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EC Tree
IUBMB Comments The enzyme, which has been isolated from the bacterium Pseudomonas aeruginosa PAO1, forms with EC 1.4.99.6, D-arginine dehydrogenase, a two-enzyme complex involved in the racemization of D- and L-arginine.
The enzyme appears in viruses and cellular organisms
Synonyms
anabolic L-arginine dehydrogenase,
dauB , NAD(P)H-dependent anabolic L-arginine dehydrogenase,
more
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anabolic L-arginine dehydrogenase
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NAD(P)H-dependent anabolic L-arginine dehydrogenase
dauB
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NAD(P)H-dependent anabolic L-arginine dehydrogenase
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NAD(P)H-dependent anabolic L-arginine dehydrogenase
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L-arginine + H2O + NAD(P)+ = 5-guanidino-2-oxopentanoate + NH3 + NAD(P)H + H+
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L-arginine:NAD(P)+ oxidoreductase (deaminating)
The enzyme, which has been isolated from the bacterium Pseudomonas aeruginosa PAO1, forms with EC 1.4.99.6, D-arginine dehydrogenase, a two-enzyme complex involved in the racemization of D- and L-arginine.
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5-guanidino-2-oxopentanoate + NH3 + NAD(P)H + H+
L-arginine + H2O + NAD(P)+
L-arginine + H2O + NAD(P)+
5-guanidino-2-oxopentanoate + NH3 + NAD(P)H + H+
additional information
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5-guanidino-2-oxopentanoate + NH3 + NAD(P)H + H+
L-arginine + H2O + NAD(P)+
DauB uses 2-ketoarginine and ammonia derived from D-arginine in the DauA-catalyzed reaction
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5-guanidino-2-oxopentanoate + NH3 + NAD(P)H + H+
L-arginine + H2O + NAD(P)+
DauB uses 2-ketoarginine and ammonia derived from D-arginine in the DauA-catalyzed reaction
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L-arginine + H2O + NAD(P)+
5-guanidino-2-oxopentanoate + NH3 + NAD(P)H + H+
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L-arginine + H2O + NAD(P)+
5-guanidino-2-oxopentanoate + NH3 + NAD(P)H + H+
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no substantial reaction with D-arginine
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additional information
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no substantial reaction with D-arginine
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UniProt
brenda
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UniProt
brenda
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physiological function
strains with a lesion at DauA or DauB genes fail to use D-arginine as sole carbon source. Growth complementation of an L-arginine auxotroph by D-arginine is abolished by a lesion at DauA or DauB. Presence of D-arginine induces L-arginine-specific genes in the parental strain PAO1 but not in its dauA or dauB mutants. DauA catalyzes oxidative deamination of D-arginine into 2-ketoarginine and ammonia, and DauB is able to use 2-ketoarginine and ammonia as substrates and convert them into L-arginine in the presence of NADPH or NADH
physiological function
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strains with a lesion at DauA or DauB genes fail to use D-arginine as sole carbon source. Growth complementation of an L-arginine auxotroph by D-arginine is abolished by a lesion at DauA or DauB. Presence of D-arginine induces L-arginine-specific genes in the parental strain PAO1 but not in its dauA or dauB mutants. DauA catalyzes oxidative deamination of D-arginine into 2-ketoarginine and ammonia, and DauB is able to use 2-ketoarginine and ammonia as substrates and convert them into L-arginine in the presence of NADPH or NADH
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DAUB_PSEAE
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
315
0
33945
Swiss-Prot
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A0A5E6UUX2_PSEFL
310
0
33470
TrEMBL
-
A0A5E7LAI2_PSEFL
315
0
33852
TrEMBL
-
A0A5E7RZS5_PSEFL
314
0
33743
TrEMBL
-
A0A6J5AKL2_9BURK
323
0
34810
TrEMBL
-
A0A5E7T0Q3_PSEFL
314
0
34067
TrEMBL
-
A0A5E7SQ10_PSEFL
315
0
33910
TrEMBL
-
A0A5M9IZW4_9PSED
315
0
33784
TrEMBL
-
A0A6S7BGW4_9BURK
375
0
40824
TrEMBL
-
A0A5E6Q302_PSEFL
127
0
13718
TrEMBL
-
A0A5E7E7M1_PSEFL
318
0
34563
TrEMBL
-
A0A5E7RN26_PSEFL
314
0
33798
TrEMBL
-
A0A5M9I2D8_PSEPA
311
0
33254
TrEMBL
-
A0A5E6U6E0_PSEFL
318
0
34520
TrEMBL
-
A0A5E7PRV1_PSEFL
315
0
33823
TrEMBL
-
A0A5E7HZD9_PSEFL
318
0
34522
TrEMBL
-
A0A6L5BX79_9PSED
315
0
34023
TrEMBL
-
A0A5E7CUP4_PSEFL
314
0
33820
TrEMBL
-
A0A5E7BRA4_PSEFL
315
0
33876
TrEMBL
-
A0A5E6MY01_PSEFL
314
0
33911
TrEMBL
-
A0A6J5FV88_9BURK
325
0
34768
TrEMBL
-
A0A5E6W114_PSEFL
315
0
33998
TrEMBL
-
A0A653NHP5_9PSED
317
0
33707
TrEMBL
-
A0A6J4ZUI0_9BURK
320
0
34581
TrEMBL
-
A0A6J5JY98_9BURK
320
0
34608
TrEMBL
-
A0A5E6WYH2_PSEFL
314
0
33982
TrEMBL
-
A0A5E7A513_PSEFL
317
0
34283
TrEMBL
-
A0A5E6RC01_PSEFL
314
0
33832
TrEMBL
-
A0A5E6XRX5_PSEFL
316
0
34342
TrEMBL
-
A0A5E7HVS5_PSEFL
315
0
34196
TrEMBL
-
A0A5E6R035_PSEFL
314
0
33698
TrEMBL
-
A0A5E6RWK1_PSEFL
314
0
33886
TrEMBL
-
A0A6J5E791_9BURK
320
0
33368
TrEMBL
-
A0A7M1JMD3_PSEAI
315
0
33870
TrEMBL
-
A0A5E7L177_PSEFL
314
0
33910
TrEMBL
-
A0A5E7JB31_PSEFL
314
0
34012
TrEMBL
-
A0A5E7K678_PSEFL
314
0
33808
TrEMBL
-
A0A5E7JJB6_PSEFL
314
0
33605
TrEMBL
-
B1FSX3_PARG4
Paraburkholderia graminis (strain ATCC 700544 / DSM 17151 / LMG 18924 / NCIMB 13744 / C4D1M)
322
0
34542
TrEMBL
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A0A5E6TNN9_PSEFL
314
0
33514
TrEMBL
-
A0A5E7MFG0_PSEFL
314
0
33709
TrEMBL
-
A0A5E7GG48_PSEFL
314
0
33754
TrEMBL
-
A0A5E6Q548_PSEFL
168
0
18125
TrEMBL
-
A0A5E7NF32_PSEFL
315
0
34144
TrEMBL
-
A0A5E7JUC6_PSEFL
315
0
33876
TrEMBL
-
A0A5E7C720_PSEFL
317
0
34300
TrEMBL
-
A0A5E7G0Q8_PSEFL
315
0
33891
TrEMBL
-
A0A6J5G3I1_9BURK
337
0
34974
TrEMBL
-
A0A5E7U1Q9_PSEFL
314
0
33682
TrEMBL
-
A0A5E6SXN1_PSEFL
314
0
33894
TrEMBL
-
A0A5E7L8R4_PSEFL
315
0
34029
TrEMBL
-
A0A5E6T5F4_PSEFL
315
0
33931
TrEMBL
-
A0A5E7K7G9_PSEFL
315
0
33815
TrEMBL
-
A0A2N7WM59_9BURK
320
0
34220
TrEMBL
-
A0A5E7CYA0_PSEFL
314
0
33862
TrEMBL
-
A0A5E7CP06_PSEFL
314
0
33980
TrEMBL
-
A0A5E7K0R0_PSEFL
315
0
33835
TrEMBL
-
A0A1X1PH31_9BURK
320
0
33429
TrEMBL
-
A0A5E7MZS5_PSEFL
314
0
33799
TrEMBL
-
A0A5E7CXC0_PSEFL
314
0
33793
TrEMBL
-
A0A6J5FWP8_9BURK
355
0
38345
TrEMBL
-
A0A5E7KXX2_PSEFL
314
0
33910
TrEMBL
-
A0A5E6UUC4_PSEFL
315
0
33895
TrEMBL
-
A0A5E7V227_PSEFL
314
0
33904
TrEMBL
-
A0A5E7TY18_PSEFL
315
0
33871
TrEMBL
-
A0A5E7IGA1_PSEFL
318
0
34462
TrEMBL
-
A0A653YLM8_9PSED
317
0
33732
TrEMBL
-
A0A5E7VVU0_PSEFL
315
0
34000
TrEMBL
-
A0A5E7JJC4_PSEFL
318
0
34567
TrEMBL
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expression in Escherichia coli
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expression of the DauBAR operon is highly induced in presence of D-arginine
expression of the DauBAR operon is highly induced in presence of D-arginine
expression of the DauBAR operon is highly induced in presence of D-arginine
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Li, C.; Lu, C.D.
Arginine racemization by coupled catabolic and anabolic dehydrogenases
Proc. Natl. Acad. Sci. USA
106
906-911
2009
Pseudomonas aeruginosa (Q9HXE4), Pseudomonas aeruginosa DSM 22644 (Q9HXE4)
brenda
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