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Information on EC 1.4.1.12 - 2,4-diaminopentanoate dehydrogenase for references in articles please use BRENDA:EC1.4.1.12Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Bacteria
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2,4-diaminopentanoate dehydrogenase
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(2R,4S)-2,4-diaminopentanoate + H2O + NAD(P)+ = (2R)-2-amino-4-oxopentanoate + NH3 + NAD(P)H + H+
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L-ornithine degradation II (Stickland reaction)
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Arginine and proline metabolism
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D-Arginine and D-ornithine metabolism
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(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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2,4-diaminopentanoic acid C4 dehydrogenase
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2R,4S-2,4-diaminopentanoate dehydrogenase
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brenda
M-E, SB4
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brenda
M-E, SB4
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brenda
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brenda
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metabolism
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the enzyme plays a regulatory role in the oxidative ornithine degradation pathway
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(2R,4S)-2,4-diaminopentanoate + H2O + NAD+
(2R)-2-amino-4-oxopentanoate + NH3 + NADH + H+
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-
?
(2R,4S)-2,4-diaminopentanoate + H2O + NADP+
(2R)-2-amino-4-oxopentanoate + NH3 + NADPH + H+
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?
(2R,5S)-2,5-diaminopentanoate + H2O + NADP+
(2R)-2-amino-5-oxopentanoate + NH3 + NADPH + H+
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?
2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
2,4-diaminopentanoate + H2O + NAD+
2-amino-4-oxopentanoate + NH3 + NADH
2,4-diaminopentanoate + H2O + NADP+
2-amino-4-oxopentanoate + NH3 + NADPH
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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
2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
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2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
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r
2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
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r
2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
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r
2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
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r
2,4-diaminopentanoate + H2O + NAD+
2-amino-4-oxopentanoate + NH3 + NADH
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2,4-diaminopentanoate + H2O + NAD+
2-amino-4-oxopentanoate + NH3 + NADH
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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
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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
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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
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2-amino-5-oxohexanoate cyclizes non-enzymically to 1-pyrroline-2-methyl-5-carboxylate
r
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(2R,4S)-2,4-diaminopentanoate + H2O + NAD+
(2R)-2-amino-4-oxopentanoate + NH3 + NADH + H+
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?
(2R,4S)-2,4-diaminopentanoate + H2O + NADP+
(2R)-2-amino-4-oxopentanoate + NH3 + NADPH + H+
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?
2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
2,5-diaminohexanoate + H2O + NAD(P)+
2-amino-5-oxohexanoate + NH3 + NAD(P)H
2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
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2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
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r
2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
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r
2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
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r
2,4-diaminopentanoate + H2O + NAD(P)+
2-amino-4-oxopentanoate + NH3 + NAD(P)H
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r
2,5-diaminohexanoate + H2O + NAD(P)+
2-amino-5-oxohexanoate + NH3 + NAD(P)H
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r
2,5-diaminohexanoate + H2O + NAD(P)+
2-amino-5-oxohexanoate + NH3 + NAD(P)H
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r
2,5-diaminohexanoate + H2O + NAD(P)+
2-amino-5-oxohexanoate + NH3 + NAD(P)H
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r
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pyridoxal 5'-phosphate
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NAD+
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NAD+
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the enzyme can function with both nucleotides as hydrogen acceptors, NADP+ and NAD+
NAD+
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the activity of the enzyme with NAD+ is 5.4times higher than that with NADP+
NADP+
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NADP+
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the enzyme can function with both nucleotides as hydrogen acceptors, NADP+ and NAD+
NADP+
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the activity of the enzyme with NAD+ is 5.4times higher than that with NADP+
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additional information
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no stimulation of activity by Mg2+, Zn2+, Mn2+, Fe2+, Cd2+, Ni2+, Cu2+
additional information
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Mn2+ has no significant effect on enzyme activity
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(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
Ni2+
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2% residual activity at 0.5 mM
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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0.2
(2R,4S)-2,4-diaminopentanoate
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at pH 8.5 and 55°C
2
(2R,5S)-2,5-diaminopentanoate
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at pH 8.5 and 55°C
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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
NAD+
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at pH 8.5 and 55°C
0.11 - 0.28
NADP+
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2
NADP+
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at pH 8.5 and 55°C
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65
(2R,4S)-2,4-diaminopentanoate
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at pH 8.5 and 55°C
0.0006
(2R,5S)-2,5-diaminopentanoate
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at pH 8.5 and 55°C
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34
NAD+
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65
NAD+
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at pH 8.5 and 55°C
5
NADP+
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57
NADP+
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at pH 8.5 and 55°C
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330
(2R,4S)-2,4-diaminopentanoate
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at pH 8.5 and 55°C
0.0003
(2R,5S)-2,5-diaminopentanoate
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at pH 8.5 and 55°C
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0.016
NAD+
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1300
NAD+
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at pH 8.5 and 55°C
2.56
NADP+
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29
NADP+
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at pH 8.5 and 55°C
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0.1
D-ornithine
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at pH 8.5 and 55°C
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8.8
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2,4-diaminopentanoate + NAD+ + H2O
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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
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additional information
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assay carried out at room temperature
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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
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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
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9
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unstable above
391436
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90
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the half-denaturation time at 90°C is 38 min and 2 min at 100°C
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4°C, phosphate buffer, pH 7,5, 10-20% glycerol, one month
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expressed in Escherichia coli Rosetta (DE3) cells
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ORD_ACESD
Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / NCIMB 10654)
353
37896
Swiss-Prot
A0A1X6WQS6_9ENTE
352
37547
TrEMBL
B9DPU3_STACT
Staphylococcus carnosus (strain TM300)
316
35039
TrEMBL
A0A2H5Z3F9_9BACT
334
36077
TrEMBL
A0A2H5ZHT2_9BACT
354
38427
TrEMBL
A0A1M4PP76_9FIRM
[Clostridium] ultunense Esp
348
37923
TrEMBL
A0A2H5YJG7_9BACT
344
36592
TrEMBL
A0A2H5XBC1_9BACT
346
36892
TrEMBL
A0A1S1NER8_9MYCO
362
38298
TrEMBL
A0A2S8BHA9_9MYCO
377
38972
TrEMBL
A0A2S8BMT5_9MYCO
354
37657
TrEMBL
A0A2H5VJA6_9BACT
330
35264
TrEMBL
V5WGZ7_9SPIO
367
38755
TrEMBL
A0A2S8BQS1_9MYCO
374
39130
TrEMBL
A0A1B6BB44_9FIRM
350
37522
TrEMBL
R7RSP1_9CLOT
345
37476
TrEMBL
I7J6N7_9CLOT
346
37550
TrEMBL
A0A1S1NB04_9MYCO
354
37052
TrEMBL
Q188N4_PEPD6
Peptoclostridium difficile (strain 630)
355
38723
TrEMBL
A0A2H5ZWJ7_9BACT
357
38180
TrEMBL
A0A1S1NIR0_9MYCO
362
39164
TrEMBL
A0A2S8BCX0_9MYCO
207
22470
TrEMBL
A0A2S8BNA2_9MYCO
366
38908
TrEMBL
M1ZKP9_9FIRM
[Clostridium] ultunense Esp
303
33022
TrEMBL
A0A011A3H8_9CLOT
346
38031
TrEMBL
A0A1S1NQ69_9MYCO
363
38261
TrEMBL
A0A2H5YP29_9BACT
332
36128
TrEMBL
A0A2S8BM69_9MYCO
496
51770
TrEMBL
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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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