KEGG ENZYME: 4.1.2.42

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-allo-threonine = glycine + acetaldehyde [RN:R08196]

Reaction(KEGG)

R08195 R08196

Substrate

D-threonine [CPD:C00820];
D-allo-threonine [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-allo-threonine [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

VNP:	KW548_20795

TFT:	RI844_10130

CKS:	H9L41_12085

RPJ:	N234_30730 N234_35660

CUH:	BJN34_31445

RME:

Rmet_4194

CTI:	RALTA_B0772

CBW:	RR42_s1597

CGD:

CR3_3495

CCUP:

BKK81_29480

CUP:	BKK80_26875

CUU:	BKK79_32780

CPAU:

EHF44_19035

COX:	E0W60_02755

CCAM:

M5D45_21590

CCAX:

KZ686_16900

CUK:	KB879_11540

CNAN:

A2G96_27930

CUPR:

IC580_18170

CUPE:

KLP38_19490

CUPP:

CTP10_R19070 CTP10_R53460

BYI:	BYI23_D007720

BURT:

BTHE68_68360

PPAI:

E1956_40530

PPK:	U875_06500

PPNO:

DA70_23570

PPNM:

LV28_07140

PRB:	X636_03075

PPUL:

RO07_01255

PSPU:

NA29_10435

PAPI:

SG18_01440

PVE:	UC34_17480

POX:	MB84_22255

PTX:	ABW99_15240

PFG:	AB870_04515

PNR:	AT302_14610

PAND:

DRB87_16120

PFIB:

PI93_010510

PCOM:

NTU39_19190

PANN:

PanNE5_27420

PANX:

OYT13_17630

BUO:	BRPE64_DCDS04080

CABK:

NK8_60290

BUE:	BRPE67_DCDS09630

BPE:

BP0453

BPC:

BPTD_0480

BPER:

BN118_0425

BPET:

B1917_3586

BPEU:

Q425_38740

BPAR:

BN117_4500

BBH:	BN112_3472

BBR:

BB4953

BBM:	BN115_4610

BBX:	BBS798_4731

BPT:

Bpet0041

BAV:

BAV3375

BHO:

D560_1496

BHM:

D558_1488

BHZ:	ACR54_04567

BTRM:

SAMEA390648701156

BBRO:

BAU06_00460

BFZ:	BAU07_00325

BPDZ:

BBN53_00315

BOH:	AKI39_00870

BGM:	CAL15_00545

BGV:	CAL12_00475

AXY:	AXYL_00071

AXO:	NH44784_021281

AXN:	AX27061_0078

AXX:	ERS451415_00076

ADT:	APT56_00670

AIS:	BUW96_26095

ASW:	CVS48_05695

ACHR:

C2U31_05340

ACHB:

DVB37_00340

ADY:	HLG70_21350

ACHO:

H4P35_00325

AMUI:

PE062_24190

APES:

FOC84_12460

AAEG:

RA224_00275

ASEL:

RAS12_21380

ACHM:

V6V88_00325

ACHA:

KYT87_00345

AVH:	WHX56_05135

ACHH:

ABFG95_15240

ACHJ:

LN047_00360

PUS:	CKA81_14160

POLL:

OEG81_00330

ODI:

ODI_R0236

BOZ:	DBV39_05120

ODH:	DHf2319_07815

PACR:

FXN63_08015

PARK:

LSG25_15325

RHY:	RD110_05405

RHOB:

HTY51_00710

POL:	Bpro_4092 Bpro_4819

PNA:

Pnap_0513

POS:	DT070_09565

POO:	F7R28_21060

AJS:

Ajs_0490

ACK:	C380_21305

ACRA:

BSY15_1982

ACID:

CBP33_02375

ACIP:

CBP36_02780

ACIN:

CBP34_02340

ACIS:

CBP35_16160

ACIO:

EAG14_19080

ARAD:

KI609_02995

ACIQ:

ACDW_06530

ACIV:

EXV95_20140

ASAH:

AVXHC19_42690

AAV:

Aave_4234

AAA:

Acav_4116

AMON:

H9L24_17945

VEI:

Veis_3378

DAC:

Daci_4362

DEL:	DelCs14_2466

DTS:	BI380_07650

DHK:	BO996_19575

DLA:	I6G47_02470

VPD:	VAPA_2c02520

CTT:	CtCNB1_4277

CTES:

O987_25450

CSER:

CCO03_16130

CTEZ:

CT3_33100

CRJ:	QMY55_21200

ADN:	Alide_0588

ADK:	Alide2_0553

RTA:

Rta_07170

RTEA:

HK414_23300

OTO:	ADJ79_06845

OTK:	C6570_00075

OTD:	J1M35_17650

HYR:	BSY239_3490

HYB:

Q5W_00455

HYL:	LPB072_19995

HYC:	E5678_13770

HYN:	F9K07_04500

HTN:	KI616_23055

HCZ:	G9Q37_19500

HYY:	JNX00_03190

HYDR:

SOM08_02600

HYDA:

ABSY19_10525

DPY:	BA022_12410

DIH:	G7047_19805

DRG:	H9K76_02520

DIJ:	HND92_02885

DIM:	K2L43_02625

DIS:	I3K84_10605

DIA:	Dtpsy_0501

MPT:

Mpe_A0329

METP:

C1M51_10865

PAIS:

PFX98_00835

ATER:

MW290_10710

HAR:

HEAR2724

MMS:	mma_0025 mma_0441

XYK:	GT347_11700

XYG:	R9X41_20185

CHEA:

PVE73_27450

BRS:

S23_11060

BSYM:

CIT39_26400

BBET:

F8237_20440

OCA:

OCAR_6698

OCG:	OCA5_c13700

OCO:	OCA4_c13700

PCAX:

AFIC_002179

BVV:	BHK69_03930

BVES:

QO058_09840

BOP:	AXW83_16940

BOS:

BSY19_202

BOI:	BLM15_26070

BOF:	FQV39_20585

BOW:	NWE53_17855

BOSE:

RMR04_31555

AZC:

AZC_0733

AQI:	J5J86_00435

FIL:	BN1229_v1_3686

FIY:	BN1229_v1_3680

TSO:

IZ6_03930

RBM:

TEF_08225

KVL:

KVU_0190

KVU:

EIO_0640

RGI:	RGI145_05520

ROS:	CTJ15_11875

RMUC:

FOB66_07340

RMT:	IAI58_16675

RFL:

Rmf_36800

RCV:	PFY06_14595

SRF:	LHU95_00415

ELIO:

KO353_11595

SHUM:

STHU_29840

SVC:	STVA_21010

STEL:

STAQ_26460

HTQ:	FRZ44_51590

HADH:

FRZ61_50040

THAR:

T8K17_02005

STI:

Sthe_1797

MTAR:

DF168_00796

LPAV:

PLANPX_1609

LLH:

I41_15830

SCHL:

QJS52_11520

» 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

[ag:BAA31547]

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

[ag:BAA31547]

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

[axy:AXYL_00071]

Reference

Authors

Liu JQ, Dairi T, Itoh N, Kataoka M, Shimizu S, 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

All links

Gene (77)   
   MGENES (77)   
Protein sequence (611)   
   UniProt (602)   
   SWISS-PROT (1)   
   PDBSTR (8)   
DNA sequence (821)   
   GenBank (413)   
   EMBL (408)   
3D Structure (3)   
   PDB (3)   
Protein domain (5)   
   InterPro (5)   
All databases (1517)   

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