Entry
Name
D-arginine dehydrogenase;
D-amino-acid:(acceptor) oxidoreductase (deaminating);
D-amino-acid dehydrogenase;
D-amino-acid:acceptor oxidoreductase (deaminating)
Class
Oxidoreductases;
Acting on the CH-NH2 group of donors;
With unknown physiological acceptors
BRITE hierarchy
Sysname
D-arginine:acceptor oxidoreductase (deaminating)
Reaction(IUBMB)
D-arginine + acceptor + H2O = 5-guanidino-2-oxopentanoate + NH3 + reduced acceptor (overall reaction) [RN:
R11018 ];
(1a) D-arginine + acceptor = iminoarginine + reduced acceptor [RN:
R11016 ];
(1b) iminoarginine + H2O = 5-guanidino-2-oxopentanoate + NH3 (spontaneous) [RN:
R11017 ]
Reaction(KEGG)
Substrate
Product
Comment
Contains a non-covalent FAD cofactor. The enzyme, which has been isolated from the bacterium Pseudomonas aeruginosa PAO1, forms with EC
1.4.1.25 , L-arginine dehydrogenase, a two-enzyme complex involved in the racemization of D- and L-arginine. The enzyme has a broad substrate range and can act on most D-amino acids with the exception of D-glutamate and D-aspartate. However, activity is maximal with D-arginine and D-lysine. Not active on glycine.
History
EC 1.4.99.6 created 1972 as EC 1.4.99.1, transferred 2015 to EC 1.4.99.6, modified 2017
Pathway
Orthology
K19746 D-arginine dehydrogenase
Genes
PAP : PSPA7_1242 PSPA7_2008
PPSE : BN5_1000(Ppsl_3554)
PCQ : PcP3B5_17690(soxA_1) PcP3B5_50450(soxA_3)
PMUI : G4G71_09095 G4G71_20780
PNT : G5B91_22535 G5B91_26040
PPAA : B7D75_05420 B7D75_09425
PPRC : PFLCHA0_c08160 PFLCHA0_c10630
PFE : PSF113_4743 PSF113_4854
PFO : Pfl01_0969 Pfl01_2315
PMUD : NCTC8068_02435 NCTC8068_04313
PBA : PSEBR_a4581 PSEBR_a4688
PDR : H681_16740 H681_19280
PALK : PSAKL28_08830 PSAKL28_17300
PSOS : POS17_0787 POS17_1041
PGY : AWU82_19035 AWU82_29055
PBZ : GN234_23560 GN234_24065
PSEP : C4K39_0794 C4K39_1053
PSHH : HU773_013545 HU773_022790
PTW : TUM18999_49980(dauA)
PZA : HU749_024090 HU749_024675
REH : H16_B1130(h16_B1130)
BTRM : SAMEA390648700389 SAMEA390648702048
DEL : DelCs14_0168 DelCs14_5711
DTS : BI380_20590 BI380_22575
DHK : BO996_02165 BO996_04170
DLA : I6G47_20530 I6G47_22535
OTD : J1M35_06175 J1M35_06215
LIM : L103DPR2_01068(lhgO_1)
URU : DSM104443_01419(dauA_2)
MLN : A9174_17330 A9174_30230
MHUA : MCHK_0585 MCHK_3415
MJR : EB229_17570 EB229_30830
MERD : EB233_14855 EB233_27035
MESO : BSQ44_03485 BSQ44_08185
AMIH : CO731_02274(soxA_2)
NIY : FQ775_03260 FQ775_08335
NOH : G5V57_06945 G5V57_31250
LAP : ACP90_00375 ACP90_22400
LABT : FIU93_00145(thiO) FIU93_05460(hcnC1)
LAGG : B0E33_05825 B0E33_11885
OAR : OA238_160p1280 OA238_c04930
SUAM : BOO69_14015 BOO69_20650
SULI : C1J05_07125 C1J05_17045
SMED : JNX03_12555 JNX03_17710 JNX03_19520
SINL : DSM14862_02067(dauA_2) DSM14862_03230(dauA_3)
SPSE : SULPSESMR1_00307(dauA)
RMM : ROSMUCSMR3_01932(dauA)
LVS : LOKVESSMR4R_02746(dauA)
PSHQ : F3W81_14375 F3W81_20400
THAS : C6Y53_03785 C6Y53_05020 C6Y53_10890
NOV : TQ38_006535 TQ38_020100
SMAG : AN936_07275 AN936_08975
SMAZ : LH19_07415 LH19_09035
SGI : SGRAN_1908 SGRAN_2687 SGRAN_3674(dauA)
SPHO : C3E99_05515 C3E99_09515 C3E99_13740
SPHD : HY78_00070 HY78_19420
SKR : BRX40_20240 BRX40_21710
SPLM : BXU08_08995 BXU08_16650
SPHC : CVN68_09715 CVN68_20120
SLUT : H9L13_06325 H9L13_09270
SLAN : GV829_00255 GV829_13505
SSAU : H8M03_01205 H8M03_01840
SCHY : GVO57_05645 GVO57_07670
SPPH : KFK14_07635 KFK14_15675
SFLA : SPHFLASMR4Y_00057(dauA)
SPZR : G5C33_04670 G5C33_05940
PALG : HFP57_05345 HFP57_07185
SMIC : SmB9_01240(dauA_1) SmB9_04240 SmB9_15660 SmB9_16330(dauA_2)
SPHS : ETR14_01540 ETR14_25785
ALH : G6N82_02340 G6N82_12425
EGN : BMF35_a0235 BMF35_a0579
EFV : CHH26_06105 CHH26_12475
QCI : NCF85_02175 NCF85_03770
ERK : CD351_05840 CD351_08730
ERR : DVR09_06090 DVR09_12050
EMV : HQR01_01655 HQR01_11700
PNS : A9D12_08635 A9D12_10900
PORL : BG023_111238 BG023_111694
PHZ : CHX26_06780 CHX26_09900
POT : E2E27_13225 E2E27_15815
SHUM : STHU_04150(dauA_1) STHU_07190(dauA_2) STHU_47910
SVC : STVA_05710(dauA_1) STVA_47980(dauA_2)
STEL : STAQ_40020(dauA_1) STAQ_40870(dauA_2)
NAO : Y958_15890 Y958_26370
HTQ : FRZ44_34250(dauA) FRZ44_42190(dauA)
HADH : FRZ61_33460(dauA) FRZ61_40360(dauA)
ECOG : FIV45_00605 FIV45_16535
MSAL : DSM43276_04562(hcnC)
MSAG : GCM10017556_12120(dauA)
» show all
Taxonomy
Reference
Authors
Tsukada K.
Title
D-amino acid dehydrogenases of Pseudomonas fluorescens.
Journal
J Biol Chem 241:4522-8 (1966)
Reference
Authors
Li C, Lu CD
Title
Arginine racemization by coupled catabolic and anabolic dehydrogenases.
Journal
Sequence
Reference
Authors
Fu G, Yuan H, Li C, Lu CD, Gadda G, Weber IT
Title
Conformational changes and substrate recognition in Pseudomonas aeruginosa D-arginine dehydrogenase.
Journal
Sequence
Reference
Authors
Yuan H, Fu G, Brooks PT, Weber I, Gadda G
Title
Steady-state kinetic mechanism and reductive half-reaction of D-arginine dehydrogenase from Pseudomonas aeruginosa.
Journal
Reference
Authors
Fu G, Yuan H, Wang S, Gadda G, Weber IT
Title
Atomic-resolution structure of an N5 flavin adduct in D-arginine dehydrogenase.
Journal
Sequence
Reference
Authors
Yuan H, Xin Y, Hamelberg D, Gadda G
Title
Insights on the mechanism of amine oxidation catalyzed by D-arginine dehydrogenase through pH and kinetic isotope effects.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 1.4.99.6
ExPASy - ENZYME nomenclature database: 1.4.99.6