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Information on EC 1.4.1.11 - L-erythro-3,5-diaminohexanoate dehydrogenase for references in articles please use BRENDA:EC1.4.1.11
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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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r
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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r
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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r
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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?
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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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r
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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KDD_ACESD
Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / NCIMB 10654)
344
0
36786
Swiss-Prot
KDD_FUSNN
Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131)
345
0
36892
Swiss-Prot
A0A1V6H2I4_9BACT
345
0
37061
TrEMBL
A0A1V5NGK6_9BACT
346
0
36910
TrEMBL
A0A151B3A6_9CLOT
350
0
37711
TrEMBL
A0A1V6C3A5_9BACT
347
0
37347
TrEMBL
G8S6N4_ACTS5
Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110)
336
0
34354
TrEMBL
A0A1E3X8I7_9BACT
351
0
37853
TrEMBL
A0A1V6F8I0_9BACT
353
0
38162
TrEMBL
A0A1V6I541_9BACT
347
0
37309
TrEMBL
A0A0H5CFK7_9PSEU
341
0
34791
TrEMBL
A0A1V6KA36_9BACT
46
0
5171
TrEMBL
W6K3G6_9MICO
271
0
28300
TrEMBL
A4X763_SALTO
Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440)
353
0
36068
TrEMBL
A0A1V5J4W1_9FIRM
346
0
36591
TrEMBL
B0VJ11_CLOAI
Cloacimonas acidaminovorans (strain Evry)
352
0
38279
TrEMBL
A0A0B3BLR6_9THEO
346
0
37584
TrEMBL
A0A1V4I6N9_9FIRM
345
0
37762
TrEMBL
E3DP58_HALPG
Halanaerobium praevalens (strain ATCC 33744 / DSM 2228 / GSL)
344
0
37126
TrEMBL
A0A1V1VYU2_9ACTN
347
0
35765
TrEMBL
A0A1V5IMC8_9ACTN
357
0
37775
TrEMBL
A0A1V5H6T8_9BACT
346
0
37186
TrEMBL
A0A1S8L4H8_9CLOT
344
0
37266
TrEMBL
A0A1V6HPN0_9DELT
348
0
36547
TrEMBL
I0L439_9ACTN
267
0
26738
TrEMBL
A0A1V5R7A7_9BACT
345
0
36987
TrEMBL
M1YQC8_9FIRM
345
0
37050
TrEMBL
E6SAM9_INTC7
Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP)
376
0
38630
TrEMBL
U5Q8K9_9BACT
346
0
37024
TrEMBL
A0A1V5JZ61_9FIRM
159
0
16451
TrEMBL
A0A132MSY7_9ACTN
49
0
5346
TrEMBL
A0A1V5T6A3_9BACT
346
0
36731
TrEMBL
A0A1V6J5G7_9BACT
347
0
37363
TrEMBL
A0A3P3XGY2_9SPIR
346
0
37254
TrEMBL
R1CHA5_9CLOT
345
0
37143
TrEMBL
A0A1V4ICV7_9CLOT
344
0
37158
TrEMBL
A0A0K3BT97_9PSEU
340
0
35028
TrEMBL
A0A0H3JB70_CLOPA
344
0
37070
TrEMBL
A0A1V5HML9_9BACT
346
0
37477
TrEMBL
U5Q8R7_9BACT
344
0
36799
TrEMBL
A0A1V5U290_9FIRM
346
0
37127
TrEMBL
R7RPE4_9CLOT
344
0
37075
TrEMBL
A0A1C4YKG4_9ACTN
353
0
36027
TrEMBL
A1SK30_NOCSJ
Nocardioides sp. (strain ATCC BAA-499 / JS614)
353
0
36104
TrEMBL
A0A3P3XT97_9SPIR
346
0
37465
TrEMBL
A0A1V6A201_9BACT
347
0
36979
TrEMBL
A0A151B3X6_9CLOT
345
0
37220
TrEMBL
A0A1V5JH96_9BACT
371
0
38043
TrEMBL
A0A3E2YK77_9ACTN
353
0
36105
TrEMBL
A0A2P8AYN3_9ACTN
338
0
34679
TrEMBL
A0A0K2J432_PORGN
347
0
37206
TrEMBL
A1X0G6_9ZZZZ
352
0
38279
TrEMBL
I7J5C9_9CLOT
346
0
37626
TrEMBL
A0A1V5Y7C2_9FIRM
346
0
37274
TrEMBL
W7J7H4_9PSEU
350
0
35322
TrEMBL
A0A1G4FIZ8_9FIRM
345
0
37141
TrEMBL
A0A151B3N6_9CLOT
685
0
78433
TrEMBL
A0A0S2W1Z4_9FIRM
346
0
36967
TrEMBL
A0A0R3JWG2_9CLOT
346
0
37482
TrEMBL
A0A1S8L610_9CLOT
344
0
37179
TrEMBL
M5DWV1_9FIRM
344
0
37165
TrEMBL
I4D4X2_DESAJ
Desulfosporosinus acidiphilus (strain DSM 22704 / JCM 16185 / SJ4)
345
0
36786
TrEMBL
A0A2P2CDF4_9ZZZZ
346
0
35779
TrEMBL
A0A2P2BVF8_9FIRM
343
0
37120
TrEMBL
A0A0K1J2J3_9RHOO
345
0
36422
TrEMBL
A0A1B6BDM8_9FIRM
345
0
36830
TrEMBL
A0A0J1FHK9_9FIRM
352
0
37008
TrEMBL
A0A088T3Q1_9BACT
342
0
36639
TrEMBL
A0A094IK06_9BACT
345
0
36841
TrEMBL
A0A1V5WT66_9BACT
353
0
38441
TrEMBL
A0A1J5PZV8_9ZZZZ
118
0
12723
TrEMBL
A0A385ARD6_9ACTN
338
0
34394
TrEMBL
A0A517XWC5_9BACT
121
0
12535
TrEMBL
Q21RL4_RHOFT
Rhodoferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
347
0
36804
TrEMBL
Q2IEQ1_ANADE
Anaeromyxobacter dehalogenans (strain 2CP-C)
340
0
35264
TrEMBL
A0A140L6N1_9CLOT
345
0
36644
TrEMBL
A0A2P2CBC5_9ZZZZ
359
0
36442
TrEMBL
A0A1V6JI53_9BACT
346
0
37348
TrEMBL
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135000
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tetramer, gel filtration
37000
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2 * 37000, the dimer is about one third as active as the tetramer, SDS-PAGE; 4 * 37000, the dimer is about one third as active as the tetramer, SDS-PAGE
68000
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dimer, gel filtration
71000
Brevibacterium L5
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gel filtration
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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
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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
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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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Brevibacterium L5
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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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