Information on EC 1.4.1.12 - 2,4-diaminopentanoate dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
1.4.1.12
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RECOMMENDED NAME
GeneOntology No.
2,4-diaminopentanoate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2R,4S)-2,4-diaminopentanoate + H2O + NAD(P)+ = (2R)-2-amino-4-oxopentanoate + NH3 + NAD(P)H + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-ornithine degradation II (Stickland reaction)
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urea cycle
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Lysine degradation
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Arginine and proline metabolism
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D-Arginine and D-ornithine metabolism
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SYSTEMATIC NAME
IUBMB Comments
(2R,4S)-2,4-diaminopentanoate:NAD(P)+ oxidoreductase (deaminating)
Also acts, more slowly, on 2,5-diaminohexanoate forming 2-amino-5-oxohexanoate, which then cyclizes non-enzymically to 1-pyrroline-2-methyl-5-carboxylate. It has equal activity with NAD+ and NADP+ [cf. EC 1.4.1.26, 2,4-diaminopentanoate dehydrogenase (NAD+)].
CAS REGISTRY NUMBER
COMMENTARY hide
39346-26-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
M-E, SB4
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Manually annotated by BRENDA team
M-E, SB4
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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the enzyme plays a regulatory role in the oxidative ornithine degradation pathway
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R,4S)-2,4-diaminopentanoate + H2O + NAD+
(2R)-2-amino-4-oxopentanoate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
(2R,4S)-2,4-diaminopentanoate + H2O + NADP+
(2R)-2-amino-4-oxopentanoate + NH3 + NADPH + H+
show the reaction diagram
-
-
-
-
?
(2R,5S)-2,5-diaminopentanoate + H2O + NADP+
(2R)-2-amino-5-oxopentanoate + NH3 + NADPH + H+
show the reaction diagram
-
-
-
-
?
2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
show the reaction diagram
2,4-diaminopentanoate + H2O + NAD+
2-amino-4-oxopentanoate + NH3 + NADH
show the reaction diagram
2,4-diaminopentanoate + H2O + NADP+
2-amino-4-oxopentanoate + NH3 + NADPH
show the reaction diagram
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enzyme is more efficient with the natural substrate (2R,4S)-2,4-diaminopentanoate (Vmax: 51.6/sec) it also reacts with (2R,4R)-2,4-diaminopentanoate (Vmax: 2.8/sec)
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-
?
2,5-diaminohexanoate + H2O + NAD(P)+
2-amino-5-oxohexanoate + NH3 + NAD(P)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
(2R,4S)-2,4-diaminopentanoate + H2O + NAD+
(2R)-2-amino-4-oxopentanoate + NH3 + NADH + H+
show the reaction diagram
-
-
-
-
?
(2R,4S)-2,4-diaminopentanoate + H2O + NADP+
(2R)-2-amino-4-oxopentanoate + NH3 + NADPH + H+
show the reaction diagram
-
-
-
-
?
2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
show the reaction diagram
2,5-diaminohexanoate + H2O + NAD(P)+
2-amino-5-oxohexanoate + NH3 + NAD(P)H
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
pyridoxal 5'-phosphate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2R,4S)-2,4-diaminopentanoate
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uncompetitive substrate inhibition
2-amino-4-ketopentanoate
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70% inhibition in the presence of 1 mM 2-amino-4-ketopentanoate
5,5'-dithiobis(2-nitrobenzoate)
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acetyl-CoA
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30% inhibition in the presence of 1 mM acetyl-CoA
Ca2+
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85% residual activity at 0.5 mM
Co2+
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34% residual activity at 0.5 mM
Cu2+
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complete inhibition at 0.5 mM
D-alanine
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45% inhibition in the presence of 1 mM D-alanine
D-ornithine
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uncompetitive inhibition
Fe2+
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84% residual activity at 0.5 mM
Mg2+
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65% residual activity at 0.5 mM
N-ethylmaleimide
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Ni2+
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2% residual activity at 0.5 mM
Organic mercurials
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p-chloromercuribenzoate
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Zn2+
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2% residual activity at 0.5 mM
additional information
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not inhibited by EDTA, KBr, KCl, KNO3, CH3COOK, and K2SO4
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
(2R,4S)-2,4-diaminopentanoate
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at pH 8.5 and 55C
2
(2R,5S)-2,5-diaminopentanoate
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at pH 8.5 and 55C
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1.2 - 1.8
2,4-Diaminopentanoate
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2.5
2,5-Diaminohexanoate
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0.05 - 2100
NAD+
0.11 - 2
NADP+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
65
(2R,4S)-2,4-diaminopentanoate
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at pH 8.5 and 55C
0.0006
(2R,5S)-2,5-diaminopentanoate
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at pH 8.5 and 55C
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34 - 65
NAD+
5 - 57
NADP+
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
330
(2R,4S)-2,4-diaminopentanoate
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at pH 8.5 and 55C
0.0003
(2R,5S)-2,5-diaminopentanoate
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at pH 8.5 and 55C
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0.016 - 1300
NAD+
2.56 - 29
NADP+
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
D-ornithine
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at pH 8.5 and 55C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.8
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2,4-diaminopentanoate + NAD+ + H2O
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 10
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half maximal activity at pH 8.0 and 10.0, 2,4-diaminopentanoate + NAD+ + H2O
9 - 10
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the enzyme shows more than 70% of maximum activity at pH 9.0-10.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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assay carried out at room temperature
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35400
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2 * 35400 SDS-PAGE, sedimentation centrifugation in 6 M guanidine-HCl
38930
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calculated from cDNA
40000
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2 * 40000 SDS-PAGE, gel electrophoresis
72000 - 80000
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sedimentation equilibrium centrifugation
80000
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gel electrophoresis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 38000, SDS-PAGE
dimer
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2 * 35400 SDS-PAGE, sedimentation centrifugation in 6 M guanidine-HCl; 2 * 40000 SDS-PAGE, gel electrophoresis
homodimer
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gel filtration, 2 * 38000 Da
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
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unstable above
391436
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90
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the half-denaturation time at 90C is 38 min and 2 min at 100C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, phosphate buffer, pH 7,5, 10-20% glycerol, one month
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta (DE3) cells
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