Information on EC 1.4.1.11 - L-erythro-3,5-diaminohexanoate dehydrogenase

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The expected taxonomic range for this enzyme is: Clostridium

EC NUMBER
COMMENTARY hide
1.4.1.11
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RECOMMENDED NAME
GeneOntology No.
L-erythro-3,5-diaminohexanoate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-erythro-3,5-diaminohexanoate + H2O + NAD+ = (S)-5-amino-3-oxohexanoate + NH3 + NADH + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amination
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-
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-
Deamination
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-
-
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oxidation
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-
-
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redox reaction
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-
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reduction
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-lysine fermentation to acetate and butanoate
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Lysine degradation
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lysine metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-erythro-3,5-diaminohexanoate:NAD+ oxidoreductase (deaminating)
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CAS REGISTRY NUMBER
COMMENTARY hide
37377-90-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Brevibacterium L5
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-
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Manually annotated by BRENDA team
strain SB4
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Manually annotated by BRENDA team
strain SB4
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NADH + NH4+
show the reaction diagram
L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NH3 + NADH + H+
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NH3 + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-acetylpyridine-NAD+
-
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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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.26
5-amino-3-oxohexanoate
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pH 7.0, 23°C
0.18 - 0.77
L-erythro-3,5-diaminohexanoate
0.13 - 0.28
NAD+
0.074
NADH
-
pH 7.0, 23°C
140
NH4+
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pH 7.0, 23°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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 - 16
NADH
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.3
Brevibacterium L5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
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
68000
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dimer, gel filtration
71000
Brevibacterium L5
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gel filtration
135000
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tetramer, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
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in absence of glycerol and EDTA, half-life is 100 h
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
-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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE