| Entry |
|
|---|
| Name |
D-amino-acid transaminase;
D-aspartate transaminase;
D-alanine aminotransferase;
D-aspartic aminotransferase;
D-alanine-D-glutamate transaminase;
D-alanine transaminase;
D-amino acid aminotransferase |
|---|
| Class |
Transferases;
Transferring nitrogenous groups;
Transaminases
 |
|---|
| Sysname |
D-alanine:2-oxoglutarate aminotransferase |
|---|
| Reaction(IUBMB) |
D-alanine + 2-oxoglutarate = pyruvate + D-glutamate [RN:R01148] |
|---|
| Reaction(KEGG) |
R01148;
(other) R01344 R01582 R02459 R02851 R02924 R05053
 |
|---|
| Substrate |
D-alanine [CPD:C00133];
2-oxoglutarate [CPD:C00026] |
|---|
| Product |
pyruvate [CPD:C00022];
D-glutamate [CPD:C00217] |
|---|
| Cofactor |
Pyridoxal phosphate [CPD:C00018] |
|---|
| Comment |
A pyridoxal-phosphate protein. The enzyme from thermophilic Bacillus
species acts on many D-amino acids with D-alanine and
D-2-aminobutyrate as the best amino donors. It can similarly use any
of several 2-oxo acids as amino acceptor, with 2-oxoglutarate and
2-oxobutyrate among the best. The enzyme from some other sources has
a broader specificity [6]. |
|---|
| Pathway |
PATH: ec00310 Lysine degradation
PATH: ec00330 Arginine and proline metabolism
PATH: ec00360 Phenylalanine metabolism
PATH: ec00472 D-Arginine and D-ornithine metabolism
PATH: ec00473 D-Alanine metabolism
PATH: ec01100 Metabolic pathways |
|---|
| Orthology |
KO: K00824 D-alanine transaminase |
|---|
| Genes |
ECA: ECA3117(dat)
PCT: PC1_2868
PWA: Pecwa_1405
PMR: PMI1701
DDA: Dd703_1218 Dd703_1465
DDC: Dd586_1307 Dd586_2840
DZE: Dd1591_1294 Dd1591_2788
PAT: Patl_4024
AMC: MADE_01083
LPN: lpg1510
LPF: lpl1516(ala)
LPP: lpp1467(ala)
LPC: LPC_0929(ala)
MCA: MCA0106
TCX: Tcr_1636
NOC: Noc_2631
AEH: Mlg_0177
HHA: Hhal_1013
TGR: Tgr7_2706
HNA: Hneap_1266
ABO: ABO_1960(dat)
TAU: Tola_0563
RMA: Rmag_0469
VOK: COSY_0432
KKO: Kkor_0334
RSO: RS01735(RSp0714)
RPI: Rpic_4521
RPF: Rpic12D_4653
REU: Reut_A2225
REH: H16_A2521(dat)
RME: Rmet_2249
CTI: RALTA_A2024
BMA: BMA0057
BMV: BMASAVP1_A0223
BML: BMA10229_A1370
BMN: BMA10247_3191
BPS: BPSL0409
BPM: BURPS1710b_0621
BPL: BURPS1106A_0459
BPD: BURPS668_0439
BPR: GBP346_A0367
BTE: BTH_I0381
BVI: Bcep1808_2988
BUR: Bcep18194_A6235
BCN: Bcen_2277
BCH: Bcen2424_2892
BCM: Bcenmc03_2902
BCJ: BCAL0705
BAM: Bamb_2942
BAC: BamMC406_2804
BMU: Bmul_0412
BMJ: BMULJ_02843(dat)
BXE: Bxe_A4217
BPY: Bphyt_0499
BGL: bglu_1g32080
BPE: BP0103 BP0769
BPA: BPP0167 BPP0330
BBR: BB0169 BB0333
BPT: Bpet4806
BAV: BAV0136(dat)
RFR: Rfer_1037 Rfer_1546
POL: Bpro_0317
PNA: Pnap_0246
VAP: Vapar_4878
MPT: Mpe_A0312
HAR: HEAR3000(dat)
MMS: mma_3249(dat)
LCH: Lcho_4238
NEU: NE1486
NET: Neut_0760
NMU: Nmul_A1990
EBA: ebA3046
AZO: azo0181(daaA)
DAR: Daro_0290
TBD: Tbd_0267
MFA: Mfla_2498
MEI: Msip34_2540
CFF: CFF8240_0563
CCV: CCV52592_1852
CHA: CHAB381_1083
CCO: CCC13826_1079
CLA: Cla_1171
SDL: Sdel_1210
DSA: Desal_1397
DRT: Dret_1208
DAT: HRM2_21590(dat)
MLO: mlr0401
MES: Meso_1614 Meso_2359
PLA: Plav_3125
SME: SMa0093 SMc01047
SMD: Smed_1094 Smed_5171
ATU: Atu2511(dat) Atu5473(dat)
ATC: AGR_C_4563 AGR_pAT_698
ARA: Arad_2269(dat) Arad_7091(dat)
AVI: Avi_5914(dat)
RET: RHE_CH01953(ypch00632)
REC: RHECIAT_CH0002065
RLE: RL2283
RLT: Rleg2_1631
RLG: Rleg_0536 Rleg_1818
RHI: NGR_c13000
BME: BMEII0363
BMI: BMEA_B0918
BMF: BAB2_0301
BMB: BruAb2_0299
BMC: BAbS19_II02850
BMS: BRA0934
BMT: BSUIS_B0927
BOV: BOV_A0876
BCS: BCAN_B0954(dat)
BMR: BMI_II928
OAN: Oant_1427 Oant_3562 Oant_4609
BJA: bll7596
BRA: BRADO6144
BBT: BBta_1647
RPA: RPA2596
RPB: RPB_2879
RPC: RPC_2581
RPD: RPD_2593
RPE: RPE_2761
RPT: Rpal_2866
NWI: Nwi_1448
NHA: Nham_1840
OCA: OCAR_6099
XAU: Xaut_4394
AZC: AZC_1963
MEX: Mext_0997
MEA: Mex_1p0774
MDI: METDI1145
MRD: Mrad2831_5636
MET: M446_6843
MPO: Mpop_0938
MCH: Mchl_0960
MNO: Mnod_7579
BID: Bind_1524
MSL: Msil_0534
CCR: CC_1744
CCS: CCNA_01818
CAK: Caul_2609
PZU: PHZ_c1727
SIL: SPO3604
SIT: TM1040_3168
RSP: RSP_1768 RSP_3455
RSH: Rsph17029_0414 Rsph17029_3100
RSQ: Rsph17025_2484
RSK: RSKD131_0068 RSKD131_3621
JAN: Jann_0363
RDE: RD1_1004(dat)
PDE: Pden_0798 Pden_3425
DSH: Dshi_3150(dat)
MMR: Mmar10_1447
HNE: HNE_3117
GBE: GbCGDNIH1_1121
ACR: Acry_2552
RRU: Rru_A1682
RCE: RC1_0133
BSU: BSU09670(dat)
BHA: BH2811
BAN: BA2256(dat-1) BA5472(dat-2)
BAR: GBAA2256(dat-1) GBAA5472(dat-2)
BAA: BA_2758
BAT: BAS2100 BAS5082
BAH: BAMEG_2340(dat1) BAMEG_5518(dat2)
BAI: BAA_2318(dat1) BAA_5498(dat2)
BCE: BC2209 BC5233
BCA: BCE_2285(dat) BCE_5351(dat)
BCZ: BCZK2037(daaA) BCZK4929(dat)
BCR: BCAH187_A2366(dat1) BCAH187_A5405(dat2)
BCB: BCB4264_A2238(dat1) BCB4264_A5356(dat2)
BCU: BCAH820_2281(dat1) BCAH820_5323(dat2)
BCG: BCG9842_B3086(dat1) BCG9842_B5604(dat2)
BCQ: BCQ_2192(dat) BCQ_5062(dat)
BCX: BCA_2339(dat1) BCA_5371(dat2)
BCY: Bcer98_1655 Bcer98_3767
BTK: BT9727_2039(daaA) BT9727_4914(dat)
BTL: BALH_2017(daaA) BALH_4731(dat)
BWE: BcerKBAB4_2079 BcerKBAB4_5026
BLI: BL02875(dat)
BLD: BLi01040(dat)
BCL: ABC2489(dat)
BAY: RBAM_009900(dat)
BPU: BPUM_0916(dat)
OIH: OB1083(daaA)
GKA: GK0672
GTN: GTNG_0579
GWC: GWCH70_0660
GYC: GYMC61_1476
SAU: SA1571
SAV: SAV1750
SAW: SAHV_1736
SAM: MW1693
SAR: SAR1835(dat)
SAS: SAS1676
SAC: SACOL1800(dat)
SAB: SAB1610c(dat)
SAA: SAUSA300_1696(dat)
SAX: USA300HOU_1741(daaA)
SAO: SAOUHSC_01867
SAJ: SaurJH9_1805
SAH: SaurJH1_1840
SAE: NWMN_1643
SAD: SAAV_1760(dat)
SEP: SE1423
SER: SERP1309(dat)
SHA: SH1172(dat)
SSP: SSP1013
SCA: Sca_1357(dat)
LMO: lmo1619(daaA)
LMF: LMOf2365_1641(dat)
LMH: LMHCC_0944(dat)
LMC: Lm4b_01630(daaA)
LIN: lin1660(daaA)
LWE: lwe1635(dat)
LSP: Bsph_4219
BBE: BBR47_23020(dat)
AAC: Aaci_1015
LSL: LSL_1670
CAC: CAC0792
CBE: Cbei_2762
STH: STH1330
VPR: Vpar_0421
DSY: DSY3261
DHD: Dhaf_4429
NTH: Nther_0630
SRU: SRU_0542
DFE: Dfer_3559
PHE: Phep_2045
RBI: RB2501_10712
GAU: GAU_2719
KOL: Kole_0085
 |
|---|
| Structures |
PDB: 1A0G 1DAA 1G2W 2DAA 2DAB 3DAA 4DAA 5DAA |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:14367287]
THORNE CB, GOMEZ CG, HOUSEWRIGHT RD.
Transamination of D-amino acids by Bacillus subtilis.
J. Bacteriol. 69 (1955) 357-62.
Bacillus subtilis [GN:bsu] |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:13263311]
THORNE CB, MOLNAR DM.
D-Amino acid transamination in bacillus anthracis.
J. Bacteriol. 70 (1955) 420-6.
Bacillus anthracis |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:4953710]
Martinez-Carrion M, Jenkins WT.
D-Alanine-D-glutamate transaminase. I. Purification and
characterization.
J. Biol. Chem. 240 (1965) 3538-46.
Bacillus subtilis [GN:bsu] |
|---|
Reference
Authors
Title
Journal
Organism
|
4 [PMID:4710577]
Ogawa T, Fukuda M, Sasaoka K.
Occurrence of D-amino acid aminotransferase in pea seedlings.
Biochem. Biophys. Res. Commun. 52 (1973) 998-1002.
Pisum sativum |
|---|
Reference
Authors
Title
Journal
Organism
|
5 [PMID:1158891]
Yonaha K, Misono H, Yamamoto T, Soda K.
D-amino acid aminotransferase of Bacillus sphaericus. Enzymologic
and spectrometric properties.
J. Biol. Chem. 250 (1975) 6983-9.
Bacillus sphaericus |
|---|
Reference
Authors
Title
Journal
Organism
|
6 [PMID:2914916]
Tanizawa K, Masu Y, Asano S, Tanaka H, Soda K.
Thermostable D-amino acid aminotransferase from a thermophilic
Bacillus species. Purification, characterization, and active site
sequence determination.
J. Biol. Chem. 264 (1989) 2445-9.
Bacillus sphaericus, Bacillus sp. |
|---|
Reference
Authors
Title
Journal
Organism
|
7 [PMID:9696787]
Fotheringham IG, Bledig SA, Taylor PP.
Characterization of the genes encoding D-amino acid transaminase and
glutamate racemase, two D-glutamate biosynthetic enzymes of Bacillus
sphaericus ATCC 10208.
J. Bacteriol. 180 (1998) 4319-23.
Bacillus sphaericus |
|---|
Reference
Authors
Title
Journal
|
8 [PMID:9485439]
van Ophem PW, Erickson SD, Martinez del Pozo A, Haller I, Chait BT,
Yoshimura T, Soda K, Ringe D, Petsko G, Manning JM.
Substrate inhibition of D-amino acid transaminase and protection by
salts and by reduced nicotinamide adenine dinucleotide: isolation
and initial characterization of a pyridoxo intermediate related to
inactivation.
Biochemistry. 37 (1998) 2879-88. |
|---|
Reference
Authors
Title
Journal
Organism
|
9 [PMID:7626635]
Sugio S, Petsko GA, Manning JM, Soda K, Ringe D.
Crystal structure of a D-amino acid aminotransferase: how the
protein controls stereoselectivity.
Biochemistry. 34 (1995) 9661-9.
Bacillus sphaericus, Bacillus sp. |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 2.6.1.21
IUBMB Enzyme Nomenclature: 2.6.1.21
ExPASy - ENZYME nomenclature database: 2.6.1.21
BRENDA, the Enzyme Database: 2.6.1.21
CAS: 37277-85-3 |
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