Entry
Name
aspartate dehydrogenase;
AspDH;
NAD-dependent aspartate dehydrogenase;
NADH2-dependent aspartate dehydrogenase;
NADP+-dependent aspartate dehydrogenase;
nadX (gene name);
L-aspartate:NAD(P)+ oxidoreductase (deaminating)
Class
Oxidoreductases;
Acting on the CH-NH2 group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
L-aspartate:NAD(P)+ oxidoreductase (2-iminosuccinate-forming)
Reaction(IUBMB)
L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H + H+ (overall reaction) [RN:
R07164 R07165 ];
(1a) L-aspartate + NAD(P)+ = 2-iminosuccinate + NAD(P)H + H+ [RN:
R07407 R07410 ];
(1b) 2-iminosuccinate + H2O = oxaloacetate + NH3 (spontaneous) [RN:
R13023 ]
Reaction(KEGG)
Substrate
Product
Comment
The enzyme is strictly specific for L-aspartate as substrate. It produces the unstable compound 2-iminosuccinate, which, in the presence of water, hydrolyses spontaneously to form oxaloacetate. The enzyme from some archaea and thermophilic bacteria is likely to transfer 2-iminosuccinate directly to EC
2.5.1.72 , quinolinate synthase, preventing its hydrolysis and enabling the de novo biosynthesis of NAD+.
History
EC 1.4.1.21 created 2005, modified 2022
Pathway
ec00760 Nicotinate and nicotinamide metabolism
Orthology
K06989 aspartate dehydrogenase
Genes
ACYG : 125181371 136788652
RTEM : 120920150 120921221
SRX : 107731187 107736706 107754162
SGH : 107560744 107567544(aspdh)
MASI : 127450503 127451774
SASA : 106591495 106601950 106606414
STRU : 115171859 115207644
OMY : 110487448(aspdh) 110511852
CCLU : 121551577 123482639
ARUT : 117970905 117970906
AFRA : 136039865 136039869
PPOI : 119109680 119110711
PTEP : 107452582 107452803
CEL : CELE_F17C8.9(F17C8.9)
MFOO : 137977017 137977020
EHX : EMIHUDRAFT_199949 EMIHUDRAFT_214926
RTG : NCTC13098_01033(nadX)
SFJ : SAMEA4384070_4073(nadX)
SOF : NCTC11214_02673(nadX)
LRI : NCTC12151_00054(nadX)
PMUD : NCTC8068_05350(nadX)
ABK : LX00_04805 LX00_09365
ABAU : IX87_00755 IX87_20070
GAI : IMCC3135_20465(nadX)
REH : H16_B0736(h16_B0736)
BMEC : WJ16_10170 WJ16_27970
BUE : BRPE67_CCDS00790(nadX)
BPX : BUPH_01292 BUPH_08279
PTER : C2L65_29265 C2L65_45115
PDIO : PDMSB3_3298.1(nadX)
PBRY : NDK50_07380 NDK50_21560
PSAA : QEN71_16940 QEN71_41325
PPAI : E1956_21805 E1956_41210
PAPI : SG18_13665 SG18_14690
PNR : AT302_01085 AT302_13325
PFIB : PI93_011780 PI93_022255
CABA : SBC2_52700(nadX_1) SBC2_81260(nadX_2)
CABK : NK8_77000 NK8_82050
BPER : BN118_0921 BN118_3500
BPET : B1917_1714 B1917_3487
BPEU : Q425_14660 Q425_35820
BPAR : BN117_0255 BN117_1450 BN117_4327
BBH : BN112_1768 BN112_3157 BN112_3641
BBR : BB0260 BB1747 BB4781
BBM : BN115_0245 BN115_1649 BN115_4458
BBX : BBS798_0255 BBS798_1648 BBS798_4557
BTRM : SAMEA390648704134(nadX)
BFZ : BAU07_03915 BAU07_23965
BOH : AKI39_14235 AKI39_22760
BOJ : CBF45_01120 CBF45_08870
BGV : CAL12_15670 CAL12_20595
AXX : ERS451415_04045(nadX)
ASW : CVS48_06345 CVS48_22910
ASEL : RAS12_02135 RAS12_22080
AVH : WHX56_15270 WHX56_24220
PIG : EGT29_00760 EGT29_02180 EGT29_16640
KGY : EHF36_01305 EHF36_08995
VBO : CKY39_14770 CKY39_21980
HYN : F9K07_11735 F9K07_22040
BBAY : A4V04_03390 A4V04_09290
NKI : KW403_11300 KW403_13255
AVV : RvVAT039_pl06520(nadX)
RHR : CKA34_28130 CKA34_28995
NEN : NCHU2750_42570(nadX) NCHU2750_43420(nadX) NCHU2750_48250
VGO : GJW-30_1_01281(nadX)
BOF : FQV39_24550 FQV39_24895 FQV39_30835
STAR : G3545_20370 G3545_23200
APRA : G3A50_09690 G3A50_21125
RHZ : RHPLAN_08010 RHPLAN_32260 RHPLAN_59480
PSIN : CAK95_26410 CAK95_27285
SIW : GH266_03965 GH266_08205 GH266_14850
PSTG : E8M01_01690 E8M01_20925
PAQT : E8L99_12615 E8L99_13005
ACUT : MRB58_19230 MRB58_21810
RMM : ROSMUCSMR3_01810(nadX)
AHT : ANTHELSMS3_02149(nadX)
TSCO : R1T40_19610 R1T40_21765
SMAG : AN936_00625 AN936_00695
SMAZ : LH19_00635 LH19_00705
RMT : IAI58_13860 IAI58_15960
RCV : PFY06_07640 PFY06_19500
SHUM : STHU_23560(nadX_1) STHU_30900(nadX_2) STHU_46520(nadX_3) STHU_50980
SVC : STVA_25120(nadX_1) STVA_32060(nadX_2) STVA_49620(nadX_3) STVA_50890
STEL : STAQ_02140(nadX_1) STAQ_21260(nadX_2) STAQ_28410(nadX_3) STAQ_46150
NCB : C0V82_23335 C0V82_23365
THAR : T8K17_16820 T8K17_24330
GSO : PH603_12325 PH603_12365
BCEL : BcellWH2_00602(nadX)
BFD : NCTC4823_03477(nadX)
BON : A361_11420 A361_14270
CFIR : NAF01_10275(nadX) NAF01_13180(nadX)
CPSS : M5V91_06990(nadX) M5V91_10090
NCM : QNK12_10895(nadX) QNK12_17685(nadX)
BCHS : JNE38_06190(nadX) JNE38_24415(nadX)
SPAE : E2C16_03295(nadX) E2C16_12085(nadX)
ETM : CE91St48_00690 CE91St48_00890
PIV : NCTC13079_01117(nadX)
RPY : Y013_10970 Y013_15090
AMAU : DSM26151_04230(nadX)
PSEV : USB125703_00894(nadX)
ACIT : HPK19_12845 HPK19_19970(nadX)
BALA : DSM104299_00965(nadX)
MEB : Abm4_0406(nadX1) Abm4_1625(nadX2)
MEW : MSWAN_0861 MSWAN_1954
MCUB : MCBB_0898(nadX_1) MCBB_1882(nadX_3)
METN : BK008_02555 BK008_07220
MFEG : GCM10025860_01240 GCM10025860_11570
SRUB : C2R22_03390 C2R22_21805
» show all
Taxonomy
Reference
1
Authors
Kretovich WL, Kariakina TI, Weinova MK, Sidelnikova LI, Kazakova OW.
Title
The synthesis of aspartic acid in Rhizobium lupini bacteroids.
Journal
Plant Soil 61:145-156 (1981)
Reference
Authors
Okamura T, Noda H, Fukuda S, Ohsugi M.
Title
Aspartate dehydrogenase in vitamin B12-producing Klebsiella pneumoniae IFO 13541.
Journal
Reference
Authors
Yang Z, Savchenko A, Yakunin A, Zhang R, Edwards A, Arrowsmith C, Tong L
Title
Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643.
Journal
Sequence
Reference
Authors
Yoneda K, Kawakami R, Tagashira Y, Sakuraba H, Goda S, Ohshima T.
Title
The first archaeal L-aspartate dehydrogenase from the hyperthermophile Archaeoglobus fulgidus: gene cloning and enzymological characterization.
Journal
Sequence
Reference
Authors
Yoneda K, Sakuraba H, Tsuge H, Katunuma N, Ohshima T.
Title
Crystal structure of archaeal highly thermostable L-aspartate dehydrogenase/NAD/citrate ternary complex.
Journal
Sequence
Reference
Authors
Li Y, Kawakami N, Ogola HJ, Ashida H, Ishikawa T, Shibata H, Sawa Y.
Title
A novel L-aspartate dehydrogenase from the mesophilic bacterium Pseudomonas aeruginosa PAO1: molecular characterization and application for L-aspartate production.
Journal
Sequence
Reference
Authors
Li Y, Ishida M, Ashida H, Ishikawa T, Shibata H, Sawa Y.
Title
A non-NadB type L-aspartate dehydrogenase from Ralstonia eutropha strain JMP134: molecular characterization and physiological functions.
Journal
Sequence
Reference
Authors
Li Y, Ogola HJ, Sawa Y.
Title
L-aspartate dehydrogenase: features and applications.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 1.4.1.21
ExPASy - ENZYME nomenclature database: 1.4.1.21