KEGG   ENZYME: 1.4.99.6Help
Entry
EC 1.4.99.6                 Enzyme                                 

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
D-arginine [CPD:C00792];
acceptor [CPD:C00028];
H2O [CPD:C00001];
iminoarginine [CPD:C21026]
Product
5-guanidino-2-oxopentanoate [CPD:C03771];
NH3 [CPD:C00014];
reduced acceptor [CPD:C00030];
iminoarginine [CPD:C21026]
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
ec00472  D-Arginine and D-ornithine metabolism
ec01100  Metabolic pathways
Orthology
K19746  D-arginine dehydrogenase
Genes
DJI: CH75_22885
DJA: HY57_05670
LRZ: BJI69_19345
PAE: PA3863(dauA)
PAEV: N297_3989
PAEI: N296_3989
PAU: PA14_14010
PAP: PSPA7_1242 PSPA7_2008
PAG: PLES_11111
PAF: PAM18_1075
PAEP: PA1S_05505
PAEM: U769_05540
PAEL: T223_05455
PAEG: AI22_28110
PAEC: M802_3987
PAEO: M801_3855
PMY: Pmen_3567
PMK: MDS_3832
PPSE: BN5_1000(Ppsl_3554)
PCQ: PcP3B5_17690(soxA_1) PcP3B5_50450(soxA_3)
PPU: PP_2246(dauA)
PPF: Pput_3492
PPT: PPS_1856
PPI: YSA_01272
PPX: T1E_5405
PPUH: B479_09190
PPUN: PP4_35420
PPUD: DW66_2104
PMON: X969_07145
PMOT: X970_07120
PFL: PFL_0805
PFB: VO64_5501
PMAN: OU5_2436
PKC: PKB_0988
PSEM: TO66_05255
PANR: A7J50_2220
PSET: THL1_1154
PSIL: PMA3_04245
REH: H16_B1130(h16_B1130)
RME: Rmet_5086
BPT: Bpet0809
AMIM: MIM_c13060
AFQ: AFA_08995
RFR: Rfer_4053
POL: Bpro_1468
AAV: Aave_2431
AJS: Ajs_2247
AAA: Acav_2785
CTES: O987_28325
LIM: L103DPR2_01068(lhgO_1)
HSE: Hsero_4377(dadA)
RGE: RGE_37740
MLO: mll6667
AMIH: CO731_02274(soxA_2)
SHZ: shn_06905
RBM: TEF_10460
PSF: PSE_p0308
RMM: ROSMUCSMR3_01932(dauA)
ZMM: Zmob_1668
ZMB: ZZ6_1641
ZMI: ZCP4_1691
SPHP: LH20_10065
SPHM: G432_07455
STAX: MC45_05645
SPHI: TS85_02500
SSAN: NX02_04735
SPKC: KC8_11005
SSY: SLG_03600
SPHR: BSY17_2402
SINB: SIDU_02795
SPHT: K426_14930
SFLA: SPHFLASMR4Y_00057(dauA)
BLAS: BSY18_2122
AAY: WYH_01402(hcnC)
ANH: A6F65_02312(hcnC)
ADO: A6F68_02824(hcnC)
RCE: RC1_3715
TMO: TMO_1029
TXI: TH3_10910
MAGQ: MGMAQ_2448
MABB: MASS_4780
MABO: NF82_23725
MCHE: BB28_24110
MSTE: MSTE_04881
RHB: NY08_1989
RFA: A3L23_00322(hcnC_1)
RHS: A3Q41_03085(hcnC_2)
SRT: Srot_0241
PDX: Psed_2739
PSEE: FRP1_07110
PSEH: XF36_07930
MIN: Minf_1810(dadA)
 » show all
Taxonomy
Reference
1  [PMID:5925166]
  Authors
Tsukada K.
  Title
D-amino acid dehydrogenases of Pseudomonas fluorescens.
  Journal
J Biol Chem 241:4522-8 (1966)
Reference
2  [PMID:19139398]
  Authors
Li C, Lu CD
  Title
Arginine racemization by coupled catabolic and anabolic dehydrogenases.
  Journal
Proc Natl Acad Sci U S A 106:906-11 (2009)
DOI:10.1073/pnas.0808269106
  Sequence
[pae:PA3863]
Reference
3  [PMID:20809650]
  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
Biochemistry 49:8535-45 (2010)
DOI:10.1021/bi1005865
  Sequence
[pae:PA3863]
Reference
4  [PMID:20932054]
  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
Biochemistry 49:9542-50 (2010)
DOI:10.1021/bi101420w
Reference
5  [PMID:21707047]
  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
Biochemistry 50:6292-4 (2011)
DOI:10.1021/bi200831a
Reference
6  [PMID:21999550]
  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
J Am Chem Soc 133:18957-65 (2011)
DOI:10.1021/ja2082729
Other DBs
ExplorEnz - The Enzyme Database: 1.4.99.6
IUBMB Enzyme Nomenclature: 1.4.99.6
ExPASy - ENZYME nomenclature database: 1.4.99.6
BRENDA, the Enzyme Database: 1.4.99.6
CAS: 37205-44-0

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