KEGG   ENZYME: 4.1.2.42
Entry
EC 4.1.2.42                 Enzyme                                 
Name
D-threonine aldolase;
D-TA;
DTA;
low specificity D-TA;
low specificity D-threonine aldolase
Class
Lyases;
Carbon-carbon lyases;
Aldehyde-lyases
Sysname
D-threonine acetaldehyde-lyase (glycine-forming)
Reaction(IUBMB)
(1) D-threonine = glycine + acetaldehyde [RN:R08195];
(2) D-allothreonine = glycine + acetaldehyde [RN:R08196]
Reaction(KEGG)
R08195 R08196
Substrate
D-threonine [CPD:C00820];
D-allothreonine [CPD:C12317]
Product
glycine [CPD:C00037];
acetaldehyde [CPD:C00084]
Comment
A pyridoxal-phosphate protein that is activated by divalent metal cations (e.g. Co2+, Ni2+, Mn2+ or Mg2+) [1,2]. The reaction is reversible, which can lead to the interconversion of D-threonine and D-allothreonine [1]. Several other D-beta-hydroxy-alpha-amino acids, such as D-beta-phenylserine, D-beta-hydroxy-alpha-aminovaleric acid and D-beta-3,4-dihydroxyphenylserine, can also act as substrate [1].
History
EC 4.1.2.42 created 2007
Pathway
ec00470  D-Amino acid metabolism
ec01100  Metabolic pathways
Orthology
K19967  D-threonine aldolase
Genes
RPJN234_30730 N234_35660
CUHBJN34_31445
RMERmet_4194
CTIRALTA_B0772
CBWRR42_s1597
CGDCR3_3495
CCUPBKK81_29480
CUPBKK80_26875
CUUBKK79_32780
CPAUEHF44_19035
COXE0W60_02755
BYIBYI23_D007720
BUEBRPE67_DCDS09630
PPKU875_06500
PPNODA70_23570
PPNMLV28_07140
PRBX636_03075
PPULRO07_01255
PSPUNA29_10435
PAPISG18_01440
PVEUC34_17480
POXMB84_22255
PTXABW99_15240
PFGAB870_04515
PNRAT302_14610
PANDDRB87_16120
PFIBPI93_010510
BUOBRPE64_DCDS04080
BPEBP0453
BPCBPTD_0480
BPERBN118_0425
BPETB1917_3586
BPEUQ425_38740
BPARBN117_4500
BBHBN112_3472
BBRBB4953
BBMBN115_4610
BBXBBS798_4731
BPTBpet0041
BAVBAV3375
BHOD560_1496
BHMD558_1488
BHZACR54_04567
BTRMSAMEA390648701156
BBROBAU06_00460
BFZBAU07_00325
BPDZBBN53_00315
BOHAKI39_00870
BGMCAL15_00545
AXYAXYL_00071
AXONH44784_021281
AXNAX27061_0078
AXXERS451415_00076
ADTAPT56_00670
AISBUW96_26095
ASWCVS48_05695
ACHRC2U31_05340
ACHBDVB37_00340
ADYHLG70_21350
PUSCKA81_14160
ODIODI_R0236
BOZDBV39_05120
PACRFXN63_08015
PARKLSG25_15325
RHYRD110_05405
POLBpro_4092 Bpro_4819
PNAPnap_0513
AAVAave_4234
AJSAjs_0490
AAAAcav_4116
ACKC380_21305
ACRABSY15_1982
ACIDCBP33_02375
ACIPCBP36_02780
ACINCBP34_02340
ACISCBP35_16160
ACIOEAG14_19080
AMONH9L24_17945
VEIVeis_3378
DACDaci_4362
DELDelCs14_2466
DTSBI380_07650
DHKBO996_19575
DLAI6G47_02470
VPDVAPA_2c02520
CTTCtCNB1_4277
CTESO987_25450
CSERCCO03_16130
ADNAlide_0588
ADKAlide2_0553
RTARta_07170
OTOADJ79_06845
OTKC6570_00075
HYRBSY239_3490
HYBQ5W_00455
HYLLPB072_19995
HYCE5678_13770
HYNF9K07_04500
HTNKI616_23055
DPYBA022_12410
DIHG7047_19805
DRGH9K76_02520
DIADtpsy_0501
MPTMpe_A0329
METPC1M51_10865
HARHEAR2724
MMSmma_0025 mma_0441
XYKGT347_11700
PAUUE8A73_019985
KAIK32_06960
BRSS23_11060
BSYMCIT39_26400
BBETF8237_20440
RBKE0H22_18965
OCAOCAR_6698
OCGOCA5_c13700
OCOOCA4_c13700
TRBHB776_00695
BOPAXW83_16940
BOSBSY19_202
BVVBHK69_03930
BOIBLM15_26070
BOFFQV39_20585
MSLMsil_3403
FILBN1229_v1_3686
FIYBN1229_v1_3680
TSOIZ6_03930
RBMTEF_08225
KVLKVU_0190
KVUEIO_0640
SPHITS85_22560
SPLMBXU08_14985
SPHCCVN68_15690
RGIRGI145_05520
ROSCTJ15_11875
RMUCFOB66_07340
SHUMSTHU_29840
SVCSTVA_21010
HADHFRZ61_50040
GYUFE374_14720
STISthe_1797
LCREPla8534_12090
LPAVPLANPX_1609
DFEDfer_1026
DSNHWI92_05860
SINHLS482_21080
 » show all
Reference
1  [PMID:9346293]
  Authors
Kataoka M, Ikemi M, Morikawa T, Miyoshi T, Nishi K, Wada M, Yamada H, Shimizu S.
  Title
Isolation and characterization of D-threonine aldolase, a pyridoxal-5'-phosphate-dependent enzyme from Arthrobacter sp. DK-38.
  Journal
Eur J Biochem 248:385-93 (1997)
DOI:10.1111/j.1432-1033.1997.00385.x
  Sequence
Reference
2  [PMID:9642221]
  Authors
Liu JQ, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H
  Title
A novel metal-activated pyridoxal enzyme with a unique primary structure, low specificity D-threonine aldolase from Arthrobacter sp. Strain DK-38. Molecular cloning and cofactor characterization.
  Journal
J Biol Chem 273:16678-85 (1998)
DOI:10.1074/jbc.273.27.16678
  Sequence
Reference
3  [PMID:10390816]
  Authors
Liu JQ, Odani M, Dairi T, Itoh N, Shimizu S, Yamada H.
  Title
A new route to L-threo-3-[4-(methylthio)phenylserine], a key intermediate for the synthesis of antibiotics: recombinant low-specificity D-threonine aldolase-catalyzed stereospecific resolution.
  Journal
Appl Microbiol Biotechnol 51:586-91 (1999)
DOI:10.1007/s002530051436
Reference
4  [PMID:10952004]
  Authors
Liu JQ, Odani M, Yasuoka T, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H
  Title
Gene cloning and overproduction of low-specificity D-threonine aldolase from Alcaligenes xylosoxidans and its application for production of a key intermediate for parkinsonism drug.
  Journal
Appl Microbiol Biotechnol 54:44-51 (2000)
DOI:10.1007/s002539900301
  Sequence
Reference
5
  Authors
Liu, J.Q., Dairi, T., Itoh, N., Kataoka, M., Shimizu, S. and Yamada, H.
  Title
Diversity of microbial threonine aldolases and their application.
  Journal
J Mol Catal B 10:107-115 (2000)
Reference
6  [PMID:12686135]
  Authors
Paiardini A, Contestabile R, D'Aguanno S, Pascarella S, Bossa F.
  Title
Threonine aldolase and alanine racemase: novel examples of convergent evolution in the superfamily of vitamin B6-dependent enzymes.
  Journal
Biochim Biophys Acta 1647:214-9 (2003)
DOI:10.1016/S1570-9639(03)00050-5
Other DBs
ExplorEnz - The Enzyme Database: 4.1.2.42
IUBMB Enzyme Nomenclature: 4.1.2.42
ExPASy - ENZYME nomenclature database: 4.1.2.42
BRENDA, the Enzyme Database: 4.1.2.42

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