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Information on EC 1.4.1.11 - L-erythro-3,5-diaminohexanoate dehydrogenase
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1.4.1.11 L-erythro-3,5-diaminohexanoate dehydrogenaseSpecify your search results
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
dehydrogenase, L-3,5-diaminohexanoate, L-3,5-diaminohexanoate dehydrogenase, L-erythro-3,5-diaminohexanoate dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, L-3,5-diaminohexanoate
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L-3,5-diaminohexanoate dehydrogenase
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L-erythro-3,5-diaminohexanoate dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-erythro-3,5-diaminohexanoate + H2O + NAD+ = (S)-5-amino-3-oxohexanoate + NH3 + NADH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amination
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Deamination
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oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
L-erythro-3,5-diaminohexanoate:NAD+ oxidoreductase (deaminating)
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CAS REGISTRY NUMBER
COMMENTARY
37377-90-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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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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. 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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.77
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
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
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
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
A0A1V6F8I0_9BACT
353
0
38162
TrEMBL
A0A1V6I541_9BACT
347
0
37309
TrEMBL
A0A1V6KA36_9BACT
46
0
5171
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
A0A1V4I6N9_9FIRM
345
0
37762
TrEMBL
E3DP58_HALPG
Halanaerobium praevalens (strain ATCC 33744 / DSM 2228 / GSL)
344
0
37126
TrEMBL
A0A1V5IMC8_9ACTN
357
0
37775
TrEMBL
A0A1V5H6T8_9BACT
346
0
37186
TrEMBL
A0A1V6HPN0_9DELT
348
0
36547
TrEMBL
A0A1V5R7A7_9BACT
345
0
36987
TrEMBL
E6SAM9_INTC7
Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP)
376
0
38630
TrEMBL
A0A1V5JZ61_9FIRM
159
0
16451
TrEMBL
A0A1V6J5G7_9BACT
347
0
37363
TrEMBL
A0A0H3JB70_CLOPA
344
0
37070
TrEMBL
A0A1V5HML9_9BACT
346
0
37477
TrEMBL
A0A1V5U290_9FIRM
346
0
37127
TrEMBL
A1SK30_NOCSJ
Nocardioides sp. (strain ATCC BAA-499 / JS614)
353
0
36104
TrEMBL
A0A151B3X6_9CLOT
345
0
37220
TrEMBL
A0A1V5Y7C2_9FIRM
346
0
37274
TrEMBL
A0A151B3N6_9CLOT
685
0
78433
TrEMBL
A0A0S2W1Z4_9FIRM
346
0
36967
TrEMBL
M5DWV1_9FIRM
344
0
37165
TrEMBL
I4D4X2_DESAJ
Desulfosporosinus acidiphilus (strain DSM 22704 / JCM 16185 / SJ4)
345
0
36786
TrEMBL
A0A1V5WT66_9BACT
353
0
38441
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
A0A1V6JI53_9BACT
346
0
37348
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
additional information
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, suspension in ammonium sulfate, 6 months, no detectable loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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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