Information on EC 1.4.1.B2 - L-erythro-3,5-diaminohexanoate dehydrogenase (NADP+)

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The expected taxonomic range for this enzyme is: Clostridium sticklandii

EC NUMBER
COMMENTARY hide
1.4.1.B2
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
L-erythro-3,5-diaminohexanoate dehydrogenase (NADP+)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-erythro-3,5-diaminohexanoate + H2O + NADP+ = (S)-5-amino-3-oxohexanoate + NH3 + NADPH + H+
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
L-erythro-3,5-diaminohexanoate:NADP+ oxidoreductase deaminating
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wastewater metagenomic collection
SwissProt
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 + acetylpyridine-NAD+
5-amino-3-oxohexanoate + NH3 + acetylpyridine-NADH + H+
show the reaction diagram
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-
-
-
?
L-erythro-3,5-diaminohexanoate + H2O + deamino-NAD+
5-amino-3-oxohexanoate + NH3 + deamino-NADH + H+
show the reaction diagram
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-
-
-
?
L-erythro-3,5-diaminohexanoate + H2O + NAD+
5-amino-3-oxohexanoate + NH3 + NADH + H+
show the reaction diagram
L-erythro-3,5-diaminohexanoate + H2O + NADP+
(S)-5-amino-3-oxohexanoate + NH3 + NADPH + H+
show the reaction diagram
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-
-
?
L-erythro-3,5-diaminohexanoate + H2O + NADP+
5-amino-3-oxohexanoate + NH3 + NADPH + 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
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either NAD+ or NADP+ serve as coenzyme. Double-reciprocal plots of activity versus pyridine nucleotide concentration are biphasic. The Km values for NADP+ are lower but a higher Vmax is observed with NAD+
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-
?
L-erythro-3,5-diaminohexanoate + H2O + NADP+
(S)-5-amino-3-oxohexanoate + NH3 + NADPH + H+
show the reaction diagram
A1X0G6
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-
-
?
L-erythro-3,5-diaminohexanoate + H2O + NADP+
5-amino-3-oxohexanoate + NH3 + NADPH + H+
show the reaction diagram
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either NAD+ or NADP+ serve as coenzyme. Double-reciprocal plots of activity versus pyridine nucleotide concentration are biphasic. The Km values for NADP+ are lower but a higher Vmax is observed with NAD+
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetylpyridine-NAD+
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deamino-NAD+
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NADP+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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5 mM, 2.3fold activation at pH 8.9, inhibition at pH 7.8
Co2+
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5 mM, 1.5fold activation at pH 8.9, inhibition at pH 7.8
Mn2+
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at pH 8.9 Mn2+ gives the highest increase in activity (232% at 0.5 mM). Concentrations of 0.01, 0.05, 0.1, 0.75, and 1.0 mM increase the enzyme activity by 110, 156, 188, 258, and 263%, respectively. The activity is maximal at 0.75 mM Mn2+
Zn2+
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5 mM, 1.6fold activation at pH 8.9, inhibition at pH 7.8
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4-Diaminopentanoate
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2,5-Diaminohexanoate
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5-amino-3-oxohexanoate
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competitive inhibition
ADP
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about half as effective as ATP
AMP
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32% as effective as ATP
arsenate
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addition of any of the neutral salts causes a parabolic inhibition. A direct comparison of arsenate and chloride ion shows that arsenate is not as inhibitory even though it has a higher ionic strength. Arsenate interacts with the enzyme differently from chloride and bromide. Sulfate, which is a large ion like arsenate, is as inhibitory as chloride (at equivalent ionic strength) with NAD+ as coenzyme, but it is much less effective than chloride with NADP+ as coenzyme
ATP
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competitive with respect to L-erythro-3,5-diaminohexanoate and NAD+
Br-
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addition of any of the neutral salts causes a parabolic inhibition. A direct comparison of arsenate and chloride ion shows that arsenate is not as inhibitory even though it has a higher ionic strength. Arsenate interacts with the enzyme differently from chloride and bromide. Sulfate, which is a large ion like arsenate, is as inhibitory as chloride (at equivalent ionic strength) with NAD+ as coenzyme, but it is much less effective than chloride with NADP+ as coenzyme
Ca2+
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0.5 mM, 22% inhibition at pH 7.8, cofactor NADP+, activation at pH 8.9
Cl-
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addition of any of the neutral salts causes a parabolic inhibition. A direct comparison of arsenate and chloride ion shows that arsenate is not as inhibitory even though it has a higher ionic strength. Arsenate interacts with the enzyme differently from chloride and bromide. Sulfate, which is a large ion like arsenate, is as inhibitory as chloride (at equivalent ionic strength) with NAD+ as coenzyme, but it is much less effective than chloride with NADP+ as coenzyme
Co2+
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0.5 mM, 71% inhibition at pH 7.8, cofactor NADP+, activation at pH 8.9
CTP
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about half as effective as ATP
Cu2+
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0.5 mM, 35% inhibition at pH 7.8, 30% inhibition at pH 8.9, cofactor NADP+
D-erythro-3,5-diaminohexanoate
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DL-beta-aminobutyrate
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Fe2+
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0.5 mM, 36% inhibition at pH 7.8, 9% inhibition at pH 8.9, cofactor NADP+
Fe3+
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0.5 mM, 8% inhibition at pH 8.9, no effect on activity at pH 7.8
GTP
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inhibits as effectively as ATP
L-beta-Lysine
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Mg2+
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0.5 mM, 63% inhibition at pH 7.8, cofactor NADP+, activation at pH 8.9
Mn2+
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0.5 mM, 52% inhibition at pH 7.8, cofactor NADP+, activation at pH 8.9
NADH
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competitive inhibition
NADPH
NH4+
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10 mM NH4Cl and higher, inhibits the reaction, probably due to the effect of chloride on the activity
SO42-
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addition of any of the neutral salts causes a parabolic inhibition. A direct comparison of arsenate and chloride ion shows that arsenate is not as inhibitory even though it has a higher ionic strength. Arsenate interacts with the enzyme differently from chloride and bromide. Sulfate, which is a large ion like arsenate, is as inhibitory as chloride (at equivalent ionic strength) with NAD+ as coenzyme, but it is much less effective than chloride with NADP+ as coenzyme
UTP
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16% as effective as ATP
Zn2+
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0.5 mM, 49% inhibition at pH 7.8, cofactor NADP+, activation at pH 8.9
additional information
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the lactams of DL-erythro-3,5-diaminohexanoate and DL-threo-3,5-diaminohexanoatae and 2-methylpyrrolidone-5-carboxylic acid have no effect on activity. Acetate (10 mM), butyrate (10 mM), acetyl phosphate (2 mM), or acetyl-CoA (0.62 mM) have no effect on enzyme activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.3
acetylpyridine-NAD+
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pH 8.8
22
deamino-NAD+
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pH 8.8
0.08 - 3.2
L-erythro-3,5-diaminohexanoate
0.48 - 16.5
NAD+
0.03 - 0.27
NADP+
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.52
2,4-Diaminopentanoate
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pH 7.4
0.19
2,5-Diaminohexanoate
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pH 7.4
1 - 4.5
ATP
0.1
D-erythro-3,5-diaminohexanoate
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pH 7.4
11.3
D-Lysine
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pH 7.4
73.4
DL-beta-aminobutyrate
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pH 7.4
2.5
L-beta-Lysine
5.4
L-ornithine
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pH 7.4
0.0195
NADH
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pH 7.4
0.0005
NADPH
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pH 7.4
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.7 - 9
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activity with NAD+ or NADP+
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3 - 9.5
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pH 7.3: about 45% of maximal activity, pH 9.5: about 80% of maximal activity, cofactor: NAD+
7.8 - 10.2
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pH 7.8: about 55% of maximal activity, pH 10.2: about 55% of maximal activity, cofactor: NADP+
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24 - 40
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activity with NAD+, the activity of the enzyme increases up to 24C, is relatively constant until 40C and then decreases
52
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activity with NADP+ increases up to 52C and then rapidly falls off, probably due to heat inactivation of the protein
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 59
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25C: about 40% of maximal activity, 50C: about 70% of maximal activity, cofactor: NAD+
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
82000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10.5
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25C, 30 min, no loss of activity
696177
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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30 min, no loss of activity
50
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t1/2: 56 min, inactivation follows first-order kinetics
55
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t1/2: 32 min, inactivation follows first-order kinetics. In the presence of both NAD+ and 3,5-diaminohexanoate, the enzyme is effectively stabilized against heat inactivation at 55C. NAD+ alone accelerates heat inactivation
59
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t1/2: 4 min, inactivation follows first-order kinetics
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 1 month, no loss of activity in crude enzyme extract
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23C, 1 day, no loss of activity in crude enzyme extract
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4C, 1 week, no loss of activity in crude enzyme extract
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, HisTrap FF column chromatography, MonoQ column chromatograhy, and Superdex 200 gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 DE3 cells