HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 1.4.1.11 - L-erythro-3,5-diaminohexanoate dehydrogenase
for references in articles please use BRENDA:EC1.4.1.11Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Clostridium sp.
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
1.4.1.11
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
L-erythro-3,5-diaminohexanoate dehydrogenase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-erythro-3,5-diaminohexanoate + H2O + NAD+ = (S)-5-amino-3-oxohexanoate + NH3 + NADH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amination
-
-
-
-
Deamination
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
L-erythro-3,5-diaminohexanoate:NAD+ oxidoreductase (deaminating)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37377-90-5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+
-
the equilibrium of the dehydrogenase reaction is more favorable for amino acid oxidation than are the equilibria of other similar reactions
-
-
r
L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NADH + NH4+
-
the equilibrium of the dehydrogenase reaction is more favorable for amino acid oxidation than are the equilibria of other similar reactions
-
-
r
L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NH3 + NADH + H+
Brevibacterium L5
-
3-keto-5-aminohexanoate has the (5S) configuration. First step in the decomposition of 3,5-diaminohexanoate by the aerobic Brevibacterium L5
-
-
r
L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NH3 + NADH + H+
Brevibacterium L5
-
3-keto-5-aminohexanoate has the (5S) configuration
-
-
r
L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NH3 + NADH + H+
-
enzyme is involved in lysine degradation
-
-
?
L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NH3 + NADH + H+
-
enzyme is involved in lysine degradation
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
-
3-keto-5-aminohexanoate has the (5S) configuration. First step in the decomposition of 3,5-diaminohexanoate by the aerobic Brevibacterium L5
-
-
r
L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NH3 + NADH + H+
-
enzyme is involved in lysine degradation
-
-
?
L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NH3 + NADH + H+
-
enzyme is involved in lysine degradation
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-acetylpyridine-NAD+
-
70% of activity with NAD+, activity with NADP is 1.3% of the activity with NAD+
additional information
-
activity with NADP+ is 1.3% of the activity with NAD+
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-erythro-3,5-diaminohexanoate
-
non-competitive inhibitor of L-erythro-3,5-diaminohexanoate
DL-threo-3,5-diaminohexanoate
-
partial inhibition by concentrations above 0.3 mM, pH 6.8
NADH
-
dimeric and tetrameric form of enzyme: product inhibition, competitive inhibitor to NAD+ and uncompetitive inhibitor to 5-amino-3-oxohexanoate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.18
L-erythro-3,5-diaminohexanoate
-
pH 6.8, 24°C, tetrameric form of enzyme, pH 6.8
0.22
L-erythro-3,5-diaminohexanoate
-
pH 6.8, 24°C, tetrameric form of enzyme, above pH 6.8
0.25
L-erythro-3,5-diaminohexanoate
-
pH 6.6, 24°C, dimeric form of enzyme, pH 6.6
0.77
L-erythro-3,5-diaminohexanoate
-
pH 6.8, 24°C, tetrameric form of enzyme, pH 7.6 and pH 8.9
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.3 - 10.2
Brevibacterium L5
-
pH 8.3: about 55% of maximal activity, pH 10.2: about 60% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37000
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
additional information
dimer
-
2 * 37000, the dimer is about one third as active as the tetramer, SDS-PAGE
dimer
-
2 * 37000, the dimer is about one third as active as the tetramer, SDS-PAGE
-
tetramer
-
4 * 37000, the dimer is about one third as active as the tetramer, SDS-PAGE
tetramer
-
4 * 37000, the dimer is about one third as active as the tetramer, SDS-PAGE
-
additional information
-
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7
-
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
-
enzyme is most stable between pH 7.0 and 8.5
391432
7.8
-
in the absence of glycerol the enzyme dissociates and inactivates at pH 7.8 or above
391434
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, suspension in ammonium sulfate, 6 months, no detectable loss of activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 1.4.1.11)
html completed
Use of this online version of BRENDA is free but requires a license. See terms of use.
Information
