposition of 3,5-diaminohexanoate by the aerobic Brevibacterium L5
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L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NH3 + NADH + H+
Brevibacterium L5
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3-keto-5-aminohexanoate has the (5S) configuration
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L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NH3 + NADH + H+
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enzyme is involved in lysine degradation
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L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NH3 + NADH + H+
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enzyme is involved in lysine degradation
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L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NH3 + NADH + H+
L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NH3 + NADH + H+
Brevibacterium L5
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3-keto-5-aminohexanoate has the (5S) configuration. First step in the decomposition of 3,5-diaminohexanoate by the aerobic Brevibacterium L5
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L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NH3 + NADH + H+
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enzyme is involved in lysine degradation
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L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NH3 + NADH + H+
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enzyme is involved in lysine degradation
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3-acetylpyridine-NAD+
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70% of activity with NAD+, activity with NADP is 1.3% of the activity with NAD+
additional information
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activity with NADP+ is 1.3% of the activity with NAD+
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NAD+
Brevibacterium L5
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NAD+
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NAD+ is most active cofactor
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D-erythro-3,5-diaminohexanoate
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non-competitive inhibitor of L-erythro-3,5-diaminohexanoate
DL-threo-3,5-diaminohexanoate
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partial inhibition by concentrations above 0.3 mM, pH 6.8
L-erythro-3,5-diaminohexanoate
Brevibacterium L5
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NADH
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dimeric and tetrameric form of enzyme: product inhibition, competitive inhibitor to NAD+ and uncompetitive inhibitor to 5-amino-3-oxohexanoate
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0.26
5-amino-3-oxohexanoate
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pH 7.0, 23°C
0.18 - 0.77
L-erythro-3,5-diaminohexanoate
0.074
NADH
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pH 7.0, 23°C
0.18
L-erythro-3,5-diaminohexanoate
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pH 6.8, 24°C, tetrameric form of enzyme, pH 6.8
0.22
L-erythro-3,5-diaminohexanoate
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pH 6.8, 24°C, tetrameric form of enzyme, above pH 6.8
0.25
L-erythro-3,5-diaminohexanoate
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pH 6.6, 24°C, dimeric form of enzyme, pH 6.6
0.75
L-erythro-3,5-diaminohexanoate
Brevibacterium L5
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pH 9.3
0.77
L-erythro-3,5-diaminohexanoate
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pH 6.8, 24°C, tetrameric form of enzyme, pH 7.6 and pH 8.9
0.13
NAD+
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pH 6.6, 24°C, dimeric form of enzyme
0.28
NAD+
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pH 6.8, 24°C, tetrameric form of enzyme
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0.5
D-erythro-3,5-diaminohexanoate
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pH 6.7, 24°C
1.2
DL-threo-3,5-diaminohexanoate
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pH 6.7, 24°C
0.004
NADH
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pH 6.8, 24°C, tetrameric form of enzyme
16
NADH
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pH 6.6, 24°C, dimeric form of enzyme
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9.3
Brevibacterium L5
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8.3 - 10.2
Brevibacterium L5
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pH 8.3: about 55% of maximal activity, pH 10.2: about 60% of maximal activity
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Brevibacterium L5
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brenda
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brenda
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brenda
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135000
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tetramer, gel filtration
68000
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dimer, gel filtration
71000
Brevibacterium L5
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gel filtration
37000
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2 * 37000, the dimer is about one third as active as the tetramer, SDS-PAGE
37000
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4 * 37000, the dimer is about one third as active as the tetramer, SDS-PAGE
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dimer
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2 * 37000, the dimer is about one third as active as the tetramer, SDS-PAGE
dimer
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2 * 37000, the dimer is about one third as active as the tetramer, SDS-PAGE
tetramer
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4 * 37000, the dimer is about one third as active as the tetramer, SDS-PAGE
tetramer
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4 * 37000, the dimer is about one third as active as the tetramer, SDS-PAGE
additional information
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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
additional information
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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
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6 - 7
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the pH at which the enzyme is most stable depends on the buffer, but generally it is between 6 and 7
391434
7 - 8.5
Brevibacterium L5
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enzyme is most stable between pH 7.0 and 8.5
391432
7.8
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in the absence of glycerol the enzyme dissociates and inactivates at pH 7.8 or above
391434
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4
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in absence of glycerol and EDTA, half-life is 100 h
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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
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-20°C, 4 months, enzyme in cells extract is stable for 4 months
Brevibacterium L5
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12°C, 100 mM EDTA, pH 6.8, 5 months, 50% loss of activity
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4°C, suspension in ammonium sulfate, 6 months, no detectable loss of activity
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Hong, S.C.L.; Barker, H.A.
Aerobic metabolism of 3,5-diaminohexanoate in a Brevibacterium. Purification of 3,5-diaminohexanoate dehydrogenase and degradation of 3-keto-5-aminohexanoate
J. Biol. Chem.
248
41-49
1973
Brevibacterium L5
brenda
Baker, J.J.; Jeng, I.; Barker, H.A.
Purification and properties of L-erythro-3,5-diaminohexanoate dehydrogenase from a lysine-fermenting Clostridium
J. Biol. Chem.
247
7724-7734
1972
Clostridium sp., Clostridium sp. SB4
brenda
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1.4.1.11 L-erythro-3,5-diaminohexanoate dehydrogenase
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