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Information on EC 1.4.1.12 - 2,4-diaminopentanoate dehydrogenase
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1.4.1.12 2,4-diaminopentanoate dehydrogenaseIUBMB Comments
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+)].
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Word Map
- 1.4.1.12
- nadp+
- meso-diaminopimelate
-
meso-dap
-
nadp+-dependent
-
symbiobacterium
- thermophilum
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
dapdh, 2,4-dapdh, 2,4-diaminopentanoate dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2R,4S)-2,4-diaminopentanoate + H2O + NAD(P)+ = (2R)-2-amino-4-oxopentanoate + NH3 + NAD(P)H + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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+)].
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CAS REGISTRY NUMBER
COMMENTARY
39346-26-4
-
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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
(2R,4S)-2,4-diaminopentanoate + H2O + NAD+
(2R)-2-amino-4-oxopentanoate + NH3 + NADH + H+
-
-
-
-
?
(2R,4S)-2,4-diaminopentanoate + H2O + NADP+
(2R)-2-amino-4-oxopentanoate + NH3 + NADPH + H+
-
-
-
-
?
(2R,5S)-2,5-diaminopentanoate + H2O + NADP+
(2R)-2-amino-5-oxopentanoate + NH3 + NADPH + H+
-
-
-
-
?
2,4-diaminopentanoate + H2O + NADP+
2-amino-4-oxopentanoate + NH3 + NADPH
-
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)
-
-
?
2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
-
-
-
-
2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
-
-
-
r
2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
-
-
-
r
2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
-
-
-
r
2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
-
-
-
r
2,4-diaminopentanoate + H2O + NAD+
2-amino-4-oxopentanoate + NH3 + NADH
-
-
-
-
-
2,4-diaminopentanoate + H2O + NAD+
2-amino-4-oxopentanoate + NH3 + NADH
-
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)
-
-
?
2,5-diaminohexanoate + H2O + NAD(P)+
2-amino-5-oxohexanoate + NH3 + NAD(P)H
-
-
2-amino-5-oxohexanoate cyclizes non-enzymically to 1-pyrroline-2-methyl-5-carboxylate
r
2,5-diaminohexanoate + H2O + NAD(P)+
2-amino-5-oxohexanoate + NH3 + NAD(P)H
-
-
2-amino-5-oxohexanoate cyclizes non-enzymically to 1-pyrroline-2-methyl-5-carboxylate
r
2,5-diaminohexanoate + H2O + NAD(P)+
2-amino-5-oxohexanoate + NH3 + NAD(P)H
-
-
2-amino-5-oxohexanoate cyclizes non-enzymically to 1-pyrroline-2-methyl-5-carboxylate
r
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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
(2R,4S)-2,4-diaminopentanoate + H2O + NAD+
(2R)-2-amino-4-oxopentanoate + NH3 + NADH + H+
-
-
-
-
?
(2R,4S)-2,4-diaminopentanoate + H2O + NADP+
(2R)-2-amino-4-oxopentanoate + NH3 + NADPH + H+
-
-
-
-
?
2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
-
-
-
-
2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
-
-
-
r
2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
-
-
-
r
2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
-
-
-
r
2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
-
-
-
r
2,5-diaminohexanoate + H2O + NAD(P)+
2-amino-5-oxohexanoate + NH3 + NAD(P)H
-
-
-
r
2,5-diaminohexanoate + H2O + NAD(P)+
2-amino-5-oxohexanoate + NH3 + NAD(P)H
-
-
-
r
2,5-diaminohexanoate + H2O + NAD(P)+
2-amino-5-oxohexanoate + NH3 + NAD(P)H
-
-
-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
the enzyme can function with both nucleotides as hydrogen acceptors, NADP+ and NAD+
NAD+
-
the activity of the enzyme with NAD+ is 5.4times higher than that with NADP+
NADP+
-
the enzyme can function with both nucleotides as hydrogen acceptors, NADP+ and NAD+
NADP+
-
the activity of the enzyme with NAD+ is 5.4times higher than that with NADP+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
no stimulation of activity by Mg2+, Zn2+, Mn2+, Fe2+, Cd2+, Ni2+, Cu2+
additional information
-
Mn2+ has no significant effect on enzyme activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-amino-4-ketopentanoate
-
70% inhibition in the presence of 1 mM 2-amino-4-ketopentanoate
additional information
-
not inhibited by EDTA, KBr, KCl, KNO3, CH3COOK, and K2SO4
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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 - 10
-
half maximal activity at pH 8.0 and 10.0, 2,4-diaminopentanoate + NAD+ + H2O
9 - 10
-
the enzyme shows more than 70% of maximum activity at pH 9.0-10.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the enzyme plays a regulatory role in the oxidative ornithine degradation pathway
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
ORD_ACESD
Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / NCIMB 10654)
353
0
37896
Swiss-Prot
K5BAL8_MYCHD
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)
358
0
38079
TrEMBL
A0A3P3ZUC2_MYCHD
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)
369
0
39290
TrEMBL
K5BEM7_MYCHD
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)
347
0
37039
TrEMBL
K5BAK8_MYCHD
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)
347
0
37487
TrEMBL
K5BKW0_MYCHD
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)
359
0
38069
TrEMBL
K5BFT5_MYCHD
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)
137
0
13751
TrEMBL
K5BBX8_MYCHD
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)
364
0
38451
TrEMBL
K5BFL9_MYCHD
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)
359
0
38609
TrEMBL
A0A3P4A3S8_MYCHD
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)
360
0
38760
TrEMBL
K5BJ31_MYCHD
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)
357
0
38324
TrEMBL
K5BC81_MYCHD
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)
357
0
38496
TrEMBL
K5BE27_MYCHD
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)
353
0
37323
TrEMBL
K5BDJ3_MYCHD
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)
357
0
37948
TrEMBL
A0A3P3ZV62_MYCHD
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)
363
0
39426
TrEMBL
K5B9N8_MYCHD
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)
357
0
38243
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35400
-
2 * 35400 SDS-PAGE, sedimentation centrifugation in 6 M guanidine-HCl
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 35400 SDS-PAGE, sedimentation centrifugation in 6 M guanidine-HCl; 2 * 40000 SDS-PAGE, gel electrophoresis
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
90
-
the half-denaturation time at 90°C is 38 min and 2 min at 100°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Somack, R.; Costilow, R.N.
2,4-Diaminopentanoic acid C4 dehydrogenase, purification and properties of the protein
J. Biol. Chem.
247
385-388
1973
Acetoanaerobium sticklandii
brenda
Stadtman, T.C.
Lysine metyabolim by clostridia, XIIB 2,5-diaminohexanoate dehydrogenase (2,4-diaminopentanoate dehydrogenase)
Adv. Enzymol. Relat. Areas Mol. Biol.
38
441-445
1973
Acetoanaerobium sticklandii, Clostridium sp., Clostridium sp. M-E SB4
-
brenda
Tsuda, Y.; Friedmann, H.C.
Ornithine metabolism by Clostridium sticklandii. Oxidation of ornithine to 2-amino-4-ketopentanoic acid via 2,4-diaminopentanoic acid; participation of B12 coenzyme, pyridoxal phosphate, and pyridine nucleotide
J. Biol. Chem.
245
5914-5926
1970
Acetoanaerobium sticklandii
brenda
Fonknechten, N.; Perret, A.; Perchat, N.; Tricot, S.; Lechaplais, C.; Vallenet, D.; Vergne, C.; Zaparucha, A.; Le Paslier, D.; Weissenbach, J.; Salanoubat, M.
A conserved gene cluster rules anaerobic oxidative degradation of L-ornithine
J. Bacteriol.
191
3162-3167
2009
Acetoanaerobium sticklandii
brenda
Fukuyama, S.; Mihara, H.; Miyake, R.; Ueda, M.; Esaki, N.; Kurihara, T.
Characterization of a thermostable 2,4-diaminopentanoate dehydrogenase from Fervidobacterium nodosum Rt17-B1
J. Biosci. Bioeng.
117
551-556
2014
Fervidobacterium nodosum
brenda
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